Soluble melanoma cell adhesion molecule (sCD146) (sCD146)

Soluble CD146 (sCD146) is the shed extracellular domain of the melanoma cell adhesion molecule (MCAM), a transmembrane glycoprotein belonging to the immunoglobulin superfamily [5, 8, 12]. It is generated through the proteolytic cleavage of membrane-bound CD146 by matrix metalloproteinases, such as MMP-2 and MMP-9, in response to inflammatory or hemodynamic stress [8, 9, 11]. Functionally, sCD146 acts as a potent pro-angiogenic and pro-tumoral factor by interacting with receptors like angiomotin and integrin αvβ3, which triggers signaling pathways involved in cell proliferation, migration, and survival [2, 14, 16]. In clinical settings, elevated levels of sCD146 in the blood or other biological fluids serve as biomarkers for cancer progression, heart failure, and various inflammatory diseases [3, 6, 15, 17]. Therapeutic strategies targeting sCD146 involve the use of neutralizing monoclonal antibodies, such as M2J-1 and mucizumab, which aim to inhibit tumor vascularization and metastasis without disrupting the physiological functions of membrane-bound CD146 on normal vessels [1, 3, 16]. These antibodies are designed to be specific for the soluble form, thereby avoiding the potential toxicity associated with targeting CD146 expressed on healthy vascular endothelium [1, 22]. This specificity is particularly important given the role of membrane CD146 in maintaining vascular integrity and regulating leukocyte trafficking [6, 12].

Other names

Soluble CD146sMCAMSoluble MUC18Soluble S-Endo1Soluble A32 antigenSoluble hemopoietic cell adhesion molecule

Neutralizing monoclonal antibodies specifically target the soluble form of CD146 to block its interaction with receptors such as angiomotin and integrin αvβ3, thereby inhibiting pro-angiogenic and pro-tumoral signaling pathways.