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Collagen Structure
Published by Anonymous on 2007/9/22 (3305 reads)
1: ScientificWorldJournal. 2007 Mar 30;7:404-20.


Collagen structure of tendon relates to function.

Franchi M, Trirè A, Quaranta M, Orsini E, Ottani V.

Department of Human Anatomical Sciences and Physiopathology of Locomotor Apparatus, University of Bologna, Bologna, Italy. marco.franchi3@unibo.it

A tendon is a tough band of fibrous connective tissue that connects muscle to bone, designed to transmit forces and withstand tension during muscle contraction. Tendon may be surrounded by different structures: 1) fibrous sheaths or retinaculae; 2) reflection pulleys; 3) synovial sheaths; 4) peritendon sheaths; 5) tendon bursae. Tendons contain a) few cells, mostly represented by tenoblasts along with endothelial cells and some chondrocytes; b) proteoglycans (PGs), mainly decorin and hyaluronan, and c) collagen, mostly type I. Tendon is a good example of a high ordered extracellular matrix in which collagen molecules assemble into filamentous collagen fibrils (formed by microfibrils) which aggregate to form collagen fibers, the main structural components. It represents a multihierarchical structure as it contains collagen molecules arranged in fibrils then grouped in fibril bundles, fascicles and fiber bundles that are almost parallel to the long axis of the tendon, named as primary, secondary and tertiary bundles. Collagen fibrils in tendons show prevalently large diameter, a D-period of about 67 nm and appear built of collagen molecules lying at a slight angle (< 5 degrees). Under polarized light microscopy the collagen fiber bundles appear crimped with alternative dark and light transverse bands. In recent studies tendon crimps observed via SEM and TEM show that the single collagen fibrils suddenly changing their direction contain knots. These knots of collagen fibrils inside each tendon crimp have been termed "fibrillar crimps", and even if they show different aspects they all may fulfil the same functional role. As integral component of musculoskeletal system, the tendon acts to transmit muscle forces to the skeletal system. There is no complete understanding of the mechanisms in transmitting/absorbing tensional forces within the tendon; however it seems likely that a flattening of tendon crimps may occur at a first stage of tendon stretching. Increasing stretching, other transmission mechanisms such as an interfibrillar coupling via PGs linkages and a molecular gliding within the fibrils structure may be involved.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 17450305 [PubMed - indexed for MEDLINE]

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2: J Magn Reson Imaging. 2007 Feb;25(2):345-61.


Collagen structure: the molecular source of the tendon magic angle effect.

Fullerton GD, Rahal A.

Radiology Department, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229, USA. fullerton@uthscsa.edu

This review of tendon/collagen structure shows that the orientational variation in MRI signals from tendon, which is referred to as the "magic angle" (MA) effect, is caused by irreducible separation of charges on the main chain of the collagen molecule. These charges are held apart in a vacuum by stereotactic restriction of protein folding due in large part to a high concentration of hydroxyproline ring residues in the amino acids of mammalian collagen. The elevated protein electrostatic energy is reduced in water by the large dielectric constant of the highly polar solvent (kappa approximately 80). The water molecules serve as dielectric molecules that are bound by an energy that is nearly equivalent to the electrostatic energy between the neighboring positive and negative charge pairs in a vacuum. These highly immobilized water molecules and secondary molecules in the hydrogen-bonded water network are confined to the transverse plane of the tendon. Orientational restriction causes residual dipole coupling, which is directly responsible for the frequency and phase shifts observed in orientational MRI (OMRI) described by the MA effect. Reference to a wide range of biophysical measurements shows that native hydration is a monolayer on collagen h(m) = 1.6 g/g, which divides into two components consisting of primary hydration on polar surfaces h(pp) = 0.8 g/g and secondary hydration h(s) = 0.8 g/g bridging over hydrophobic surface regions. Primary hydration further divides into side-chain hydration h(psc) = 0.54 g/g and main-chain hydration h(pmc) = 0.263 g/g. The main-chain fraction consists of water that bridges between charges on the main chain and is responsible for almost all of the enthalpy of melting DeltaH = 70 J/g-dry mass. Main-chain water bridges consist of one extremely immobilized Ramachandran water bridge per tripeptide h(Ra) = 0.0658 g/g and one double water bridge per tripeptide h(dwb) = 0.1974 g/g, with three water molecules that are sufficiently slowed to act as the spin-lattice relaxation sink for the entire tendon. (c) 2007 Wiley-Liss, Inc.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 17260393 [PubMed - indexed for MEDLINE]

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3: Clin Calcium. 2006 Jun;16(6):971-76.


[Bone and bone related biochemical examinations. Bone and collagen related metabolites. Structure and metabolisms of collagen]

[Article in Japanese]

Hosoi T.

National Center for Geriatrics and Gerontology, Department of Advanced Medicine.

Collagens are the most abundant proteins in mammals. They are the major structural proteins in bone as well as other organs. The synthesis of collagens is regulated by numerous growth factors, cytokines and hormones. The higher structure of collagen is derived from the series of biosynthesis including its characteristic primary amino acid structure and post-translational modifications. The degradation products of collagen have been utilized as markers for bone turnover.

Publication Types:
English Abstract
Review

PMID: 16751693 [PubMed - indexed for MEDLINE]

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4: Curr Top Dev Biol. 2006;72:205-36.


Regulation of hepatocyte cell cycle progression and differentiation by type I collagen structure.

Hansen LK, Wilhelm J, Fassett JT.

Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, Minnesota 55455, USA.

