Laminin Function
Published by Anonymous on 2007/9/24 (2240 reads)
1: Matrix Biol. 2000 Aug;19(4):309-17.
Structure and function of laminin LG modules.
Timpl R, Tisi D, Talts JF, Andac Z, Sasaki T, Hohenester E.
Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152, Martinsried, Germany. timpl@biochem.mpg.de
Laminin G domain-like (LG) modules of approximately 180-200 residues are found in a number of extracellular and receptor proteins and often are present in tandem arrays. LG modules are implicated in interactions with cellular receptors (integrins, alpha-dystroglycan), sulfated carbohydrates and other extracellular ligands. The recently determined crystal structures of LG modules of the laminin alpha2 chain reveal a compact beta sandwich fold and identify a novel calcium binding site. Binding epitopes for heparin, sulfatides and alpha-dystroglycan have been mapped by site-directed mutagenesis and show considerable overlap. The epitopes are located in surface loops around the calcium site, which in other proteins (agrin, neurexins) are modified by alternative splicing. Efficient ligand binding often requires LG modules to be present in tandem. The close proximity of the N- and C-termini in the LG module, as well as a unique link region between laminin LG3 and LG4, impose certain constraints on the arrangement of LG tandems. Further modifications may be introduced by proteolytic processing of laminin G domains, which is known to occur in the alpha2, alpha3 and alpha4 chains.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 10963991 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Dev Dyn. 2000 Jun;218(2):213-34.
Form and function: the laminin family of heterotrimers.
Colognato H, Yurchenco PD.
Department of Pathology & Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
The laminins are a family of glycoproteins that provide an integral part of the structural scaffolding of basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from alpha, beta, and gamma chain subunits, secreted and incorporated into cell-associated extracellular matrices. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors. Through these interactions, laminins critically contribute to cell differentiation, cell shape and movement, maintenance of tissue phenotypes, and promotion of tissue survival. Recent advances in the characterization of genetic disruptions in humans, mice, nematodes and flies have revealed developmental roles for the different laminin subunits in diverse cell types, affecting differentiation from blastocyst formation to the post-natal period. These genetic defects have challenged some of the previous concepts about basement membranes and have shed new light on the diversity and complexity of laminin functions as well as established the molecular basis of several human diseases. Copyright 2000 Wiley-Liss, Inc.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 10842354 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Methods Mol Biol. 2000;139:27-37.
Analysis of laminin structure and function with recombinant glycoprotein expressed in insect cells.
Mathus TL, Yurchenco PD.
Robert Wood Johnson Medical School, Piscataway, NJ, USA.
Publication Types:
Review
PMID: 10840775 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: FASEB J. 1990 Feb 1;4(2):148-60.
Structure and function of laminin: anatomy of a multidomain glycoprotein.
Beck K, Hunter I, Engel J.
Institute for Biophysics, University Linz, Austria.
Laminin is a large (900 kDa) mosaic protein composed of many distinct domains with different structures and functions. Globular and rodlike domains are arranged in an extended four-armed, cruciform shape that is well suited for mediating between distant sites on cells and other components of the extracellular matrix. The alpha-helical coiled-coil domain of the long arm is involved in the specific assembly of the three chains (A, B1, B2, and possible variants) of laminin and is the only domain composed of multiple chains. It is terminated by a large globular domain composed of five homologous subdomains formed by the COOH-terminal part of the A chain. Sites for receptor-mediated cell attachment and promotion of neurite outgrowth reside in the terminal region of the long arm. A second cell attachment site, a cell signaling site with mitogenic action, binding sites for the closely associated glycoprotein nidogen/entactin, and regions involved in calcium-dependent aggregation are localized in the short arms. These domains, which to a large extent are composed of Cys-rich repeats with limited homology to EGF, are the most highly conserved regions in laminins of different origin. At present, most structural and functional data have been collected for a laminin expressed by a mouse tumor, which can be readily isolated in native form and dissected into functional fragments by limited proteolysis. Increasing information on laminins from different species and tissues demonstrates considerable variations of structure. Isoforms of laminin assembled from different chains are focally and transiently expressed and may serve distinct functions at early stages of development even before being laid down as major components of basement membranes.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 2404817 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: J Oral Pathol. 1988 Aug;17(7):309-23.
Laminin: molecular organization and biological function.
Campbell JH, Terranova VP.
Department of Oral Biology, SUNY, Buffalo 14214.
Laminin, the most abundant glycoprotein molecule found in basement membrane, has multiple functions in eukaryotic tissues. It serves to attach epithelial cells to basement membrane, aids development and migration of specific cell types in growth and maturation, and has been implicated in tumor metastasis and some types of infection. Current concepts of the molecular organization and myriad functions of the laminin molecule are reviewed.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 3145965 [PubMed - indexed for MEDLINE]
Structure and function of laminin LG modules.
