Thrombospondin type-1 domain-containing protein 4 (THSD4)

Thrombospondin type-1 domain-containing protein 4 (THSD4) is a secreted, non-enzymatic glycoprotein of the ADAMTS-like (ADAMTSL) family that functions as a key extracellular matrix (ECM) structural constituent. THSD4 physically interacts with fibrillin-1, facilitating microfibril assembly crucial for tissue elasticity and integrity in organs such as the aorta, skin, and bone. It plays roles in pulmonary physiology, bone mass regulation, and is implicated as a modulator in the tumor microenvironment of colorectal cancer, restraining TGF-β signaling and cancer metastasis. In the skin, THSD4 supports hair growth by mediating interactions between the dermal papilla and hair matrix, playing a central role in age-related ECM remodeling. Mutations in THSD4 are associated with familial thoracic aortic aneurysm, aortic dissection, and may influence susceptibility to osteoporosis and cancer progression[1][2][3][4][5].

Other names

ADAMTS-like protein 6ADAMTSL-6ADAMTSL6A disintegrin and metalloproteinase with thrombospondin motifs-like protein 6FVSY9334PRO34005FLJ13710AAT12

Not targeted by approved drugs; mechanisms relate to promoting microfibril assembly through interaction with fibrillin-1 and attenuation of TGF-β signaling, potentially via sequestration of active/latent TGF-β complexes[4][1][3].