Cell behavior is strongly influenced by the extracellular matrix (ECM) to which cells adhere. Both chemical determinants within ECM molecules and mechanical properties of the ECM network regulate cellular response, including proliferation, differentiation, and apoptosis. Type I collagen is the most abundant ECM protein in the body with a complex structure that can be altered in vivo by proteolysis, cross-linking, and other processes. Because of collagen's complex and dynamic nature, it is important to define the changes in cell response to different collagen structures and its underlying mechanisms. This chapter reviews current knowledge of potential mechanisms by which type I collagen affects cell behavior, and it presents data that elucidate specific intracellular signaling pathways by which changes in type I collagen structure differentially regulate hepatocyte cell cycle progression and differentiation. A network of polymerized fibrillar type I collagen (collagen gel) induces a highly differentiated but growth-arrested phenotype in primary hepatocytes, whereas a film of monomeric collagen adsorbed to a rigid dish promotes cell cycle progression and dedifferentiation. Studies presented here demonstrate that protein kinase A (PKA) activity is significantly elevated in hepatocytes on type I collagen gel relative to collagen film, and inhibition of this elevated PKA activity can promote hepatocyte cell cycle progression on collagen gel. Additional studies are presented that examine changes in hepatocyte cell cycle progression and differentiation in response to increased rigidity of polymerized collagen gel by fiber cross-linking. Potential mechanisms underlying these cellular responses and their implications are discussed.

Publication Types:
Review

PMID: 16564336 [PubMed - indexed for MEDLINE]

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5: Micron. 2005;36(7-8):593-601. Epub 2005 Sep 1.


The role of collagen in bone structure: an image processing approach.

Tzaphlidou M.

Laboratory of Medical Physics, Medical School, Ioannina University, P.O. Box 1186, 45110 Ioannina, Greece. mtzaphli@cc.uoi.gr

Bone collagen structure in normal and pathological tissues is illustrated using techniques of thin section transmission electron microscopy and computer-assisted analysis. The normal bone collagen types, fibril architecture and diameter are described. In pathological tissue, deviations from normal fine structure are reflected in abnormal arrangements of collagen fibrils and abnormalities in fibril diameter. Computer analyses of normal fibril positive staining patterns are presented in order to provide a basis for comparing such patterns with pathological ones.

Publication Types:
Review

PMID: 16209926 [PubMed - indexed for MEDLINE]

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6: IUBMB Life. 2005 Mar;57(3):161-72.


Collagen structure: the Madras triple helix and the current scenario.

Bhattacharjee A, Bansal M.

Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.

This year marks the 50th anniversary of the coiled-coil triple helical structure of collagen, first proposed by Ramachandran's group from Madras. The structure is unique among the protein secondary structures in that it requires a very specific tripeptide sequence repeat, with glycine being mandatory at every third position and readily accommodates the imino acids proline/hydroxyproline, at the other two positions. The original structure was postulated to be stabilized by two interchain hydrogen bonds, per tripeptide. Subsequent modeling studies suggested that the triple helix is stabilized by one direct inter chain hydrogen bond as well as water mediated hydrogen bonds. The hydroxyproline residues were also implicated to play an important role in stabilizing the collagen fibres. Several high resolution crystal structures of oligopeptides related to collagen have been determined in the last ten years. Stability of synthetic mimics of collagen has also been extensively studied. These have confirmed the essential correctness of the coiled-coil triple helical structure of collagen, as well as the role of water and hydroxyproline residues, but also indicated additional sequence-dependent features. This review discusses some of these recent results and their implications for collagen fiber formation.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 16036578 [PubMed - indexed for MEDLINE]

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7: Adv Protein Chem. 2005;70:301-39.


Molecular structure of the collagen triple helix.

Brodsky B, Persikov AV.

Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.

The molecular conformation of the collagen triple helix confers strict amino acid sequence constraints, requiring a (Gly-X-Y)(n) repeating pattern and a high content of imino acids. The increasing family of collagens and proteins with collagenous domains shows the collagen triple helix to be a basic motif adaptable to a range of proteins and functions. Its rodlike domain has the potential for various modes of self-association and the capacity to bind receptors, other proteins, GAGs, and nucleic acids. High-resolution crystal structures obtained for collagen model peptides confirm the supercoiled triple helix conformation, and provide new information on hydrogen bonding patterns, hydration, sidechain interactions, and ligand binding. For several peptides, the helix twist was found to be sequence dependent, and such variation in helix twist may serve as recognition features or to orient the triple helix for binding. Mutations in the collagen triple-helix domain lead to a variety of human disorders. The most common mutations are single-base substitutions that lead to the replacement of one Gly residue, breaking the Gly-X-Y repeating pattern. A single Gly substitution destabilizes the triple helix through a local disruption in hydrogen bonding and produces a discontinuity in the register of the helix. Molecular information about the collagen triple helix and the effect of mutations will lead to a better understanding of function and pathology.

Publication Types:
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 15837519 [PubMed - indexed for MEDLINE]

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8: J Musculoskelet Neuronal Interact. 2005 Mar;5(1):5-21.


Development of tendon structure and function: regulation of collagen fibrillogenesis.

Zhang G, Young BB, Ezura Y, Favata M, Soslowsky LJ, Chakravarti S, Birk DE.

Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.

In the tendon, the development of mature mechanical properties is dependent on the assembly of a tendon-specific extracellular matrix. This matrix is synthesized by the tendon fibroblasts and composed of collagen fibrils organized as fibers, as well as fibril-associated collagenous and non-collagenous proteins. All of these components are integrated, during development and growth, to form a functional tissue. During tendon development, collagen fibrillogenesis and matrix assembly progress through multiple steps where each step is regulated independently, culminating in a structurally and functionally mature tissue. Collagen fibrillogenesis occurs in a series of extracellular compartments where fibril intermediates are assembled and mature fibrils grow through a process of post-depositional fusion of the intermediates. Linear and lateral fibril growth occurs after the immature fibril intermediates are incorporated into fibers. The processes are regulated by interactions of extracellular macromolecules with the fibrils. Interactions with quantitatively minor fibrillar collagens, fibril-associated collagens and proteoglycans influence different steps in fibrillogenesis and the extracellular microdomains provide a mechanism for the tendon fibroblasts to regulate these extracellular interactions.

