Single-chain type IV collagen (SCCOL-IV)

Single-chain type IV collagen (SCCOL-IV), also known as the non-triple helical form of the type IV collagen alpha-1 chain (NTH alpha-1(IV)), is a specialized extracellular matrix protein derived from the COL4A1 gene (Tokunaka et al., 2011). While physiological type IV collagen typically forms a heterotrimeric triple helix essential for basement membrane structure, SCCOL-IV is secreted as a monomeric polypeptide and is predominantly found in the interstitium of malignant tumors (Imamura et al., 2011). It is significantly upregulated during active neovascularization and tumor tissue expansion, where it is thought to facilitate the formation of vascular-like networks (Tokunaka et al., 2011). Because SCCOL-IV is largely absent from normal adult tissues, it serves as a highly specific biomarker for tumor progression and a potential diagnostic tool. Therapeutic interventions targeting SCCOL-IV, such as the monoclonal antibody NK46141, aim to inhibit tumor growth by disrupting pathological vasculogenesis and angiogenesis (Nippon Kayaku, 2015). This specificity for the tumor microenvironment makes SCCOL-IV an attractive target for developing selective anti-cancer therapies with minimal impact on healthy basement membranes.

Other names

Non-triple helical type IV collagen alpha-1 chainNTH alpha-1(IV)SCCOL-IVNon-triple helical form of COL4A1

Inhibition of tumor vasculogenesis and suppression of tumor tissue expansion through targeted binding by monoclonal antibodies that recognize the non-triple helical conformation of the collagen alpha-1(IV) chain.