Mouse Serine Protease HTRA1, HTRA1 ELI

Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin.

HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production.

May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin.

Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space.

Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins.

Inhibits signaling mediated by TGF-beta family members.

This activity requires the integrity of the catalytic site, but it is unclear whether it leads to the proteolytic degradation of TGF-beta proteins themselves (PubMed:18551132) or not (PubMed:14973287). By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development.

Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.