Abstract
Transforming growth factors-beta (TGFbeta1, 2 and 3) are secreted in a complex with their propeptides (latency-associated peptide 1 (LAP1), 2 and 3). TGFbeta signaling requires the dissociation of LAP and TGFbeta, a process termed latent TGFbeta activation. This process is a critical but incompletely understood step in the regulation of TGFbeta function. In particular, the extent to which activation mechanisms differ among the three TGFbeta isoforms is relatively unexplored. We show here that alphaVbeta6 binds and activates latent TGFbeta3.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antigens, Neoplasm*
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Cell Line
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Gene Deletion
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Integrins / metabolism*
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Ligands
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Mice
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Mink
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Oligopeptides / genetics
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Oligopeptides / metabolism
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Protein Binding
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Protein Isoforms / pharmacology
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Proteins / metabolism
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Substrate Specificity
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TNF Receptor-Associated Factor 2
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Transfection
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Transforming Growth Factor beta / chemistry
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Transforming Growth Factor beta / genetics
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Transforming Growth Factor beta / metabolism*
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Transforming Growth Factor beta / pharmacology
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Transforming Growth Factor beta1
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Transforming Growth Factor beta3
Substances
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Antigens, Neoplasm
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Integrins
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Ligands
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Oligopeptides
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Protein Isoforms
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Proteins
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TNF Receptor-Associated Factor 2
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Tgfb1 protein, mouse
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Tgfb3 protein, mouse
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Transforming Growth Factor beta
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Transforming Growth Factor beta1
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Transforming Growth Factor beta3
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integrin alphavbeta6
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arginyl-glycyl-aspartic acid