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• W2075965099 abstract "Epiligrin is a new glycoprotein in most epithelial basement membranes (BMs) and is a ligand for cell adhesion via integrin α3β1. In the extracellular matrix of human foreskin keratinocytes (HFKs), epiligrin contains three disulfide-bonded, glycoprotein subunits, E170, E145, and E135, based on molecular size in kilodaltons. Epiligrin, immunopurified with MAb P1E1, induced cell adhesion and localization of integrin α3β1 in focal adhesions (FAs). Cell adhesion to epiligrin was inhibited with an anti-α3β1 MAb. Epiligrin also colocalized with integrin α6β4 in hemidesmosome-like stable anchoring contacts (SACs). α3β1-FAs encircled α6β4-SACs in a complex adhesion structure. α3β1 and epiligrin localized in BM junctions of epithelial cells primarily in organs of endodermal/ectodermal origin. In epidermis, epiligrin was detected in the lamina lucida of BMs. α3β1 localized in plasma membranes of basal cells in contact with epiligrin and also in lateral/apical membranes. Epiligrin is the ligand of an adhesion super complex composed of α3β1-FAs and α6β4-SACs (hemidesmosomes)." @default.
• W2075965099 created "2016-06-24" @default.
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• W2075965099 date "1991-05-01" @default.
• W2075965099 modified "2023-10-14" @default.
• W2075965099 title "Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes" @default.
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• W2075965099 doi "https://doi.org/10.1016/0092-8674(91)90092-d" @default.
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