Protein tyrosine phosphatase receptor type M (PTPRM) (PTPRM)

Protein tyrosine phosphatase receptor type M (PTPRM), also known as PTPmu, is a transmembrane protein belonging to the type IIB receptor protein tyrosine phosphatase family. In healthy tissues, PTPRM mediates homophilic cell-cell adhesion and regulates signaling pathways involved in maintaining tissue architecture (UniProt P28827). However, in glioblastoma (GBM) and other aggressive gliomas, PTPRM is frequently subjected to pathological proteolytic cleavage by metalloproteases. This process generates a unique, tumor-specific extracellular fragment that remains associated with the glioma cell surface or is secreted into the microenvironment (Burden-Gulley et al., 2010). This fragment serves as a highly specific biomarker because the full-length, functional protein is typically absent or downregulated in these malignant cells. Experimental therapies and diagnostic tools utilize specialized peptides, such as SBK2, to selectively bind this PTPRM-derived fragment (Sun et al., 2020). This targeting approach allows for the precise delivery of imaging contrast agents or cytotoxic drugs directly to glioma cells while sparing healthy brain tissue. By targeting the altered state of PTPRM, researchers aim to improve the precision of glioma treatment while minimizing effects on normal neural cells.

Other names

PTPmuR-PTP-muPTPμReceptor-type tyrosine-protein phosphatase mu

Targeted binding to the extracellular fragment of proteolytically cleaved PTPRM on tumor cells