logo logo
 
 
SmartSection is developed by The SmartFactory (http://www.smartfactory.ca), a division of INBOX Solutions (http://inboxinternational.com)
Integrin Expression
Published by Anonymous on 2007/9/27 (3074 reads)
1: Prog Retin Eye Res. 2007 Mar;26(2):99-161. Epub 2006 Dec 27.


Control of integrin genes expression in the eye.

Vigneault F, Zaniolo K, Gaudreault M, Gingras ME, Guérin SL.

Oncology and Molecular Endocrinology Research Center, CHUL, 2705 Laurier Blvd, Ste-Foy, Qc, Canada G1V 4G2.

The ending race for sequencing the human genome has left the scientists faced with new challenges. Indeed, now that almost every human gene has been sequenced and precisely positioned on the human chromosomes, one of the next, most burning task consist in understanding how transcription of these genes is ensured in any given cell. The integrins encoding genes are no exception. Integrins bridge the cell to the many components from the extracellular matrix (ECM), such as laminins (LM) and collagens, and thereby transduce intracellular signals that will alter many of the cell's properties such as adhesion, migration, proliferation and survival. As a much clearer picture of the many proteins that belong to this family has emerged over the last few years, tremendous efforts have been dedicated to the identification of the regulatory sequences that modulate their expression. This review provides an overview of the current state of knowledge about the organization of the regulatory elements and the transcription factors (TF) they bind that are used by the cell in order to ensure transcription of each of the integrins gene. A particular attention has been given to those reported to be expressed in the eye. It also explores how components from the ECM might participate in the control of integrins gene expression and establishes links to wound healing of the corneal epithelium, a process that transiently alter the composition of the basement membrane on which the epithelial cells lie.

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

PMID: 17194617 [PubMed - indexed for MEDLINE]

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

2: Mini Rev Med Chem. 2006 Feb;6(2):227-34.


Multimodality imaging of tumor integrin alphavbeta3 expression.

Chen X.

Molecular Imaging Program at Stanford, MIPS, Department of Radiology, Stanford University, CA 94305, USA. shawchen@stanford.edu

Most solid tumors are angiogenesis dependent. Anti-angiogenic pharmaceuticals that inhibit the growth of new blood vessels offer considerable promise as anti-cancer agents. With increasing numbers of anti-angiogenic drugs in clinical trials, there is an urgent need for detailed characterization of the heterogeneity of tumor vasculature and dissection of the complex network of mechanisms that control tumor angiogenesis. Non-invasive molecular imaging will play a key role in individualized anti-angiogenic therapy based upon molecular features of the new blood vessel growth. Integrin alpha(v)beta(3), which binds several ligands via an RGD tripeptide sequence, is uniquely expressed in tumor vasculature and aggressive tumor cells, making it a potential target for anti-angiogenic interventions. This review highlights some recent advances in multimodality imaging of tumor integrin expression with emphasis on positron emission tomography (PET).

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

PMID: 16472190 [PubMed - indexed for MEDLINE]

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

3: Cancer Metastasis Rev. 2005 Sep;24(3):383-93.


Integrin-dependent signal transduction regulating cyclin D1 expression and G1 phase cell cycle progression.

Walker JL, Assoian RK.

Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6084, USA.

Integrins and growth factor receptors coordinately regulate proliferation in nontransformed cells. Coordinate signaling from these receptors controls the activation of the G1 phase cyclin-dependent kinases, largely by regulating levels of cyclin D1 and p27(kip1). Induction of cyclin D1 is one of the best understood examples of an integrin/growth factor receptor-regulated G1 phase target. This review focuses on the integrin-dependent signal transduction events that regulate the expression of cyclin D1 during G1 phase.

Publication Types:
Research Support, N.I.H., Extramural
Review

PMID: 16258726 [PubMed - indexed for MEDLINE]

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

4: Biochim Biophys Acta. 2004 Apr 1;1691(1):1-15.


Regulation of E-cadherin expression and beta-catenin/Tcf transcriptional activity by the integrin-linked kinase.

Oloumi A, McPhee T, Dedhar S.

British Columbia Cancer Agency and Jack Bell Research Centre, University of British Columbia, Vancouver Hospital, 2660 Oak St. Vancouver, BC, Canada V6H 3Z6.

