VLA‐2 is a collagen receptor on endothelial cells

OʼConnell, P J.; Faull, Randall J.; Russ, Graeme R.; d’Apice, Anthony J.F.

doi:10.1038/icb.1991.16

Cited by 16 publications

(8 citation statements)

References 19 publications

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“…44G4 recognizes endoglin [8 12]. RM2.I84 recognizes a polymorphism of CDl Ib [16] atid RMACll reeognizes CDw49b [17] and were used as negative controls.…”

Section: Monoclonal Antibodiesmentioning

confidence: 99%

Endoglin: a 180-kD endothelial cell and macrophage restricted differentiation molecule

OʼConnell

McKenzie

Fisicaro

et al. 1992

Clinical and Experimental Immunology

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SUMMARYA MoAb RMAC8 was generated by immunizing Balb/c mice with cultured human umbilical vein endothelial cells (HUVE). The molecule recognized had a mol. wt of 180 kD non-reduced, 95 kD after reduction and 66 kD in its reduced and N-deglycosylated form. Sequential immunoprecipitation studies with the MoAb 44G4, which recognizes the o-and N-glycosylated homodimer endoglin, showed that both MoAbs recognize the same molecule on HUVE and phorbol myristate acetate (PMA)-stimulated U937 cells. The distribution of the RMAC8-recognized molecule was the same as that described for endoglin, i.e. arterial and venous endothelium, myelomonocytic and pre-B leukaemia cells and cell lines; however, unlike 44G4, RMAC8 also reacted weakly with monocytes and strongly with in vitro differentiated macrophages as well as peritoneal and alveolar macrophages. This distribution of endoglin was confirmed by Northern blot analysis using a full length endoglin cDNA probe. These studies suggest that endoglin is a differentiation marker on macrophages.

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“…44G4 recognizes endoglin [8 12]. RM2.I84 recognizes a polymorphism of CDl Ib [16] atid RMACll reeognizes CDw49b [17] and were used as negative controls.…”

Section: Monoclonal Antibodiesmentioning

confidence: 99%

Endoglin: a 180-kD endothelial cell and macrophage restricted differentiation molecule

OʼConnell

McKenzie

Fisicaro

et al. 1992

Clinical and Experimental Immunology

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“…Anti-human ␣2 MAbs AK7 (33,65), which (according to flow cytometry results) binds MA104 cell surfaceexpressed ␣2␤1 integrin (17,57) and blocks SA11 infection of MA104 cells by 50 to 60% at 12 to 40 g/ml (17), and P1E6 were purchased from Pharmingen, San Diego, Calif., and Invitrogen, Burwood, Victoria, Australia, respectively. Antihuman ␣2 MAb 12F1 and anti-␤1 MAb B3B11 were purchased from Chemicon, Temecula, Calif. Purified anti-human ␣2 MAbs HAS3 and HAS4 were provided by F. Watt, Imperial Cancer Research Fund, London, England.…”

Section: Methodsmentioning

confidence: 99%

Monkey Rotavirus Binding to α2β1 Integrin Requires the α2 I Domain and Is Facilitated by the Homologous β1 Subunit

