Tetraspanin-8 (Tspan8)

Tetraspanin-8 (Tspan8) is an integral membrane protein belonging to the tetraspanin family, characterized by four transmembrane domains and expressed across a variety of tissues, including the pancreas, stomach, kidney, and brain[1][4][5]. It plays a central role in organizing protein microdomains on the cell surface, modulating partner protein interactions (such as integrins and SNARE proteins), and regulating signal transduction. Tspan8 is critically involved in processes such as cell development, adhesion, migration, and the regulated fusion of secretory granules, notably by sequestering syntaxin-2 to control biphasic release events like mucin and insulin secretion[2][3]. Elevated or dysregulated Tspan8 expression is implicated in the promotion of cancer cell invasion, metastasis, cancer stemness, drug resistance, and serves as a prognostic biomarker especially in digestive system tumors and ovarian cancer[1][4]. Its multifaceted role in both normal biology and disease, particularly cancer, makes it a focus of ongoing therapeutic and diagnostic research, though no specific small-molecule or antibody drugs are presently approved that directly target Tspan8.

Other names

CO-029TM4SF3Tspan-8

Modulation of cell–cell adhesion and motility (by complexing with integrins and affecting protein clustering) - Regulation of exocytosis (by sequestering SNARE proteins such as syntaxin-2 and syntaxin-3, thus controlling secretory granule fusion)