Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Kern, Andreas; Eble, Johannes A.; Golbik, Ralph; Kühn, Klaus

doi:10.1111/j.1432-1033.1993.tb18017.x

Cited by 199 publications

(208 citation statements)

References 47 publications

Supporting

Mentioning

188

Contrasting

Unclassified

Order By: Relevance

“…These two integrins bind both collagen IV and collagen I, however, with distinct specificity as follows: integrin α 1 β 1 has a higher affinity for collagen IV, while α 2 β 1 binds stronger to collagen I (Kern et al, 1993;Tulla et al, 2001a). It was shown that deletion of α 1 β 1 integrin by the homologous recombination resulted in dramatic decrease in adhesion and migration of fibroblasts and smooth muscle cells to collagen IV substrate (Gardner et al, 1996), while the importance of α 2 β 1 integrin was demonstrated by the decrease of adhesion and morphogenesis on collagen IV after using antisense mRNA (Keely et al, 1995).…”

Section: Integrin Receptorsmentioning

confidence: 99%

“…By affinity chromatography using immobilized CB3 fragments and cellular lysates, α 1 β 1 and α 2 β 1 were isolated as the only integrins eluted from the affinity column (Vandenberg et al, 1991). Using purified integrins and shorter tryptic fragments of CB3, one binding site for α 1 β 1 integrin and two for α 2 β 1 integrin were located in different but adjacent positions on CB3 fragment (Kern et al, 1993). Further refinement of the α 1 β 1 recognition site was achieved by digestion of one of the tryptic peptides with thermolysin .…”

Section: Integrin Receptorsmentioning

confidence: 99%

See 1 more Smart Citation

Mammalian collagen IV

Khoshnoodi

Pedchenko

Hudson

2008

Microscopy Res & Technique

554

504

View full text Add to dashboard Cite

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.

show abstract

Section: Integrin Receptorsmentioning

confidence: 99%

Section: Integrin Receptorsmentioning

confidence: 99%

Mammalian collagen IV

Khoshnoodi

Pedchenko

Hudson

2008

Microscopy Res & Technique

554

504

View full text Add to dashboard Cite

show abstract

“…EHS, Engelbreth-Holm-Swarm. Kern et al, 1993), and a3pl Sonnenberg et al, 1991). EHS tumor laminin-1 also possesses a cryptic RGD site which is recognized by pl and p3 integrins, although their corresponding a chains have not been firmly identified (Aumailley et al, 1990b;1991).…”

mentioning

confidence: 99%

Binding of Purified Collagen Receptors (α1β1, α2β1) and RGD‐Dependent Integrins to Laminins and Laminin Fragments

Pfaff

Göhring

Brown

et al. 1994

European Journal of Biochemistry

View full text Add to dashboard Cite

Integrins alp1 and a2/3l, when purified by collagen affinity chromatography, showed distinct binding to mouse tumor laminin-1, which has the chain composition alplyl. The binding was, however, about 10-fold lower than to collagen IV. Only little (alpl) or no binding (a2pl) was observed to two different laminin isoforms (a2ply1, a2p2yl) from human placenta. Binding to laminin-1 was abolished by EDTA and could be specifically inhibited by antibodies to the respective integrin a subunit. These antibodies also inhibited cell adhesion to collagens. The binding of soluble integrins was weaker than that of immobilized integrins but could be enhanced by an activating anti@ integrin). No enhancement was observed for immobilized integrins. Studies with laminin-1 fragments demonstrated lack of binding to the major cell-adhesive fragment E8 from the long arm, fragments E3 and E4, involved in heparin-binding and self-assembly, respectively, and fragment P1, corresponding to the inner segments of the short arms. A larger short-arm fragment (ElXNd), which lacks the N-terminal pl chain domains V and VI, was as active as laminin. Together, these results, suggested the localization of the binding sites for alp1 and a2pl to the N-terminal region of the laminin a1 chain. Fragment P1 but not intact laminin-1 bound to aVp3 integrin in an EDTA-sensitive and RGD-sensitive manner, underscoring previous data on the cryptic nature of the RGD site in laminin-1. Further analyses by surface plasmon resonance assays demonstrated a KD = 50 nM for a2plllaminin-1 bindmg and a KD = 450 nM for aVp3lfragment P1 binding and confirmed the antipl-mediated increase in affinity for a2pl.