Integrin-linked kinase (ILK) is a serine/threonine protein kinase which interacts with the cytoplasmic domains of beta1 and beta3 integrins. ILK structure and its localization at the focal adhesion allows it not only to interact with different structural proteins, but also to mediate many different signalling pathways. Extracellular matrices (ECM) and growth factors each stimulate ILK signalling. Constitutive activation of ILK in epithelial cells results in oncogenic phenotypes such as disruption of cell extracellular matrix and cell to cell interactions, suppression of suspension-induced apoptosis, and induction of anchorage independent cell growth and cell cycle progression. More specifically, pathological overexpression of ILK results in down-regulation of E-cadherin expression, and nuclear accumulation of beta-catenin, leading to the subsequent activation of the beta-catenin/Tcf transcription complex, the downstream components of the Wnt signalling pathway. Here we review the data implicating ILK in the regulation of these two signalling pathways, and discuss recent novel insights into the molecular basis and requirement of ILK in the process of epithelial to mesenchymal transformation (EMT).

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

PMID: 15053919 [PubMed - indexed for MEDLINE]

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

5: Immunol Rev. 2002 Aug;186:189-207.


Integrin-dependent regulation of gene expression in leukocytes.

Rossetti G, Collinge M, Bender JR, Molteni R, Pardi R.

Unit of Leukocyte Biology, Department of Molecular Biology and Functional Genomics, Vita-Salute San Raffaele University School of Medicine, Milan, Italy.

In addition to their role in strengthening intercellular adhesion, leukocyte integrins transduce signals which affect genetic programs, consequently defining cell phenotype and function. These signals can be independently sufficient, or can cooperate with other environmental stimuli to affect gene expression regulation. In the past several years, there has been an emergence of mechanistic data which contribute to our understanding of these critical integrin roles. In this review, we describe anchorage-dependent T lymphocyte proliferation and, in particular, how leukocyte integrin engagement overcomes the G1 to S cell cycle restriction point in antigen-activated T cells. The related role of alphaLbeta2 integrin (LFA-1) as a T cell co-stimulatory molecule is discussed. This includes defining mechanisms whereby LFA-1 engagement enhances transcriptional activation of numerous genes by regulating its association with transcription modulators such as JAB-1, and through interaction with other gene-activating signaling complexes such as JAK-STATs. Evidence is presented to support that leukocyte integrin engagement provides potent signals which stabilize otherwise labile activation mRNA transcripts, including those encoding cytokine and extracellular matrix degrading proteins. These integrin-dependent mechanisms, all described recently, play important roles in T cell differentiation and proliferation, immune surveillance and inflammatory responses.

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

PMID: 12234372 [PubMed - indexed for MEDLINE]

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

6: Biorheology. 2000;37(1-2):109-16.


Chondrocyte integrin expression and function.

Loeser RF.

Department of Medicine-Rheumatology, Rush Medical College of Rush-Presbyterian-St. Luke's Medical Center, Chicago, IL 60612, USA.

The extracellular matrix (ECM) is an "information rich" environment and interactions between the chondrocyte and ECM regulate many biological processes important to cartilage homeostasis and repair including cell attachment, growth, differentiation, and survival. The integrin family of cell surface receptors appears to play a major role in mediating cell-matrix interactions that are important in regulating these processes. Chondrocytes have been found to express several members of the integrin family which can serve as receptors for fibronectin (alpha 5 beta 1), types II and VI collagen (alpha 1 beta 1, alpha 2 beta 1, alpha 10 beta 1), laminin (alpha 6 beta 1), and vitronectin and osteopontin (alpha V beta 3). Integrin expression can be regulated by growth factors including IGF-I and TGF-beta. By providing a link between the ECM and the cytoskeleton, integrins may be important transducers of mechanical stimuli. Integrin binding stimulates intracellular signaling which can affect gene expression and regulate chondrocyte function. Further studies are needed to more clearly define the role of integrins in cartilage.

Publication Types:
Review

PMID: 10912183 [PubMed - indexed for MEDLINE]

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

7: J Mammary Gland Biol Neoplasia. 1998 Apr;3(2):191-200.


Comment in:
J Mammary Gland Biol Neoplasia. 1998 Apr;3(2):109-16.

Altered integrin expression and the malignant phenotype: the contribution of multiple integrated integrin receptors.

