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Background
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TGF-β 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-β1 has been implicated in a variety of pathological conditions Because of the necessity for regulating its activity tightly, TGF-β is secreted by cells in the form of an inactive complex. This complex consists of TGF-β1 associated non-covalently with a protein designated the latency associated peptide (LAP). TGF-β1 and LAP represent components of a pro-peptide that is cleaved in a post-golgi compartment prior to secretion. LAP and TGF-β1 each consist of a disulfide-linked homodimer and the association of these two components renders TGF-β1 inactive and inaccessible to anti-TGF-β antibodies. In many instances in vivo, associated LAP and TGF-β, called the small latent TGF-β complex, are bound to an additional protein designated the latent TGF-β1 binding protein (LTBP), forming the large latent TGF-β1 complex. The mechanisms by which active TGF-β1 is released from these latent complexes represent important control steps for the regulation of the numerous effects of TGF-β1. Despite considerable study, these mechanisms are not well understood.
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Pathways
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EGFR Signaling Pathway, Dopaminergic Neurogenesis, Cellular Response to Molecule of Bacterial Origin, Glycosaminoglycan Metabolic Process, Regulation of Leukocyte Mediated Immunity, Regulation of Muscle Cell Differentiation, Positive Regulation of Immune Effector Process, Cell-Cell Junction Organization, Production of Molecular Mediator of Immune Response, Ribonucleoside Biosynthetic Process, Skeletal Muscle Fiber Development, Regulation of Carbohydrate Metabolic Process, Protein targeting to Nucleus, Autophagy
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