show abstract

“…6 -8). Five laminin-binding integrins of the ␤1 family recognize different sites and isoforms of laminin: ␣6␤1 (9, 10) and ␣7␤1 (11,12) bind to laminin-1, recognizing specifically the E8 domain; ␣1␤1 binds to a cryptic site in the E1 region of laminin (13), but also to types I and IV collagen (14). The ␣3␤1 integrin binds to laminin-5 (kalinin) (15) and to other matrix proteins; ␣2␤1 is predominantly a collagen receptor (16), but when isolated from endothelial cells it also binds to laminin-1 (17).…”

mentioning

confidence: 99%

Specific Induction of Cell Motility on Laminin by α7 Integrin

Echtermeyer

Schober

Pöschl

et al. 1996

Journal of Biological Chemistry

View full text Add to dashboard Cite

Laminin, the major glycoprotein of basement membranes, actively supports cell migration in development, tissue repair, tumor growth, metastasis, and other pathological processes. Previously we have shown that the locomotion of murine skeletal myoblasts is specifically and significantly enhanced on laminin but not on other matrix proteins. One of the major laminin receptors of myoblasts is the ␣7␤1 integrin, which was first described in human MeWo melanoma cells and Rugli glioblastoma cells. In order to investigate and directly test the role of the ␣7 integrin in cell migration on laminin, we expressed the murine ␣7B splice variant in human 293 kidney cells and 530 melanoma cells which cannot migrate on laminin and are devoid of endogenous ␣7. Northern blotting of the transfected cells showed that the ␣7 mRNA was expressed efficiently, and the protein was detected on the cell surface by immunofluorescence and fluorescence-activated cell sorter analysis. Cell motility measurements by computer-assisted time-lapse videomicroscopy of the ␣7-transfected cells revealed an 8 -10-fold increase in motility on laminin-1 and its E8 fragment, but not on fibronectin. Mock-transfected cells did not migrate significantly on laminin or on fibronectin. Similarly, transmigration of ␣7-transfected 293 cells through laminin-coated filters in a Boyden chamber assay was significantly enhanced in comparison to mocktransfected cells. These findings prove that ␣7 integrin expression confers a gain of function-motile phenotype to immobile cells and may be responsible for transduction of the laminin-induced cell motility.Cells utilize extracellular matrix to migrate during embryonic development, tissue regeneration, and invasion of tissues in inflammation and tumor metastasis (reviewed in Ref. 1). Laminin-1, a major glycoprotein of basement membranes, has been shown to promote migration of different cell types including neural crest cells (2), skeletal myoblasts (3), or B16 mouse melanoma cells (4). The mechanism of laminin-induced cell locomotion and the cellular receptors mediating the locomotor signals are, however, not known. Integrin-and non-integrin receptors are involved in the specific adhesion of cells to laminin. Dystroglycan, a 156-kDa protein forms a transmembrane linkage together with other proteins between laminin-2 and dystrophin in the muscle cell membrane (5); a high affinity laminin receptor of 67 kDa has been isolated from several tumor cells, myoblasts, and other primary cells (for reviews, see Refs. 6 -8). Five laminin-binding integrins of the ␤1 family recognize different sites and isoforms of laminin: ␣6␤1 (9, 10) and ␣7␤1 (11, 12) bind to laminin-1, recognizing specifically the E8 domain; ␣1␤1 binds to a cryptic site in the E1 region of laminin (13), but also to types I and IV collagen (14). The ␣3␤1 integrin binds to laminin-5 (kalinin) (15) and to other matrix proteins; ␣2␤1 is predominantly a collagen receptor (16), but when isolated from endothelial cells it also binds to laminin-1 (17).While much has been publi...

show abstract

Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Cited by 199 publications

References 47 publications

Mammalian collagen IV

Mammalian collagen IV

Binding of Purified Collagen Receptors (α1β1, α2β1) and RGD‐Dependent Integrins to Laminins and Laminin Fragments

Specific Induction of Cell Motility on Laminin by α7 Integrin

Contact Info

Product

Resources

About