Zutter MM, Sun H, Santoro SA.

Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

The integrins are a family of cell surface adhesion receptors that mediate adhesion to either components of the extracellular matrix or to other cells. The beta1 family of integrins represent the major class of cell substrate receptors with specificities primarily for collagens, laminins, and fibronectins. The role of the integrin family of cell surface adhesion receptors in normal mammary gland morphogenesis and the contributions of altered integrin receptor expression to the invasive and metastatic phenotype have been the primary focus of our lab, as well as a number of other laboratories. The alpha2beta1 integrin is expressed at high levels by normal differentiated epithelial cells including those of the normal breast. Using breast cancer as a model, we evaluated changes in integrin expression in malignancy. We and other investigators made the key observation that alpha2beta1 integrin expression is decreased in adenocarcinoma of the breast in a manner that correlates with the stage of differentiation. Studies of other adenocarcinomas have yielded similar results. When the alpha2beta1 integrin was reexpressed in a poorly differentiated mammary carcinoma that expressed no detectable alpha2 integrin subunit, a dramatic reversion of malignant phenotype to a differentiated epithelial phenotype was observed, indicating a critical role for alpha2beta1 expression in mammary gland differentiation. Other laboratories using monoclonal antibodies to competitively inhibit alpha2beta1 integrin adhesion or oncogenic transformation using c-erb2 have confirmed the important role of that alpha2beta1 integrin in mammary gland morphogenesis. Re-expression of the alpha2beta1 integrin also results in upregulation of both the alpha6 and beta4 integrin subunits. To determine the contribution of enhanced alpha6 and beta4 integrin expression to the abrogation of the malignant phenotype by alpha2beta1 integrin expression, we have now separately re-expressed the human alpha6 or beta4 integrin subunit in the breast cancer model.

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

PMID: 10819527 [PubMed - indexed for MEDLINE]

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

8: Ann N Y Acad Sci. 1999;890:204-22.


Matrix remodeling after stroke. De novo expression of matrix proteins and integrin receptors.

Ellison JA, Barone FC, Feuerstein GZ.

Department of Cardiovascular Pharmacology, SmithKline Beecham Pharmaceuticals, Philadelphia, Pennsylvania, USA.

Following an ischemic insult to the central nervous system a reorganization of cells and tissue takes place as the surrounding cells attempt to limit the injury, repair the damage, and restore normal architecture of the brain. This tissue remodeling requires de novo synthesis of genes and proteins which enables cells to actively change their relationship with the existing extracellular matrix and with other cells to reorganize the damaged tissue. We have identified two key molecular components of the matrix remodeling process after focal ischemia: osteopontin (OPN) and its integrin receptor alpha v beta 3 (alpha v beta 3). OPN is initially expressed by activated macrophages and microglia in the periinfarct region (24-48 hr) and at later times (5-15 days) in the core infarct. After focal stroke the alpha v beta 3 was upregulated by astrocytes in the periinfarct region. Spatial and temporal analyses demonstrated that at 5 days after injury the alpha v beta 3-positive astrocytes were at a distance from the osteopontin-expressing macrophages; by 15 days the alpha v beta 3-expressing astrocytes were localized within an osteopontin-rich matrix. In vitro OPN was shown to induce migration of astrocytes in a Boyden chamber system. These data suggest that OPN derived from microglia at the infarct border zone (and possible macrophages in the infarct core) may serve as an "astrokine" (suggested term for astrocyte chemoattractant) to organize the astrocyte scar after focal stroke. Our data demonstrate profound changes in brain matrix remodeling after focal ischemic stroke, including the synthesis and release of matrix proteins alien to the normal brain, the expression of integrin receptors that ligate these proteins, and possibly a novel function for microglial-derived OPN in astrocyte migration after focal ischemia that may drive glial activation, organization, and repair functions.

Publication Types:
Review

PMID: 10668427 [PubMed - indexed for MEDLINE]

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

9: J Appl Physiol. 2000 Jan;88(1):337-43.


Integrin signaling's potential for mediating gene expression in hypertrophying skeletal muscle.

Carson JA, Wei L.