Publication Types:
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 15788867 [PubMed - indexed for MEDLINE]

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9: Protein Pept Lett. 2002 Apr;9(2):107-16.


Recent progress on collagen triple helix structure, stability and assembly.

Berisio R, Vitagliano L, Mazzarella L, Zagari A.

Centro di Studio di Biocristallografia, CNR, Via Mezzocannone 6, I-80134 Napoli, Italy.

Collagen is the major structural protein in skin, bone, tendon, cartilage and blood vessels. Its triple helical structure has been long studied by fibre diffraction. More recently, single crystal X-ray diffraction on collagen-like polypeptide models has allowed a significantly improved description of the triple helix and it has shed light on the relationships between triple helix features and stability. This review outlines the current knowledge regarding collagen triple helix structure, stability, and assembly, with a particular emphasis on the latest structural results.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 12141907 [PubMed - indexed for MEDLINE]

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10: IUBMB Life. 2002 Feb;53(2):77-84.


Structure and function of collagen-derived endostatin inhibitors of angiogenesis.

Sasaki T, Hohenester E, Timpl R.

Max-Planck-Institut für Biochemie, Martinsried, Germany.

Endostatins are inhibitors of endothelial cell migration and angiogenesis and have been shown to reduce tumor growth in animal models. They are derived from the nontriplehelical C-terminal NC1 domains of collagens XV and XVIII, which are released proteolytically in trimeric form and further converted to monomeric endostatins of about 20 kDa. Both endostatin isoforms share a compact globular fold, but differ in certain binding properties for proteins and cells, as well as in tissue distribution. Differences in activity were found between NC1 domains and endostatins and are related to the oligomerization state. Endostatin effects are not restricted to endothelial cells, but also control renal epithelial cells and neuronal guidance in C. elegans. Cellular receptors are still insufficiently characterized and include for endostatin-XVIII heparan sulfate proteoglycans. Receptor engagement elicits various downstream effects including tyrosine kinase and gene activation. Much remains to be learned, however, about details of the signal transduction cascades and how they interfere with pro-angiogenic factors under physiological conditions and during therapeutic treatment.

Publication Types:
Review

PMID: 12049199 [PubMed - indexed for MEDLINE]

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11: Sheng Wu Yi Xue Gong Cheng Xue Za Zhi. 2002 Jan;19(1):127-31.


[Materials and structure design of artificial dermis equivalent based on collagen]

[Article in Chinese]

Gao C, Wang D, Yuan J, Shen J.

Department of Polymer Science and Engineering, Zhejiang University, Hangzhou 310027. cygao@mail.hz.zj.cn

The schematic structure model, materials selection and microstructure modulation are introduced for the design of artificial dermis equivalent. The artificial skin should also possess a bilayer structure that imitates then natural skin, i.e. the top layer functions as a temporary epidermis which is composed of polymer elastomer that is permeable for moisture but not for water, the bottom layer is the skin regeneration template employing collagen based sponge. In addition to collagen, polysaccharides like glycosaminoglycan is also used in the artificial dermis equivalent in order to simulate the natural extracellular matrix of skin and to modulate the degradation rate. The pore size and morphology of collagen porous membranes can be controlled by variation of the pH value, concentration and freezing temperature. Hence, the microstructure of the dermis equivalent can be optimized. The collagen based artificial dermis equivalent thus fabricated may be an option to skin graft in the clinical treatment of full skin injuries and ulcers.

Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review

PMID: 11951499 [PubMed - indexed for MEDLINE]

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12: Seikagaku. 2001 Oct;73(10):1239-45.


[Structure and functional role of type XVIII collagen/endostatin]

[Article in Japanese]

Yamaguchi N.

Department of Molecular Pathogenesis, Medical Research Institute, Tokyo Medical and Dental University, Kandasurugadai 2-3-10, Chiyoda-ku, Tokyo 101-0062.

Publication Types:
Review

PMID: 11725541 [PubMed - indexed for MEDLINE]

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13: Pharm Unserer Zeit. 2001;30(6):488-94.


[Supporting function of collagen and hydroxyapatite. Structure and function of bone]

[Article in German]

Felsenberg D.

Universitätsklinikum Benjamin Franklin Ragiologische Klinik und Poliklinik Hindenburgdamm 30 12200 Berlin.

Publication Types:
Review

PMID: 11715680 [PubMed - indexed for MEDLINE]

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14: Micron. 2001 Apr;32(3):251-60.


Collagen structure and functional implications.

Ottani V, Raspanti M, Ruggeri A.

Istituto di Anatomia Umana Normale, Via Irnerio 48, 40126, Bologna, Italy.

The bio-mechanical requirements to which the connective tissue is subjected suggest that a causal correlation exist between the substructure and the collagen fibril function. We discuss the relationship between the inner structure of collagen fibrils, their diameter, their spatial layout and the functional requirements they have to withstand, and suggest that collagen fibrils may belong to two different forms indicated as "T-type" and "C-type". The first class, consisting of large, heterogeneous fibrils, parallely tightly packed, subjected to tensile stress along their axis is found in highly tensile structures such as tendons, ligaments and bone. The other class, consisting of small, homogeneous fibrils, helically arranged, resisting multidirectional stresses, is mostly present within highly compliant tissues such as blood vessel walls, skin and nerve sheaths. What causes these architectures to appear is discussed in detail in this review.

