Identification of a multifunctional, cell-binding peptide sequence from the a1(NC1) of type IV collagen.

Tsilibary, Effie C.; Reger, Lorrel A.; Vogel, Ann M.; Koliakos, George; Anderson, Shane S.; Charonis, Aristidis S.; Alegre, John N.; Furcht, Leo T.

doi:10.1083/jcb.111.4.1583

Cited by 47 publications

(34 citation statements)

References 36 publications

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“…In addition, three heparin-binding sequences have also been found in the triple-helical and NC1 domains of α1(IV) and α2(IV) chains (Koliakos et al, 1989). 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).…”

Section: Nonintegrin Receptorsmentioning

confidence: 99%

Mammalian collagen IV

Khoshnoodi

Pedchenko

Hudson

2008

Microscopy Res & Technique

569

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: Nonintegrin Receptorsmentioning

confidence: 99%

Mammalian collagen IV

Khoshnoodi

Pedchenko

Hudson

2008

Microscopy Res & Technique

569

487

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“…Studies have found that the cleavage sites also overlap with many integrin binding domains such as α 1 β 1 , resulting in the availability of α v β 3 integrin binding sites known to promote neutrophil binding [115,118]. Collagen IV networks are highly adhesive to all cells types except erythrocytes [115,119]. Furthermore, cell binding has been found to be enhanced in the presence of various ECM molecules such as perlecan, SPARC, and von Willebrand factor (vWF) [115,118,119].…”

Section: The Basement Membrane Supports Valve Endothelial Cells and Amentioning

confidence: 99%

Extracellular Matrix Organization, Structure, and Function

Wiltz¹,

Arevalos²,

Balaoing³

et al. 2013

Calcific Aortic Valve Disease

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“…This proteolyzed collagen fragment is likely liberated from the basement membranes of the kidney, lung, and testis, which contain abundant amounts of the α3 chain containing type IV collagen. VBM organization is dependent on the assembly of a type IV collagen network, which is believed to occur through the carboxy-terminal NC1 domain (Madri and Pratt 1986;Tsilibary et al 1990;Zhang et al 1994;Timpl 1996;Madri 1997;Zeisberg et al 2001). Type IV collagen is one of the major macromolecular constituents of all mam-…”

Section: Tumstatinmentioning

confidence: 99%