Exercise Science Department, University of South Carolina, Columbia, South Carolina 29208, USA. jcarson@sph.sc.edu

Overloaded skeletal muscle undergoes dramatic shifts in gene expression, which alter both the phenotype and mass. Molecular biology techniques employing both in vivo and in vitro hypertrophy models have demonstrated that mechanical forces can alter skeletal muscle gene regulation. This review's purpose is to support integrin-mediated signaling as a candidate for mechanical load-induced hypertrophy. Research quantifying components of the integrin-signaling pathway in overloaded skeletal muscle have been integrated with knowledge regarding integrins role during development and cardiac hypertrophy, with the hope of demonstrating the pathway's importance. The role of integrin signaling as an integrator of mechanical forces and growth factor signaling during hypertrophy is discussed. Specific components of integrin signaling, including focal adhesion kinase and low-molecular-weight GTPase Rho are mentioned as downstream targets of this signaling pathway. There is a need for additional mechanistic studies capable of providing a stronger linkage between integrin-mediated signaling and skeletal muscle hypertrophy; however, there appears to be abundant justification for this type of research.

Publication Types:
Review

PMID: 10642399 [PubMed - indexed for MEDLINE]

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

10: Cell Adhes Commun. 1998;6(2-3):217-24.


Integrin signaling: cytoskeletal complexes, MAP kinase activation, and regulation of gene expression.

Danen EH, Lafrenie RM, Miyamoto S, Yamada KM.

Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892, USA. edanen@yoda.nidr.nih.gov

Members of the integrin family of adhesion receptors mediate interactions of cells with the extracellular matrix. Besides their role in tissue morphogenesis by anchorage of cells to basement membranes and migration along extracellular matrix proteins, integrins are thought to play a key role in mediating the control of gene expression by the extracellular matrix. Studies over the past 10 years have shown that integrin-mediated cell adhesion can trigger signal transduction cascades involving translocation of proteins and protein tyrosine phosphorylation events. In this review, we discuss approaches used in our lab to study early events in integrin signalling as well as further downstream changes.

Publication Types:
Review

PMID: 9823472 [PubMed - indexed for MEDLINE]

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

11: Am J Pathol. 1998 Nov;153(5):1347-51.


Comment on:
Am J Pathol. 1998 Nov;153(5):1435-42.

Role of the beta3 integrin subunit in human primary melanoma progression: multifunctional activities associated with alpha(v)beta3 integrin expression.

Seftor RE.

Department of Anatomy and Cell Biology, University of Iowa, Iowa City 52242-1109, USA. richard-seftor@uiowa.edu

Publication Types:
Comment
Review

PMID: 9811323 [PubMed - indexed for MEDLINE]

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

12: Curr Top Microbiol Immunol. 1998;231:167-85.


The ups and downs of alpha 2 beta 1-integrin expression: contributions to epithelial cell differentiation and the malignant phenotype.

Zutter MM, Santoro SA.

Department of Pathology, Barnes Hospital, Washington University School of Medicine, St. Louis, MO 63110, USA.

Publication Types:
Review

PMID: 9479866 [PubMed - indexed for MEDLINE]

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

13: Proc Soc Exp Biol Med. 1997 Feb;214(2):123-31.


The regulation of expression of integrin receptors.

Kim LT, Yamada KM.

Laboratory of Developmental Biology, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892-4370, USA.

The integrins are a family of cell surface receptors that mediate cell-extracellular matrix and cell-cell interactions. The quantities and activities of these receptors are modulated during a wide variety of biological processes. A variety of agents have been found to affect expression of integrins and their function. These include cytokines, hormones, and pharmacologic agents. Mechanisms regulating integrin expression and function include regulation of protein levels by transcriptional or posttranscriptional mechanisms, alteration of protein structure by alternative splicing of mRNA, mobilization to the cell surface of preexisting intracellular stores of integrins, and modulation of receptor activity (inside-out signaling). We review studies that assess the effects of external agents on integrin levels using the cytokine TGFbeta as an example. We also review studies that analyze integrin regulation with an emphasis on the control of integrin gene transcription. This review shows that the strategies for integrin modulation are quite complex. This regulatory sophistication is likely necessary, given the critical role that integrins play in the myriad social interactions of cells.

Publication Types:
Review

PMID: 9034129 [PubMed - indexed for MEDLINE]

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

14: Adv Exp Med Biol. 1997;400B:765-73.


