Ribonuclease pancreatic (RNASE1) (RNASE1)

Ribonuclease pancreatic (RNASE1) is a potent secretory enzyme belonging to the Ribonuclease A superfamily that plays a critical role in regulating extracellular RNA levels. Its primary physiological function is the catalytic degradation of single- and double-stranded RNA in the extracellular space, which helps maintain vascular homeostasis by clearing pro-inflammatory and pro-coagulatory extracellular RNA (eRNA) released during cell death. Beyond its nuclease activity, RNASE1 has recently been identified as a non-canonical ligand for several receptor tyrosine kinases, including ALK in non-small cell lung cancer and EphA4 in breast cancer, where it triggers oncogenic signaling pathways independently of its catalytic function. In the tumor microenvironment, RNASE1 also contributes to immune evasion by internalizing into T cells and interacting with STAT1 to induce cellular dysfunction. Therapeutically, RNASE1 is being investigated both as a treatment (recombinant versions for cardiovascular and inflammatory diseases) and as a target (using inhibitors or antibodies to block its role in cancer progression).

Other names

HP-RNaseRIB-1RNase UpI-1Ribonuclease 1Ribonuclease ARAC1RNS1Ribonuclease A family member 1

Ligand-mediated activation of receptor tyrosine kinases (ALK, EphA4); Catalytic degradation of extracellular RNA; Inhibition of STAT1-mediated T-cell cytotoxicity