Ribonuclease pancreatic (RNase 1)

Ribonuclease pancreatic (RNase 1) is a secretory endoribonuclease enzyme encoded by the human RNASE1 gene. It is a member of the ribonuclease A superfamily and catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides, with a preference for poly(C) substrates. Unlike related digestive homologs, human RNase 1 is widely expressed in many tissues and is found at remarkable concentrations in the blood and other biological fluids. It degrades both single- and double-stranded RNA and plays roles beyond digestion, particularly in regulating extracellular RNA in processes such as blood coagulation, inflammation, and innate immunity. The protein is monomeric, may be glycosylated at specific sites, and interacts with cell-surface glycans. Engineered forms of RNase 1 are being developed as anticancer agents. Abnormal serum levels or glycoforms of RNase 1 have been implicated as candidate biomarkers in certain cancers[1][2][3][5].

Other names

Ribonuclease A family member 1, pancreaticRNASE1RNase ARIB1RNS1RAC1HP-RNaseRIB-1RNase UpI-1Ribonuclease 1Ribonuclease A C1ribonuclease pancreaticribonuclease, RNase A family, 1 (pancreatic)

RNA degradation by endonucleolytic cleavage; Potential antitumor effect via targeted RNA hydrolysis in cancer cells