The immunological characterization of several human ribonucleases by using primary binding tests

Abstract

RNAases (ribonucleases), purified from four human tissues, as well as bovine pancreatic RNAase (RNAase A), were studied by immunodiffusion methods and by two different primary binding tests. The enzymes fell into two groups immunologically, those purified from plasma and pancreas in one and those from spleen and liver in the other. No antigenic cross-reaction between the two groups was detected by any of the immunoassays used. There was a slight antigenic cross-reaction between the human and bovine pancreatic RNAases. The liver and spleen RNAases were immunologically identical by all criteria used, whereas a small but consistent antigenic difference between the human plasma and human pancreas enzymes was detected. The significance of this difference between the human plasma and pancreas RNAases is discussed in relation to similarities and differences in their properties.

Human endothelial cells selectively express large amounts of pancreatic‐type ribonuclease (RNase 1)

“…From the post‐translational point of view, EC‐RNase occurs as a heterogenously glycosylated protein that might be identical to serum‐ and to urinary‐RNases as a direct consequence of its release by endothelium into the blood stream and subsequent renal clearance. Besides, EC‐RNase and HP‐RNase should have different carbohydrate compositions, based on consistent antigenic differences between pancreatic and serum pancreatic‐type RNases [Neuwelt et al, 1977; Yamashita et al, 1986] and between urinary and pancreatic RNases [Beintema et al, 1988], respectively.…”

Effect of Hemodialysis on Acid Leukocyte-Type Ribonuclease, Alkaline Ribonuclease and Polymorphonuclear Elastase Serum Levels in Patients with End-Stage Renal Disease

“…RNase is present in all living cells; however, only pancreatic-type alkaline RNase and spleen leukocyte-type acid RNase were identified in plasma [12, 13]. In subjects with normal renal function, serum alkaline RNase is a marker of pancreatic injury [16], negative nitrogen body balance [17] and protein malnutrition [18].…”

“…Patients with ESRD present with an RNase plasma concentration amounting to 10- to 20-fold of its normal level [10]. Since the RNase of human plasma is composed of two different fractions, one of pancreatic and the other of leukocytic origin [12, 13], the accumulation of these fractions in plasma is determined by two different equilibria between the rate of their release from cellular space and removal from the extracellular fluids. In mice, kidney uptake of up to 80% of the administrated radiolabeled alkaline pancreatic RNase is registered while liver and intestine uptake is about 5 and 10%, respectively [14, 15].…”

“…Plasma RNase is composed of two isoenzymes, acid of leukocytic origin, and alkaline deriving from the pancreas. Acid leukocyte-type RNase should represent granulocyte involvement in the increase of leukocyte LMWPs, while pancreatic-type alkaline RNase should represent LMWPs not depending on leukocyte activation [11,12,13]. The aim of this study was to assess a relationship between HD treatment and changes in concentration of PMN elastase, which is a marker of granulocyte protein output, as well as acid RNase and alkaline RNase.…”

Non-Specificity of Elevated Serum Ribonuclease as a Pancreatic Tumour Marker

“…The ribonu cléase activity in plasma and serum could therefore be originating from any or all of these organs. However, the liver-extracted and the pancreas-extracted enzymes differ immunologically [17] and in their substrate specificity, the pancreatic enzyme being more active against cytidylic acid residues [2. 16,20] and double-stranded RNA than is the liver/spleen type.…”