Publication Types:
Review

PMID: 11006505 [PubMed - indexed for MEDLINE]

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15: Cell Struct Funct. 2000 Apr;25(2):97-101.


Collagen XVIII/endostatin structure and functional role in angiogenesis.

Zatterstrom UK, Felbor U, Fukai N, Olsen BR.

Harvard Medical School, Department of Cell Biology, Boston, MA 02115, USA.

The angiogenesis inhibitor endostatin is a 20 kDA C-terminal fragment of collagen XVIII, a proteoglycan/collagen found in vessel walls and basement membranes. The endostatin fragment was originally identified in conditioned media from a murine endothelial tumor cell line. Endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies. The molecular mechanisms behind the inhibition of angiogenesis have not yet been elucidated. Studies of the crystal structure of endostatin have shown a compact globular fold, with one face particularly rich in arginine residues acting as a heparin-binding epitope. It was initially suggested that zinc binding was essential for the antiangiogenic mechanism but later studies indicate that zinc has a structural rather than a functional role in endostatin. The generation of endostatin or endostatin-like collagen XVIII fragments is catalyzed by proteolytic enzymes, including cathepsin L and matrix metalloproteases, that cleave peptide bonds within the protease-sensitive hinge region of the C-terminal domain. The processing of collagen XVIII to endostatin may represent a local control mechanism for the regulation of angiogenesis.

Publication Types:
Review

PMID: 10885579 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

16: J Gastroenterol Hepatol. 1998 Sep;13 Suppl:S19-32.


Molecular mechanisms in the reversible regulation of morphology, proliferation and collagen metabolism in hepatic stellate cells by the three-dimensional structure of the extracellular matrix.

Senoo H, Imai K, Matano Y, Sato M.

Department of Anatomy, Akita University School of Medicine, Japan. senoo@ipc.akita-u.ac.jp

Hepatic stellate cells (vitamin A-storing cells, lipocytes, interstitial cells, fat-storing cells, Ito cells) exist in the perisinusoidal space of the hepatic lobule and store 80% of the body's retinoids as retinyl palmitate in lipid droplets in the cytoplasm. Under physiological conditions, these cells play pivotal roles in the regulation of retinoid homeostasis; they express specific receptors for retinol-binding protein (RBP), a binding protein specific for retinol, on their cell surface, and take up the complex of retinol and RBP by receptor-mediated endocytosis. However, in pathological conditions such as liver fibrosis, these cells lose retinoids and synthesize a large amount of extracellular matrix (ECM) components including collagen, proteoglycan and adhesive glycoproteins. The morphology of these cells also changes from star-shaped stellate cells to that of fibroblasts or myofibroblasts. The three-dimensional structure of ECM components was found to regulate reversibly the morphology, proliferation and functions of hepatic stellate cells. Molecular mechanisms in the reversible regulation of stellate cells by ECM imply cell surface integrin binding to ECM components followed by signal transduction processes and then cytoskeleton assembly.

Publication Types:
Review

PMID: 9792031 [PubMed - indexed for MEDLINE]

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17: J Struct Biol. 1998;122(1-2):119-22.


Fibrillar structure and mechanical properties of collagen.

Fratzl P, Misof K, Zizak I, Rapp G, Amenitsch H, Bernstorff S.

Materials Physics Institute and Ludwig-Boltzmann Institute of Osteology, University of Wien, Strudlhofgasse 4, Wien, A-1090, Austria. fratzl@unileoben.ac.at

Collagen type I is among the most important stress-carrying protein structures in mammals. Despite their importance for the outstanding mechanical properties of this tissue, there is still a lack of understanding of the processes that lead to the specific shape of the stress-strain curve of collagen. Recent in situ synchrotron X-ray scattering experiments suggest that several different processes could dominate depending on the amount of strain. While at small strains there is a straightening of kinks in the collagen structure, first at the fibrillar then at the molecular level, higher strains lead to molecular gliding within the fibrils and ultimately to a disruption of the fibril structure. Moreover, it was observed that the strain within collagen fibrils is always considerably smaller than in the whole tendon. This phenomenon is still very poorly understood but points toward the existence of additional gliding processes occurring at the interfibrillar level. Copyright 1998 Academic Press.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 9724612 [PubMed - indexed for MEDLINE]

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18: J Struct Biol. 1998;122(1-2):111-8.


The collagen fibril: the almost crystalline structure.

Prockop DJ, Fertala A.

Center for Gene Therapy, Allegheny University of the Health Sciences, Philadelphia, Pennsylvania, 19102, USA.

The structure of collagen fibrils has intrigued many investigators over the years. A crystal structure has been available for some time, but the crystal structure has been difficult to reconcile with other observations about collagen fibrils such as their roundness and their growth from paraboloidal tips. Several alternative models recently have been suggested, but none of them fully account for all the data. One recent approach to solving the fibrillar structure is to define specific binding sites on the collagen monomer that direct self-assembly of monomers into fibrils. Copyright 1998 Academic Press.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 9724611 [PubMed - indexed for MEDLINE]

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19: Histol Histopathol. 1997 Apr;12(2):557-66.


Collagen types VIII and X, two non-fibrillar, short-chain collagens. Structure homologies, functions and involvement in pathology.

Sutmuller M, Bruijn JA, de Heer E.

Department of Pathology, University of Leiden, The Netherlands.

