Source:http://www.reactome.org/biopax/48887BiochemicalReaction3244
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Authored: Heldin, CH, Moustakas, A, Huminiecki, L, Jassal, B, 2006-02-02,
Edited: Jassal, B, 2006-03-22 11:41:32,
Reviewed: Heldin, CH, 2006-04-18 14:26:12,
Reviewed: Huang, Tao, 2012-05-14,
The large latent complex (LLC) of TGF-beta-1 (TGFB1) is secreted by exocytosis to the extracellular region. TGF-beta-1 in the LLC cannot interact with the receptors and for this reason we say that it requires "activation". This means release from the LLC. This release is achieved by many mechanisms: proteolytic cleavage of the LTBPs, thrombospondin-1 binding to the LLC, integrin alphaV-beta6 binding to the LLC, reactive oxygen species and low pH. The release of mature dimeric TGF-beta-1 is essentially a mechanical process that demands cleavage and opening of the LLC structure so that the caged mature C-terminal TGF-beta-1 polypeptide is released to reach the receptor.
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Secretion and activation of the latent large complex of TGF-beta-1
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