Eicosanoid 12(S)-HETE upregulates endothelial cell alpha V beta 3 integrin expression and promotes tumor cell adhesion to vascular endothelium.

Honn KV, Tang DG.

Department of Radiation Oncology, Wayne State University, Detroit, MI 48202, USA.

Publication Types:
Review

PMID: 9547628 [PubMed - indexed for MEDLINE]

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

15: Acta Haematol. 1997;97(1-2):63-6.


Beta-1-integrin expression in adult acute lymphoblastic leukemia: possible relationship with the stem cell antigen CD34.

Cacciola RR, Stagno F, Impera S, Assisi AR, Cacciola E Jr, Guglielmo P.

Institute of Hematology, University of Catania, Italy.

In the hemopoietic system, interactions between stem cells and components of the bone marrow microenvironment play a pivotal role in blood cell proliferation and differentiation. Among the adhesion molecules, the integrins of the beta 1-subfamily are known to direct cell-cell and cell-matrix interactions and evidence has been provided that CD34-positive stem cells bind either to the bone marrow stroma or to the extracellular matrix proteins through the beta 1-integrins. It seems that changes in their expression pattern or signalling function are likely to reflect disturbances at the hemopoietic bone marrow microenvironmental level. Any alteration of their biological functions makes them attractive candidates for playing decisive roles in the leukemic processes. In this view, beta 1-integrins have been recognized to mediate those cellular interactions and migrations that are important in the biology of leukemia. In this paper we review some aspects of the role played by beta 1-integrins, especially VLA-4 and VLA-5, in adult acute lymphoblastic leukemia in relation with the expression rate of the stem cell antigen CD34.

Publication Types:
Review

PMID: 8980611 [PubMed - indexed for MEDLINE]

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

16: Bull Cancer. 1996 Jan;83(1):13-21.


[Modulation of integrin alpha-v-beta-1 expression on human tumor cells by leukemia inhibitory factor (LIF) and oncostatin M (OSM)]

[Article in French]

Heymann D, Harb J, Ringeard S, Blanchard F, Lassort D, Raher S, Godard A.

Inserm U211, Institut de Biologie, Nantes, France.

Integrins belong to a large family of heterodimeric membrane glycoproteins which mediate cell-cell or cell-extracellular matrix interactions. These interactions could play a major role during the migration of tumor cells across the extracellular matrix and vascular endothelium and would thus appear to be a requisite for the metastatic process. Treatment of the Foss human melanoma cell line with LIF or OSM, two cytokines involved in acute-phase response, increased the expression of membrane alpha v beta 1 by 1.5-2 fold. The same phenomenon was observed on the SK-N-SH human neuroblastoma cell line. This modulation, which was inhibited by specific monoclonal antibodies against alpha v or beta 1 integrin subunits, was concomitant with improved tumor cell attachment to the fibronectin matrix. Similar results were obtained after TNF-alpha treatment. Our findings demonstrate the ability of LIF and OSM to modulate tumor cell capacity to adhere to the matrix component, suggesting a potential role for these cytokines in modulation of tumoral progression.

Publication Types:
English Abstract
Review

PMID: 8672851 [PubMed - indexed for MEDLINE]

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

17: Nippon Rinsho. 1995 Jul;53(7):1678-82.


[Comparison of the pattern of integrin expression between primary tumors and liver metastasis of gastric and colorectal cancers]

[Article in Japanese]

Takamura H, Endo Y, Ninomiya I, Yonemura Y, Sasaki T.

Department of Surgery II, School of Medicine, Kanazawa University.

To investigate the interrelationship between integrin VLA3 overexpression and liver metastasis, immunohistochemical studies of VLA3 were made in 73 cases of gastric cancer (66 cases without liver metastasis, 7 cases with liver metastasis) and 15 cases of colorectal cancer (3 cases without liver metastasis, 12 cases with liver metastasis). The rate of integrin VLA3 expression in 69 primary gastric and colorectal cancers without liver metastasis was 41%, that was higher than that (0%) in the 19 primary tumors of gastric and colorectal cancers with liver metastasis. In contrast, the positive rate for integrin VLA3 staining in 19 cases involving liver metastasis of gastric and colorectal cancers was 58% (11/19), which was higher than that (0%) in primary tumors. These findings suggest that VLA3 may play an important role in the process of liver metastasis of gastric and colorectal cancers.

