TGF-beta is capable of producing a variety of effects and virtually all cell types respond to this factor in some way. The inappropriate presence of active TGF-beta1 has been implicated in a variety of pathological conditions Because of the necessity for regulating its activity tightly, TGF-beta is secreted by cells in the form of an inactive complex. This complex consists of TGF-beta1 associated non-covalently with a protein designated the latency associated peptide (LAP).
TGF-beta1 and LAP represent components of a pro-peptide that is cleaved in a post-golgi compartment prior to secretion. LAP and TGF-beta1 each consist of a disulfide-linked homodimer and the association of these two components renders TGF-beta1 inactive and inaccessible to anti-TGF-beta antibodies.
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