Timpl R, Tisi D, Talts JF, Andac Z, Sasaki T, Hohenester E.
Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, D-82152, Martinsried, Germany. timpl@biochem.mpg.de
Laminin G domain-like (LG) modules of approximately 180-200 residues are found in a number of extracellular and receptor proteins and often are present in tandem arrays. LG modules are implicated in interactions with cellular receptors (integrins, alpha-dystroglycan), sulfated carbohydrates and other extracellular ligands. The recently determined crystal structures of LG modules of the laminin alpha2 chain reveal a compact beta sandwich fold and identify a novel calcium binding site. Binding epitopes for heparin, sulfatides and alpha-dystroglycan have been mapped by site-directed mutagenesis and show considerable overlap. The epitopes are located in surface loops around the calcium site, which in other proteins (agrin, neurexins) are modified by alternative splicing. Efficient ligand binding often requires LG modules to be present in tandem. The close proximity of the N- and C-termini in the LG module, as well as a unique link region between laminin LG3 and LG4, impose certain constraints on the arrangement of LG tandems. Further modifications may be introduced by proteolytic processing of laminin G domains, which is known to occur in the alpha2, alpha3 and alpha4 chains.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 10963991 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Dev Dyn. 2000 Jun;218(2):213-34.
Form and function: the laminin family of heterotrimers.
Colognato H, Yurchenco PD.
Department of Pathology & Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
The laminins are a family of glycoproteins that provide an integral part of the structural scaffolding of basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from alpha, beta, and gamma chain subunits, secreted and incorporated into cell-associated extracellular matrices. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors. Through these interactions, laminins critically contribute to cell differentiation, cell shape and movement, maintenance of tissue phenotypes, and promotion of tissue survival. Recent advances in the characterization of genetic disruptions in humans, mice, nematodes and flies have revealed developmental roles for the different laminin subunits in diverse cell types, affecting differentiation from blastocyst formation to the post-natal period. These genetic defects have challenged some of the previous concepts about basement membranes and have shed new light on the diversity and complexity of laminin functions as well as established the molecular basis of several human diseases. Copyright 2000 Wiley-Liss, Inc.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 10842354 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Methods Mol Biol. 2000;139:27-37.
Analysis of laminin structure and function with recombinant glycoprotein expressed in insect cells.
Mathus TL, Yurchenco PD.
Robert Wood Johnson Medical School, Piscataway, NJ, USA.
Publication Types:
Review
PMID: 10840775 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: FASEB J. 1990 Feb 1;4(2):148-60.
Structure and function of laminin: anatomy of a multidomain glycoprotein.
Beck K, Hunter I, Engel J.
Institute for Biophysics, University Linz, Austria.
Laminin is a large (900 kDa) mosaic protein composed of many distinct domains with different structures and functions. Globular and rodlike domains are arranged in an extended four-armed, cruciform shape that is well suited for mediating between distant sites on cells and other components of the extracellular matrix. The alpha-helical coiled-coil domain of the long arm is involved in the specific assembly of the three chains (A, B1, B2, and possible variants) of laminin and is the only domain composed of multiple chains. It is terminated by a large globular domain composed of five homologous subdomains formed by the COOH-terminal part of the A chain. Sites for receptor-mediated cell attachment and promotion of neurite outgrowth reside in the terminal region of the long arm. A second cell attachment site, a cell signaling site with mitogenic action, binding sites for the closely associated glycoprotein nidogen/entactin, and regions involved in calcium-dependent aggregation are localized in the short arms. These domains, which to a large extent are composed of Cys-rich repeats with limited homology to EGF, are the most highly conserved regions in laminins of different origin. At present, most structural and functional data have been collected for a laminin expressed by a mouse tumor, which can be readily isolated in native form and dissected into functional fragments by limited proteolysis. Increasing information on laminins from different species and tissues demonstrates considerable variations of structure. Isoforms of laminin assembled from different chains are focally and transiently expressed and may serve distinct functions at early stages of development even before being laid down as major components of basement membranes.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 2404817 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: J Oral Pathol. 1988 Aug;17(7):309-23.
Laminin: molecular organization and biological function.
Campbell JH, Terranova VP.
Department of Oral Biology, SUNY, Buffalo 14214.
Laminin, the most abundant glycoprotein molecule found in basement membrane, has multiple functions in eukaryotic tissues. It serves to attach epithelial cells to basement membrane, aids development and migration of specific cell types in growth and maturation, and has been implicated in tumor metastasis and some types of infection. Current concepts of the molecular organization and myriad functions of the laminin molecule are reviewed.
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 3145965 [PubMed - indexed for MEDLINE]
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