Publication Types:
Comparative Study
English Abstract
Review

PMID: 7630007 [PubMed - indexed for MEDLINE]

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

18: Nippon Rinsho. 1995 Jul;53(7):1660-5.


[Integrin expression and ability to adhere to extracellular matrix and endothelial cells in human lung cancers]

[Article in Japanese]

Hirasawa M, Shijubo N, Inuzuka M, Abe S.

Third Department of Internal Medicine, Sapporo Medical University School of Medicine.

Tumor cell interaction with extracellular matrix and endothelial cells constitute the most crucial factor of metastasis. Integrins are one of adhesion molecules which mediate the interaction. Most lung cancers adhered strongly to extracellular matrix corresponding with expression of integrins. Three lung cancers which expressed few or no integrins had very weak ability to adhere to extracellular matrix. Strong binding to endothelial cells was found in most lines but the three lung cancers had very little ability to adhere to endothelial cells. Binding to endothelial cells were strongly inhibited by antibodies to beta-1 subunit. Lung cancers may adhere to extracellular matrix and endothelial cells through integrins, especially the beta-1 subfamily.

Publication Types:
English Abstract
Review

PMID: 7630004 [PubMed - indexed for MEDLINE]

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

19: J Invest Dermatol. 1994 Nov;103(5 Suppl):31S-38S.


Junctional epidermolysis bullosis: defects in expression of epiligrin/nicein/kalinin and integrin beta 4 that inhibit hemidesmosome formation.

Gil SG, Brown TA, Ryan MC, Carter WG.

Department of Cell Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.

Junctional epidermolysis bullosis (JEB) is a heterogeneous inherited blistering disorder of human epithelial basement membranes (BMs). Characteristically, the epidermis detaches from the BM between the basal cells and the lamina lucida due to reduced numbers of hemidesmosomes (HDs). Attempts to identify a candidate gene for JEB led to the characterization of nicein, a protein complex in normal BMs that is absent from BMs of patients with JEB gravis. In independent research, two related BM glycoproteins, epiligrin and kalinin, were identified as functional adhesion components of HDs. Epiligrin was characterized as a BM ligand for basal cell adhesion via integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4 in HDs. Kalinin was characterized as an adhesive ligand and a component of anchoring filaments. Recent antibody and sequence studies on epiligrin/nicein/kalinin have identified limited homologies with laminin. Ongoing studies in multiple laboratories seek to identify mutations in one or more of the three subunits of epiligrin that are causal in JEB gravis. Consistent with the genetic heterogeneity of JEB, we have identified a patient with a variant form of JEB that is associated with pyloric atresia. This patient has negligible HDs, normal epiligrin, but reduced expression of integrin beta 4. A defect in the beta 4 expression may define a subset of JEB cases that also present with pyloric atresia. These results testify to the dual requirements for epiligrin in the BM and integrin beta 4 in the plasma membrane in regulating function of HDs in epithelium.

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

PMID: 7963682 [PubMed - indexed for MEDLINE]

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

20: Nippon Rinsho. 1994 Jun;52(6):1480-5.


[Expression of integrin molecules in sarcoid lesions]

[Article in Japanese]

Shigehara K, Shijubo N, Abe S, Ohmichi M, Hiraga Y.

Dep. of Internal Medicine (Section 3), Sapporo Medical University.

In order to assess the role of adhesion molecules in sarcoid lesions, we examined the expression of integrin families and extracellular matrix proteins by immunohistochemical techniques in sarcoid lymph nodes. Epithelioid cells exhibited intensive expression of ICAM-1, the alpha 5 and the beta 2 molecules. Lymphocytes exhibited intensive expression of ICAM-1, the alpha 4, the alpha 5 and beta 2 molecules. Laminin and type IV collagen were detected at basement membranes in vessels. Fibronectin was distributed within granulomas with a concentric pattern and around granulomas with a fibrillar pattern. Its distribution was well correspondence with the alpha 5 expression. These data suggest that integrin families might play an important role in granuloma formation and migration of lymphocytes into inflamed sarcoid lesions.

Publication Types:
English Abstract
Review

PMID: 8046827 [PubMed - indexed for MEDLINE]
 

Navigate through the articles
Previous article Integrin Function
Copyright © 2007-2008 by Biologicalworld.com