Collagens can be divided into two groups, i.e., fibrillar and non-fibrillar collagens. Short-chain collagens, a subgroup of non-fibrillar collagens, comprises collagen type VIII and type X. These two collagen types show several similarities in structure and possibly also in function. Type VIII collagen appears to be secreted by rapidly proliferating cells. It can be found in basement membranes and may serve as a molecular bridge between different types of matrix molecules. In different tissues this collagen type may serve different functions. Stabilization of membranes, angiogenesis, and interactions with other extracellular matrix molecules. Since collagen type X is produced by hypertrophic chondrocytes, this collagen type can only be found in matrix of the hypertrophic zone of the epiphyseal growth plate cartilage. Collagen type X is probably involved in the process of mineralization, endochondral ossification, and is also proposed to play a role in angiogenesis. Collagen types VII and X may be involved in matrix and bone disorders. Their structure, function, and involvement in pathology are discussed in this review.

Publication Types:
Review

PMID: 9151143 [PubMed - indexed for MEDLINE]

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20: Matrix Biol. 1997 Mar;15(8-9):545-54.


The collagen triple-helix structure.

Brodsky B, Ramshaw JA.

Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway, USA.

Recent advances, principally through the study of peptide models, have led to an enhanced understanding of the structure and function of the collagen triple helix. In particular, the first crystal structure has clearly shown the highly ordered hydration network critical for stabilizing both the molecular conformation and the interactions between triple helices. The sequence dependent nature of the conformational features is also under active investigation by NMR and other techniques. The triple-helix motif has now been identified in proteins other than collagens, and it has been established as being important in many specific biological interactions as well as being a structural element. The nature of recognition and the degree of specificity for interactions involving triple helices may differ from globular proteins. Triple-helix binding domains consist of linear sequences along the helix, making them amenable to characterization by simple model peptides. The application of structural techniques to such model peptides can serve to clarify the interactions involved in triple-helix recognition and binding and can help explain the varying impact of different structural alterations found in mutant collagens in diseased states.

Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 9138287 [PubMed - indexed for MEDLINE]

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21: Bioessays. 1994 Mar;16(3):171-8.


The cuticle of the nematode Caenorhabditis elegans: a complex collagen structure.

Johnstone IL.

Institute of Genetics, University of Glasgow, UK.

The cuticle of the nematode Caenorhabditis elegans forms the barrier between the animal and its environment. In addition to being a protective layer, it is an exoskeleton which is important in maintaining and defining the normal shape of the nematode. The cuticle is an extracellular matrix consisting predominantly of small collagen-like proteins that are extensively crosslinked. Although it also contains other protein and non-protein compounds that undoubtedly play a significant part in its function, the specific role of collagen in cuticle structure and morphology is considered here. The C. elegans genome contains between 50 and 150 collagen genes, most of which are believed to encode cuticular collagens. Mutations that result in cuticular defects and grossly altered body form have been identified in more than 40 genes. Six of these genes are now known to encode cuticular collagens, a finding that confirms the importance of this group of structural proteins to the formation of the cuticle and the role of the cuticle as an exoskeleton in shaping the worm. It is likely that many more of the genes identified by mutations giving altered body form, will be collagen genes. Mutations in the cuticular collagen genes provide a powerful tool for investigating the mechanisms by which this group of proteins interact to form the nematode cuticle.

Publication Types:
Review

PMID: 8166670 [PubMed - indexed for MEDLINE]

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22: Prog Nucleic Acid Res Mol Biol. 1994;47:29-80.


Collagen genes: mutations affecting collagen structure and expression.

Cole WG.

Division of Orthopaedics, Hospital for Sick Children, Toronto, Ontario, Canada.

It is to be expected that more collagen genes will be identified and that additional heritable connective tissue diseases will be shown to arise from collagen mutations. Further progress will be fostered by the coordinated study of naturally occurring and induced heritable connective tissues diseases. In some instances, human mutations will be studied in more detail using transgenic mice, while in others, transgenic studies will be used to determine the type of human phenotype that is likely to result from mutations of a given collagen gene. Further studies of transcriptional regulation of the collagen genes will provide the prospect for therapeutic control of expression of specific collagen genes in patients with genetically determined collagen disorders as well as in a wide range of common human diseases in which abnormal formation of the connective tissues is a feature.

Publication Types:
Review

PMID: 8016323 [PubMed - indexed for MEDLINE]

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23: Contrib Nephrol. 1994;107:163-7.


Structure and organization of type IV collagen of renal glomerular basement membrane.

Hudson BG, Kalluri R, Gunwar S, Noelken ME.

Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City.

Publication Types:
Review

PMID: 8004963 [PubMed - indexed for MEDLINE]

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24: J Biol Chem. 1993 Dec 15;268(35):26033-6.


Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis.

Hudson BG, Reeders ST, Tryggvason K.

Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City 66160.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 8253711 [PubMed - indexed for MEDLINE]

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25: Biochem Soc Trans. 1993 May;21(2):464-8.


Structure/function relationships in the collectins (mammalian lectins containing collagen-like regions).

Reid KB.

Department of Biochemistry, University of Oxford, U.K.

Publication Types:
Review

PMID: 8359511 [PubMed - indexed for MEDLINE]

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26: Clin Orthop Relat Res. 1992 Sep;(282):250-72.


Collagen types. Molecular structure and tissue distribution.

Burgeson RE, Nimni ME.

Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129.

The collagens are products of a superfamily of closely related genes. Currently, there are 13 described collagens encompassing at least 25 separate genes. The collagen molecules can be categorized into four classes. Class I consists of molecules that form the banded collagen fibers that are readily seen by routine electron microscopy. The banded fibers are heterogenous with respect to collagen type, containing at least two and often three collagen types in each fibril. This multiplicity is believed to effect the rate of fibril growth and the final fibril diameter. Class II contains collagens that adhere to the surface of the banded fibrils. The function of these molecules is not yet known. The third Class consists of molecules that form independent fiber systems. These include the basement membrane, beaded filaments, anchoring fibrils, and the network surrounding hypertrophic chondrocytes. The last class contains several collagens with unknown fiber forms, and whose functions are unclear. Tissues contain multiple fiber forms and therefore many individual collagen types. Bone is no different, and there are presently four known collagens in the bone cortex. This article summarizes knowledge of the structures and functions of the collagen superfamily.

