Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains (Q24338782)

cell adhesion mediated by integrin

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

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Johannes A Eble

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Anja Kassner

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Stephan Niland

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Joachim Grifka

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Susanne Grässel

Journal of Biological Chemistry

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language of work or name

English

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publication date

1 September 2006

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published in

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volume

281

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issue

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page(s)

25745-56

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cites work

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Cloning and chromosomal location of human alpha 1(XVI) collagen

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Discrete integration of collagen XVI into tissue-specific collagen fibrils or beaded microfibrils

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Type VII collagen gene expression by cultured human cells and in fetal skin. Abundant mRNA and protein levels in epidermal keratinocytes

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The collagen receptor integrins have distinct ligand recognition and signaling functions

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Isolation, cloning, and sequence analysis of the integrin subunit alpha10, a beta1-associated collagen binding integrin expressed on chondrocytes

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alpha11beta1 integrin is a receptor for interstitial collagens involved in cell migration and collagen reorganization on mesenchymal nonmuscle cells

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Deletion of integrin alpha 1 by homologous recombination permits normal murine development but gives rise to a specific deficit in cell adhesion.

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Integrin-mediated preadipocyte adhesion and migration on laminin-1.

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Role of integrins in regulating epidermal adhesion, growth and differentiation

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The alpha2beta1 integrin inhibitor rhodocetin binds to the A-domain of the integrin alpha2 subunit proximal to the collagen-binding site

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Molecular structure and interaction of recombinant human type XVI collagen

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alpha 2beta 1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen

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Interaction of type IV collagen with the isolated integrins alpha 1 beta 1 and alpha 2 beta 1

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Recombinant soluble human alpha 3 beta 1 integrin: purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner

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Prolyl hydroxylation of collagen type I is required for efficient binding to integrin alpha 1 beta 1 and platelet glycoprotein VI but not to alpha 2 beta 1.

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A monoclonal antibody against an activation epitope on mouse integrin chain beta 1 blocks adhesion of lymphocytes to the endothelial integrin alpha 6 beta 1

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Identification in collagen type I of an integrin alpha2 beta1-binding site containing an essential GER sequence

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Multiple binding sites in collagen type I for the integrins alpha1beta1 and alpha2beta1.

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Monoclonal antibodies identify residues 199-216 of the integrin alpha2 vWFA domain as a functionally important region within alpha2beta1.

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The fibril-associated collagen IX provides a novel mechanism for cell adhesion to cartilaginous matrix

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There is binding of collagen IV to beta 1 integrin during early skin basement membrane assembly.

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The A-Domain of Integrin alpha2 Binds Specifically to a Range of Collagens but is not a General Receptor for the Collagenous Motif

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The Integrin α1 A-domain Is a Ligand Binding Site for Collagens and Laminin

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The spatial orientation of the essential amino acid residues arginine and aspartate within the alpha1beta1 integrin recognition site of collagen IV has been resolved using fluorescence resonance energy transfer

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inferred from DOI database lookup

7 January 2021

based on heuristic

Collagen XVI is expressed by human dermal fibroblasts and keratinocytes and is associated with the microfibrillar apparatus in the upper papillary dermis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M509942200