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Ribonuclease 4 is a small, secreted enzyme (119 residues) of the ribonuclease A family, highly conserved across vertebrates[1][4]. It is characterized by strict specificity, cleaving RNA after uridine residues, and is found in human plasma and tissues such as pancreas, liver, saliva, and specifically in intestinal epithelial cells (notably goblet and Paneth cells)[1][3][5]. RNASE4 plays a major role in RNA metabolism, possesses antimicrobial activity against certain gut bacteria, induces angiogenesis, and protects neurons from degeneration[4][5]. It is co-expressed and shares promoter regions with angiogenin (RNASE5), another member of the ribonuclease A family, and is being investigated in the context of neurodegenerative diseases (ALS) and inflammatory bowel disease (IBD)[3][4][5]. Its structure is notable for having a shortened C-terminus that determines its substrate specificity[1][2]. Recombinant RNASE4 protein can stimulate neurogenesis and vascular formation in experimental models, and altered levels or genetic variants are associated with ALS risk and intestinal inflammation[4][5].
Recombinant RNASE4 protein: angiogenesis stimulation, neuroprotection in ALS models via RNA cleavage and possible modulation of cellular differentiation. Antimicrobial activity: RNASE4 binds and kills specific gut bacteria such as Parasutterella, modulating the microbiome.
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