Interactions of Type IV Collagen and Its Domains with Human Mesangial Cells

Setty, Suman; Kim, Youngki; Fields, Gregg B.; Clegg, Dennis O.; Wayner, Elizabeth A.; Tsilibary, Effie-Photini C

doi:10.1074/jbc.273.20.12244

Cited by 34 publications

(30 citation statements)

References 51 publications

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“…In addition to the triple-helical part, NC1 domain of collagen IV also promotes cell adhesion (Chelberg et al, 1989;Herbst et al, 1988;Setty et al, 1998), stimulates outgrowth of embryonic neurons (Lein et al, 1991), and inhibits morphogenesis in Hydra vulgaris (Zhang et al, 1994). The latter finding led to the suggestion that NC1 domain could inhibit angiogenesis by disrupting the assembly of vascular basement membrane (Sarras and Hudson, 1997).…”

Section: Integrin Receptorsmentioning

confidence: 97%

“…A synthetic peptide (TAGSCLRKFSTM) corresponding to a sequence from α1(IV) NC1 domain has been shown to promote adhesion and spreading of endothelial cells (Tsilibary et al, 1990). Another heparin-binding peptide, Hep-III (GEFYFDLRLKGDK), derived from the interruption of α1 chain promoted adhesion of keratinocytes and mesangial cells (Setty et al, 1998;Wilke and Furcht, 1990). Interestingly, the same peptide mediates binding of α 3 β 1 integrin and may also interact with α 2 β 1 integrin depending on integrin expression levels (Kim et al, 1994;Setty et al, 1998).…”

Section: Nonintegrin Receptorsmentioning

confidence: 99%

“…This interaction is critical for a variety of biological processes, including cell adhesion, migration, survival, proliferation, and differentiation. Cell culture studies have shown that collagen IV is the binding substrate for a large number of cell types including platelets (Santoro, 1986;Staatz et al, 1990), hepatocytes (Rubin et al, 1981), keratinocytes (Murray et al, 1979), endothelial (Cheng and Kramer, 1989;Herbst et al, 1988), mesangial (Setty et al, 1998), pancreatic (Kaido et al, 2004), and tumor cells such as breast and prostate carcinoma (Abecassis et al, 1987;Dedhar et al, 1993), melanoma (Chelberg et al, 1989), fibrosarcoma, and glioma (Aumailley and Timpl, 1986;Knight et al, 2000). Cell attachment to collagen IV is mediated by multiple binding sites within both triple-helical and NC1 domains, suggesting involvement of several adhesion receptors (Chelberg et al, 1989;Herbst et al, 1988;Wayner and Carter, 1987).…”

Section: Interaction To Cell Surface Receptorsmentioning

confidence: 99%

“…Another heparin-binding peptide, Hep-III (GEFYFDLRLKGDK), derived from the interruption of α1 chain promoted adhesion of keratinocytes and mesangial cells (Setty et al, 1998;Wilke and Furcht, 1990). Interestingly, the same peptide mediates binding of α 3 β 1 integrin and may also interact with α 2 β 1 integrin depending on integrin expression levels (Kim et al, 1994;Setty et al, 1998). However, the degree of cell spreading on Hep-III is significantly lower than on full-length type IV collagen or its triple-helical domain, and Hep-III only partially inhibited cell motility on collagen IV, indicating rather limited contribution of proteoglycans to mechanisms of cell adhesion and migration.…”

Section: Nonintegrin Receptorsmentioning

confidence: 99%

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Mammalian collagen IV

Khoshnoodi

Pedchenko

Hudson

2008

Microscopy Res & Technique

555

487

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Four decades have passed since the first discovery of collagen IV by Kefalides in 1966. Since then collagen IV has been investigated extensively by a large number of research laboratories around the world. Advances in molecular genetics have resulted in identification of six evolutionary related mammalian genes encoding six different polypeptide chains of collagen IV. The genes are differentially expressed during the embryonic development, providing different tissues with specific collagen IV networks each having unique biochemical properties. Newly translated α-chains interact and assemble in the endoplasmic reticulum in a chain-specific fashion and form unique heterotrimers. Unlike most collagens, type IV collagen is an exclusive member of the basement membranes and through a complex inter-and intramolecular interactions form supramolecular networks that influence cell adhesion, migration, and differentiation. Collagen IV is directly involved in a number of genetic and acquired disease such as Alport's and Goodpasture's syndromes. Recent discoveries have also highlighted a new and direct role for collagen IV in the development of rare genetic diseases such as cerebral hemorrhage and porencephaly in infants and hemorrhagic stroke in adults. Years of intensive investigations have resulted in a vast body of information about the structure, function, and biology of collagen IV. In this review article, we will summarize essential findings on the structural and functional relationships of different collagen IV chains and their roles in health and disease.

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Section: Integrin Receptorsmentioning

confidence: 97%

Section: Nonintegrin Receptorsmentioning

confidence: 99%

Section: Interaction To Cell Surface Receptorsmentioning

confidence: 99%

Section: Nonintegrin Receptorsmentioning

confidence: 99%

See 2 more Smart Citations

Mammalian collagen IV

Khoshnoodi

Pedchenko

Hudson

2008

Microscopy Res & Technique

555

487

View full text Add to dashboard Cite

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“…Additional integrins, such as ␣ 3 ␤ 1 , that bind the triple-helical domain may be involved (12,13). The NC1 domain was initially characterized as a ligand for ␣ 1 ␤ 1 and ␣ 2 ␤ 1 integrins in human mesangial cells (4), and binding of ␣ 1 ␤ 1 integrin to recombinant ␣1NC1 was later confirmed (14). In contrast, recombinant ␣2NC1 was identified as a novel ligand for a different subset of integrins (␣ v ␤ 3 , ␣ v ␤ 5 , and ␣ 3 ␤ 1 ) in endothelial cells, suggesting the existence of a non-RGD-binding motif (15).…”

mentioning

confidence: 99%

αvβ3 and αvβ5 Integrins Bind Both the Proximal RGD Site and Non-RGD Motifs within Noncollagenous (NC1) Domain of the α3 Chain of Type IV Collagen

