Receptor protein-tyrosine phosphatase mu (PTPRM) (PTPRM)

Receptor protein-tyrosine phosphatase mu (PTPRM), also known as PTPmu, is a member of the type IIB receptor protein tyrosine phosphatase family that normally functions as a cell-cell adhesion molecule (UniProt P28827). In healthy tissues, PTPRM mediates stable cell-to-cell contact; however, in various cancers, particularly glioblastoma, the protein undergoes extensive proteolytic cleavage (Burden-Gulley et al., 2010). This cleavage, mediated by enzymes such as ADAM metalloproteases and gamma-secretase, results in the loss of the full-length tumor-suppressive form and the accumulation of specific proteolyzed fragments on the surface of cancer cells (Phillips et al., 2019). These fragments serve as unique biomarkers for the tumor microenvironment and are not typically found in healthy tissue (Brady-Kalnay et al., 2014). Therapeutic and diagnostic strategies involve using specific peptides, such as SBK2, to target these fragments for tumor imaging and the delivery of therapeutic agents. By exploiting the cancer-specific proteolysis of PTPRM, researchers aim to improve the precision of surgical resection and the efficacy of targeted therapies in invasive cancers.

Other names

PTPmuPTPμProtein tyrosine phosphatase receptor type MR-PTP-muPTPRL1

Binding to the extracellular proteolyzed fragments of PTPRM to facilitate tumor-specific imaging or drug delivery.