Publication Types:
Review

PMID: 1516320 [PubMed - indexed for MEDLINE]

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27: Electron Microsc Rev. 1992;5(1):25-35.


Abnormal collagen fibril structure as studied by electron microscopy.

Tzaphlidou M.

Laboratory of Medical Physics, Medical School, University of Ioannina, Greece.

Transmission electron microscopy has emerged as an ideal tool for the study and diagnosis of various disorders that involve collagen, since the information obtained by this technique is at the ultrastructural level. Structural alterations of collagen fibrils brought about by these disorders are discussed. The positive staining pattern of such fibrils is also investigated. In addition, this review describes how quantitative studies of electron-optical images from abnormal collagen fibrils can lead to information about the changes produced by collagen defects which relate to molecular or fibril architecture.

Publication Types:
Review

PMID: 1370381 [PubMed - indexed for MEDLINE]

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28: Adv Carbohydr Chem Biochem. 1991;49:239-61.


Structure of collagen fibril-associated, small proteoglycans of mammalian origin.

Garg HG, Lyon NB.

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Massachusetts General Hospital, Boston.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 1814173 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

29: J Biol Chem. 1990 Sep 15;265(26):15349-52.


Mutations that alter the primary structure of type I collagen. The perils of a system for generating large structures by the principle of nucleated growth.

Prockop DJ.

Department of Biochemistry and Molecular Biology, Jefferson Institute of Molecular Medicine, Jefferson Medical College, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2203776 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

30: Trends Genet. 1990 Sep;6(9):293-300.


Brittle bones--fragile molecules: disorders of collagen gene structure and expression.

Byers PH.

Department of Pathology, University of Washington, Seattle 98195.

Mutations in the genes that encode the chains of type I collagen, the major structural protein in most tissues, usually produce brittle bones. The consequences of even apparently minor mutations--single base substitutions--can range from lethal to mild, and the phenotypic consequences reflect the nature and position of the mutation. The manner in which phenotypes are produced depends on the effect of the mutation on the structural integrity of the molecule and on whether or how the abnormal molecules can be incorporated into an extracellular matrix.

Publication Types:
Review

PMID: 2238087 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

31: Mol Cell Biochem. 1990 Jul 17;96(1):1-14.


Collagen and the myocardium: fibrillar structure, biosynthesis and degradation in relation to hypertrophy and its regression.

Eghbali M, Weber KT.

Cardiovascular Institute, Michael Reese Hospital, University of Chicago Pritzker School of Medicine, IL 60616.

The extracellular matrix of the myocardium contains an elaborate structural matrix composed mainly of fibrillar types I and III collagen. This matrix is responsible for the support and alignment of myocytes and capillaries. Because of its alignment, location, configuration and tensile strength, relative to cardiac myocytes, the collagen matrix represents a major determinant of myocardial stiffness. Cardiac fibroblasts, not myocytes, contain the mRNA for these fibrillar collagens. In the hypertrophic remodeling of the myocardium that accompanies arterial hypertension, a progressive structural and biochemical remodeling of the matrix follows enhanced collagen gene expression. The resultant significant accumulation of collagen in the interstitium and around intramyocardial coronary arteries, or interstitial and perivascular fibrosis, represents a pathologic remodeling of the myocardium that compromises this normally efficient pump. This report reviews the structural nature, biosynthesis and degradation of collagen in the normal and hypertrophied myocardium. It suggests that interstitial heart disease, or the disproportionate growth of the extracellular matrix relative to myocyte hypertrophy, is an entity that merits greater understanding, particularly the factors regulating types I and III collagen gene expression and their degradation.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2146489 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

32: Ann N Y Acad Sci. 1990;580:97-111.


Structure of the human type IV collagen genes.

Tryggvason K, Soininen R, Hostikka SL, Ganguly A, Huotari M, Prockop DJ.

Biocenter, University of Oulu, Finland.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2186699 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

33: Ann N Y Acad Sci. 1990;580:8-16.


The structure of type XII collagen.

Gordon MK, Gerecke DR, Dublet B, van der Rest M, Sugrue SP, Olsen BR.

Department of Anatomy and Cellular Biology, Tufts University School of Medicine, Boston, Massachusetts 02111.

Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2186698 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

34: Ann N Y Acad Sci. 1990;580:74-80.


Fibrillar collagen genes. Structure and expression in normal and diseased states.

Ramirez F, Boast S, D'Alessio M, Lee B, Prince J, Su MW, Vissing H, Yoshioka H.

Department of Microbiology and Immunology, Morse Institute of Molecular Genetics, State University of New York, Brooklyn 11203.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2186697 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

35: Ann N Y Acad Sci. 1990;580:32-43.


The structure and function of type VII collagen.

Burgeson RE, Lunstrum GP, Rokosova B, Rimberg CS, Rosenbaum LM, Keene DR.

Shriners Hospital for Crippled Children, Portland, Oregon 97201.

Publication Types:
Review

PMID: 2186694 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

36: Ann N Y Acad Sci. 1990;580:1-7.


The structure and macromolecular organization of type IX collagen in cartilage.

Shimokomaki M, Wright DW, Irwin MH, van der Rest M, Mayne R.

Department of Cell Biology and Anatomy, University of Alabama, Birmingham 35294.

Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2186687 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

37: Am J Med Genet. 1989 Sep;34(1):72-80.


Inherited disorders of collagen gene structure and expression.

Byers PH.

Department of Pathology, University of Washington, Seattle 98195.