Londrigan

Graham

Takada

et al. 2003

J Virol

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Rotaviruses utilize integrins during virus-cell interactions that lead to infection. Cell binding and infectionby simian rotavirus SA11 were inhibited by antibodies (Abs) to the inserted (I) domain of the ␣2 integrin subunit. To determine directly which integrins or other proteins bind rotaviruses, cell surface proteins precipitated by rotaviruses were compared with those precipitated by anti-␣2␤1 Abs. Two proteins precipitated by SA11 and rhesus rotavirus RRV from MA104 and Caco-2 cells migrated indistinguishably from ␣2␤1 integrin, and SA11 precipitated ␤1 from ␣2␤1-transfected CHO cells. These viruses specifically precipitated two MA104 cell proteins only, but an additional 160-to 165-kDa protein was precipitated by SA11 from Caco-2 cells. The role of the ␣2 I domain in rotavirus binding, infection, and growth was examined using CHO cell lines expressing wild-type or mutated human ␣2 or ␣2␤1. Infectious SA11 and RRV, but not human rotavirus Wa, specifically bound CHO cell-expressed human ␣2␤1 and, to a lesser extent, human ␣2 combined with hamster ␤1. Binding was inhibited by anti-␣2 I domain monoclonal Abs (MAbs), but not by non-I domain MAbs to ␣2, and required the presence of the ␣2 I domain. Amino acid residues 151, 221, and 254 in the metal ion-dependent adhesion site of the ␣2 I domain that are necessary for type I collagen binding to ␣2␤1 were not essential for rotavirus binding. Rotavirus-␣2␤1 binding led to increased virus infection and RRV growth. SA11 and RRV require the ␣2 I domain for binding to ␣2␤1, and their binding to this integrin is distinguishable from that of collagen.Virus attachment and entry into host cells are multistep processes that influence cellular tropism and can involve sequential recognition of multiple receptors and coreceptors. Rotaviruses, a genus within the Reoviridae family, cause severe gastroenteritis following infection of intestinal enterocytes. The virus spike protein, VP4, which is a major determinant of tropism and receptor binding (4,20,51,58), is proteolytically cleaved by trypsin into VP5* and VP8*, which increases the virus infectivity and internalization rate (1,14,28,29). Several glycoconjugates have been implicated in rotavirus attachment (4,5,22,32,38,42,68,74,84). Although a minority of animal rotaviruses, including simian strains SA11 and RRV, can utilize terminal sialic acids (SA) as receptors (12, 13, 22, 32), SA are not essential for infectivity (63). SA-using porcine rotaviruses OSU and CRW-8 appear to use ganglioside-and glycolipid-based receptors, respectively (43, 68). RRV binds sialosides with low affinity via a galectin-like region in VP8* (24,25).In searching for rotavirus receptors, Coulson et al. found that VP4 and rotavirus outer capsid protein VP7 contain sequences corresponding to integrin recognition sites (17). Integrins are ␣/␤ heterodimeric, transmembrane glycoproteins important for cell surface adhesion and signaling. The RDGE sequence in VP4 at amino acids (aa) 307 to 310 corresponds to the putative ␣2␤1 integrin recognition sequence ...

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“…Given the large distance between the major binding locations of a3 and a6 (a chain long arm) and peptide A on the laminin 1 molecule (see Figure 2), it is unlikely that peptide A is inhibiting interaction with these integrins. Two further integrin a types have been described which can bind to both laminin 1 and collagens, al and a2 [17,[39][40][41]. There is ample evidence in the literature for abundant expression of a2 integrin on HUVECs in culture, and for a major role of this integrin in attachment of these cells to laminin 1 and collagen [17,35,40,42,43].…”

Section: Discussionmentioning

confidence: 99%

“…D'Apice, Department of Nephrology, Royal Melbourne Hospital, Melbourne, Australia. This IgG2a mAb was raised against the a2,1 integrin of human umbilical vein endothelial cells (HUVECs) and recognizes the a2 subunit [17].…”

Section: Experimental Materialsmentioning

confidence: 99%

Evidence for the location of a binding sequence for the α2β1 integrin of endothelial cells, in the β1 subunit of laminin

Underwood

Bennett

Kirkpatrick

et al. 1995

Biochemical Journal

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To date no specific location on laminin 1 for the binding of alpha 2 beta 1 integrin has been described, although recent evidence supports a location in the E1XNd fragment of the cross region. We have identified a peptide sequence from this region, in the beta 1 chain of laminin 1, YGYYGDALR, which inhibits the adhesion of endothelial cells to laminin 1 and type-IV collagen. A structurally related sequence from the CNBr-cleaved fragment CB3 of the alpha 1 chain of collagen type IV, FYFDLR, inhibits endothelial cell adhesion to both collagen types I and IV and laminin 1. The CB3 fragment containing the FYFDLR sequence has been shown to contain binding sites for both alpha 1 beta 1 and alpha 2 beta 1 integrins. Present experiments with anti-integrin antibodies indicate that the alpha 2 beta 1 integrin on endothelial cells can account for all the cell binding to collagen types I and IV, and that this integrin makes a major contribution towards the adhesion of these cells to laminin 1. We therefore propose that the peptide FYFDLR participates in alpha 2 beta 1 binding to collagen type IV and that the putatively structurally similar peptide, YGYYGDALR, participates in alpha 2 beta 1 binding to laminin 1. This is the first account of structurally related peptide sequences from laminin 1 and type-IV collagen which show reciprocal inhibition of cell adhesion to either ligand and which might form part of a common integrin-binding site, as well as the first suggestion of a precise location contributing to the alpha 2 beta 1 integrin binding site on laminin 1.

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VLA‐2 is a collagen receptor on endothelial cells

Cited by 16 publications

References 19 publications

Endoglin: a 180-kD endothelial cell and macrophage restricted differentiation molecule

Endoglin: a 180-kD endothelial cell and macrophage restricted differentiation molecule

Monkey Rotavirus Binding to α2β1 Integrin Requires the α2 I Domain and Is Facilitated by the Homologous β1 Subunit

Evidence for the location of a binding sequence for the α2β1 integrin of endothelial cells, in the β1 subunit of laminin

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