Human TGF-β2 consists of two disulfide-linked, identical subunits, and displays 71.4% sequence homology with TGF-β1. TGF-β2 is synthesized in cells as a 442 amino acid. Furin cleaves the protein, yielding an N-terminal cleavage product which corresponds to latency-associated peptide (LAP), and the 25 kD C-terminal portion of the precursor constitutes the mature TGF-β2. TGF-β activators can release TGF-β from LAP. These activators include proteases that degrade LAP, thrombospondin-1, reactive oxygen species, and integrins avb6 and avb8. TGF-β2 is the predominant form of TGF-β in ocular tissues, and elevated levels of TGF-β2 have been found in the aqueous humor of patients with primary open-angle glaucoma (POAG), a major cause of blindness worldwide. There is an accumulation of extracellular matrix (ECM) in the trabecular meshwork (TM) of glaucoma patients, and TGF-β2 seems to be responsible for this ECM increase. It has been identified that bone morphogenetic protein-4 and 7 (BMP4, BMP7) are potent antagonists of the fibrogenic effects of TGF-β2 on human TM cells. Smad7 seems to participate in the antagonistic effect of BMP7 on TGF-β2 signaling.