As a result of investigations completed during the last 15 years, the molecular bases of most form of osteogenesis imperfecta (OI) and of some forms of the Ehlers-Danlos syndrome (EDS) are now known. Most forms of OI result from point mutations in the genes (COL1A1 and COL1A2) that encode the chains of type I procollagen or mutations that affect the expression of these genes. Less frequently, mutations that affect the size of the chain can also result in these phenotypes. The phenotypic presentation appears to be determined by the nature of the mutation, the chain in which it occurs, and, for point mutations, the position of the substitution and the nature of the substituting amino acid in the protein product. Similar mutations in the gene (COL3A1) that encodes the chains of type III procollagen result in the EDS type IV phenotype. Mutations which result in deletion of the cleavage site for the aminoterminal procollagen protease result in the EDS type VII phenotype and other mutations which affect the structure of the triple-helical domain by deletions and alter the conformation of the substrate at the site of proteolytic conversion can produce mixed phenotypes. Alterations in post-translational processing of collagenous proteins can result in the EDS type VI and EDS type IX phenotypes. Linkage analysis and study of type II collagen proteins from individuals with a variety of skeletal dysplasias suggest that similar mutations in these genes also result in clinically apparent phenotypes. Mutations in the majority of the 20 known collagen genes have not yet been identified.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 2683783 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

38: J Card Surg. 1988 Dec;3(4):523-33.


The cross-linking and structure modification of the collagen matrix in the design of cardiovascular prosthesis.

Nimni ME.

Department of Biochemistry, University of Southern California School of Medicine, Los Angeles.

Glutaraldehyde cross-linking of native or reconstituted collagen fibrils and tissues rich in collagen significantly reduces biodegradation. Other aldehydes are less efficient than glutaraldehyde in generating chemically, biologically, and thermally stable cross-links. Implants of collagenous materials cross-linked with glutaraldehyde are subject long-term to calcification, biodegradation, and low-grade immune reactions. We have attempted to overcome these problems by enhancing cross-linking through (a) bridging of activated carboxyl groups with diamines and (b) using glutaraldehyde to cross-link the epsilon-NH2 groups in collagen and the unreacted amines introduced by aliphatic dismines. This cross-linking reduces tissue degradation and nearly eliminates humoral antibody induction. Covalent binding of diphosphonates, specifically 3-amino-1-hydroxypopane-1, 1-diphosphonic acid (3-APD), and to a lesser extent chondroitin sulfate to collagen or to the cross-ling-enhanced collagen network reduces its potential for calcification. Platelet aggregation also is reduced by glutaraldehyde cross-linking and nearly eliminated by the covalent binding of chondroitin sulfate to collagen. The cytotoxicity of residual glutaraldehyde can be minimized by chemical neutralization and thorough rough rinsing.

Publication Types:
Review

PMID: 2980056 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

39: Biochem Soc Trans. 1988 Oct;16(5):661-3.


Collagen gene structure.

Dalgleish R.

Department of Genetics, University of Leicester, U.K.

The collagens of vertebrates may be divided into three groups according to chain size and whether or not the helical domains are continuous. Present evidence suggests that, at least within one of these groups, similarity between collagens is reflected in the organization of the genes that encode them. Early evidence suggested that collagen genes evolved on the basis of exons which are multiples of a primordial building block of 54 bp, separated by much larger introns. This model of collagen gene evolution is contradicted by the recent discovery of a collagen gene with a single long open reading frame.

Publication Types:
Review

PMID: 3069510 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

40: Int Rev Immunol. 1988 Sep;4(1):65-81.


Collagen-induced arthritis in rodents: a review of immunity to type II collagen with emphasis on the importance of molecular conformation and structure.

Cremer MA, Kang AH.

Department of Medicine, University of Tennessee, Memphis.

Publication Types:
Review

PMID: 3072386 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

41: Biophys Chem. 1988 Feb;29(1-2):195-209.


The molecular and fibrillar structure of collagen and its relationship to the mechanical properties of connective tissue.

Parry DA.

Department of Physics and Biophysics, Massey University, Palmerston North, New Zealand.

The conformation of type I collagen molecules has been refined using a linked-atom least-squares procedure in conjunction with high-quality X-ray diffraction data. In many tendons these molecules pack in crystalline arrays and a careful measurement of the positions of the Bragg reflections allows the unit cell to be determined with high precision. From a further analysis of the X-ray data it can be shown that the highly ordered overlap region of the collagen fibrils consists of a crystalline array of molecular segments inclined by a small angle with respect to the fibril axis. In contrast, the gap region is less well ordered and contains molecular segments that are likely to be inclined by a similar angle but in a different vertical plane to that found in the overlap region. The collagen molecule thus has a D-periodic crimp in addition to the macroscopic crimp observed visually in the collagen fibres of many connective tissues. The growth and development of collagen fibrils have been studied by electron microscopy for a diverse range of connective tissues and the general pattern of fibril growth has been established as a function of age. In particular, relationships between fibril size distribution, the content and composition of the glycosaminoglycans in the matrix and the mechanical role played by the fibrils in the tissue have been formulated and these now seem capable of explaining many new facets of connective tissue structure and function.

Publication Types:
Review

PMID: 3282560 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

42: Pathol Immunopathol Res. 1988;7(1-2):132-8.


Osteogenesis imperfecta and other inherited disorders of the structure and synthesis of type I collagen: models for the analysis of mutations that result in inherited chondrodysplasias.

Cohn DH, Byers PH.

Department of Pathology, University of Washington, Seattle.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 3065765 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

43: Ann N Y Acad Sci. 1988;543:47-61.


Imperfect collagenesis in osteogenesis imperfecta. The consequences of cysteine-glycine substitutions upon collagen structure and metabolism.