Pedchenko

Zent

Hudson

2004

Journal of Biological Chemistry

101

103

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The NC1 domains of human type IV collagen, in particular ␣3NC1, are inhibitors of angiogenesis and tumor growth (Petitclerc, E., Boutaud, A., Prestayko, A., Xu, J., Sado, Y., Ninomiya, Y., Sarras, M. P., Jr., Hudson, B. G., and Brooks, P. C. (2000) J. Biol. Chem. 275, 8051-8061). The recombinant ␣3NC1 domain contained a RGD site as part of a short collagenous sequence at the N terminus, designated herein as RGD-␣3NC1. Others, using synthetic peptides, have concluded that this RGD site is nonfunctional in cell adhesion, and therefore, the antiangiogenic activity is attributed exclusively to ␣ v ␤ 3 integrin interactions with non-RGD motifs of the RGD-␣3NC1 domain (Maeshima, Y., Colorado, P. C., and Kalluri, R. (2000) J. Biol. Chem. 275, 23745-23750). This nonfunctionality is surprising given that RGD is a binding site for ␣ v ␤ 3 integrin in several proteins. In the present study, we used the ␣3NC1 domain with or without the RGD site, expressed in HEK 293 cells for native conformation, as an alternative approach to synthetic peptides to assess the functionality of the RGD site and non-RGD motifs. Our results demonstrate a predominant role of the RGD site for endothelial adhesion and for binding of ␣ v ␤ 3 and ␣ v ␤ 5 integrins. Moreover, we demonstrate that the two non-RGD peptides, previously identified as the ␣ v ␤ 3 integrin-binding sites of the ␣3NC1 domain, are 10-fold less potent in competing for integrin binding than the native protein, indicating the importance of additional structural and/or conformational features of the ␣3NC1 domain for integrin binding. Therefore, the RGD site, in addition to non-RGD motifs, may contribute to the mechanisms of endothelial cell adhesion in the human vasculature and the antiangiogenic activity of the RGD-␣3NC1 domain.Type IV collagen is the major constituent of basement membranes, a specialized form of extracellular matrix underlying all epithelia, that compartmentalizes tissues and provides molecular signals for influencing cell behavior. The type IV collagen family is comprised of six ␣-chains (␣1-␣6) that assemble into three kinds of triple-helical protomers of different chain composition. Each protomer has three functional domains: a 7 S domain at the N terminus, a long triple-helical collagenous domain in the middle of the molecule, and a trimeric noncollagenous (NC1) domain at the C terminus. Protomers selfassemble into networks by end-to-end associations that connect four 7 S domains at one end and connect two NC1 trimeric domains at the other end, forming an NC1 hexamer configuration (1). Three types of networks are known: an ␣1⅐␣1⅐␣2 network, present in the basement membranes of all tissues and animal phyla and ␣3⅐␣4⅐␣5 and ␣1⅐␣2⅐␣5.␣6 networks that have a restricted tissue distribution. These networks are essential for tissue development and function. They provide mechanical stability, a scaffold for assembly of other macromolecular components, and act as a ligand for integrins, receptors that mediate cell adhesion, migration, growth, and differentiation.Cell ...

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Complement 3 is involved in changing the phenotype of human glomerular mesangial cells

Wan

Fukuda

Endo

et al. 2007

Journal Cellular Physiology

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Complement activation contributes to tissue injury in various forms of glomerulopathy and is characterized by deposition of complement components, which accelerates the progression of chronic renal damage. We recently reported that complement 3 (C3), a critical component of the complement system, is associated with the synthetic phenotype of vascular smooth muscle cells. It is possible that C3 stimulates mesangial cells to assume the synthetic phenotype to, in turn, induce glomerular injury and sclerosis. We investigated the role of C3 in the growth and phenotype of mesangial cells. Cultured human mesangial cells (HMCs) expressed C3 mRNA and protein, and levels were increased in response to IFN-g and TNF-a. HMCs also expressed C3a receptor mRNA and protein. Exogenous C3a stimulated DNA synthesis in HMCs in a dose-dependent manner. C3a decreased expression h-caldesmon mRNA, a marker of the contractile phenotype, and increased the expression of osteopontin, matrix Gla, and collagen type1 a1 (collagen IV) mRNAs, which are markers of the synthetic phenotype. C3a decreased expression of a-smooth muscle actin in HMCs. Small interfering RNA (siRNA) targeting C3 reduced the DNA synthesis and proliferation of HMCs, increased expression of h-caldesmon mRNA, and decreased expression of osteopontin, matrix Gla, and collagen IV mRNAs in HMCs. These results indicate that C3 causes HMCs to convert to the synthetic phenotype and stimulates growth of mesangial cells, suggesting that C3 may play an important role in phenotypic regulation of mesangial cells in renal diseases.

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Interactions of Type IV Collagen and Its Domains with Human Mesangial Cells

Cited by 34 publications

References 51 publications

Mammalian collagen IV

Mammalian collagen IV

αvβ3 and αvβ5 Integrins Bind Both the Proximal RGD Site and Non-RGD Motifs within Noncollagenous (NC1) Domain of the α3 Chain of Type IV Collagen

Complement 3 is involved in changing the phenotype of human glomerular mesangial cells

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