Steinmann B, Superti-Furga A, Royce PM.

Department of Pediatrics, University of Zurich, Switzerland.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 3063164 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

44: Oxf Surv Eukaryot Genes. 1987;4:1-33.


Collagen gene structure.

Sykes B.

Publication Types:
Review

PMID: 3150808 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

45: Ryumachi. 1985 Nov;25(5):381-93.


[Fibronectin--functions, structure, immunological aspects and relation to collagen disease]

[Article in Japanese]

Watanabe Y, Nishikawa J.

Publication Types:
Review

PMID: 3914090 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

46: Biochem Soc Symp. 1984;49:67-84.


Collagen gene structure: the paradox may be resolved.

Boedtker H, Aho S.

Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6443754 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

47: Birth Defects Orig Artic Ser. 1984;20(3):65-77.


Lethal mutations in type I collagen: structure-function relationships in the type I collagen molecule.

Byers PH, Bonadio JF.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6391576 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

48: Semin Arthritis Rheum. 1983 Aug;13(1):1-86.


Collagen: structure, function, and metabolism in normal and fibrotic tissues.

Nimni ME.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6138859 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

49: Int Rev Connect Tissue Res. 1983;10:1-63.


The structure of collagen genes.

Boedtker H, Fuller F, Tate V.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 6315622 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

50: Ryumachi. 1980 Sep;20(4):298-304.


[Collagen structure and diseases (author's transl)]

[Article in Japanese]

Igarashi M.

Publication Types:
Review

PMID: 7003760 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

51: Tanpakushitsu Kakusan Koso. 1979 Nov;24(13):1391-403.


[The subcomponent C1q of the first component of human complement--its structure and similarities to the collagen molecules (author's transl)]

[Article in Japanese]

Yonemasu K.

Publication Types:
Review

PMID: 395572 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

52: Bull Rheum Dis. 1979-1980;30(3-4):1016-22.


Disorders of collagen structure and metabolism.

Jimenez SA, Lally EV.

Publication Types:
Review

PMID: 391314 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

53: J Invest Dermatol. 1978 Jul;71(1):9-11.


Connective tissue structure: cell binding to collagen.

Kleinman HK, Murray JC, McGoodwin EB, Martin GR.

Established lines of fibroblasts have been shown to adhere to collagen substrates via a serum-derived glycoprotein. The attachment of various other cells to collagen types I-IV is examined here. Cells such as human skin fibroblasts, periosteum, hepatocytes, connective tissue cells, and monocytes required the serum glycoprotein and adhered equally well to all collagens, but attachment of chondrocytes, epidermal cells, and neutrophils was inhibited by the serum glycoprotein. Attachment of 2 tumorigenic cells, an osteosarcoma and a fibrosarcoma, was found to be unaffected by the serum glycoprotein. In addition, the fibrosarcoma and epidermal cells attached preferentially to type IV (basement membrane) collagen.

Publication Types:
Review

PMID: 355571 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

54: Sci Prog. 1976 Autumn;63(251):419-44.


Current topics in the biosynthesis, structure and function of collagen.

Bailey AJ, Robins SP.

Publication Types:
Review

PMID: 785598 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

55: Int Rev Connect Tissue Res. 1976;7:1-60.


The primary structure of collagen.

Fietzek PP, Kühn K.

Publication Types:
Review

PMID: 177376 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

56: Semin Arthritis Rheum. 1974 Winter;4(2):95-150.


Collagen: Its structure and function in normal and pathological connective tissues.

Nimni ME.

Publication Types:
In Vitro
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 4617304 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

57: Harvey Lect. 1974;68:351-432.


Collagen biology: structure, degradation, and disease.

Gross J.

Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review

PMID: 4375674 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

58: Clin Orthop Relat Res. 1972;85:257-74.


Current concepts of collagen structure.

Steven FS.

Publication Types:
Review

PMID: 4556558 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

59: Adv Protein Chem. 1971;25:243-352.


The chemistry and structure of collagen.

Traub W, Piez KA.

Publication Types:
Review

PMID: 4111984 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

60: Arkh Patol. 1970;32(7):3-20.


[Contemporary concepts on the structure of collagen]

[Article in Russian]

Shekhter AB, Istranov LP.

Publication Types:
In Vitro
Review

PMID: 4924663 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

61: Symp Soc Dev Biol. 1970;29:164-94.


Collagen of embryonic type in the vertebrate eye and its relation to carbohydrates and subunit structure of tropocollagen.

Dische Z.

Publication Types:
Review

PMID: 4269661 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

62: Essays Biochem. 1969;5:59-87.


The structure of collagen.

Kühn K.

Publication Types:
Review

PMID: 4915277 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

63: Postepy Biochem. 1968;14(1):85-104.


[The actual view on the structure and properties of collagen]

[Article in Polish]

Skonieczna M, Sopata I, Wize J, Wojtecka-Lukasik E.

Publication Types:
Review

PMID: 4873705 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

64: Naturwissenschaften. 1967 Mar;54(5):101-9.


[Studies on the structure of collagen]

[Article in German]

Kühn K.

Publication Types:
Review

PMID: 4871925 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

65: Tanpakushitsu Kakusan Koso. 1966 Dec;11(14):1321-9.


[Crystalline structure of poly-L-proline--its relation to collagen structure]

[Article in Japanese]

Takigawa R, Tomita K.

Publication Types:
Review

PMID: 5342588 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------

66: Int Rev Connect Tissue Res. 1963;1:127-82.


MOLECULAR STRUCTURE OF COLLAGEN.

RAMACHANDRAN GN.

Publication Types:
Review

PMID: 14110864 [PubMed - indexed for MEDLINE]
 

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