Disease relevance of Rnase1

• The three-dimensional structure of rat pancreatic RNase A expressed in Escherichia coli was determined [1].
• We cloned 537 basepairs (bp) of rat partial peroxisome proliferator-activated receptor gamma2 (PPARgamma2) cDNA and examined the effect of fasting or obesity on the expression of two isoforms of rat PPARgamma, gamma1 and gamma2, in either subcutaneous or mesenteric adipose tissue specimens using an RNase A protection assay [2].

High impact information on Rnase1

• Three molecules, asialo-fetuin, asialo-orosomucoid, and lactosaminated RNase A dimer, the oligosaccharide chains of which terminate in galactose residues, were bound and internalized almost exclusively (greater than 90%) by hepatocytes [3].
• It was sensitive to denaturation by sodium dodecyl sulfate and trypsin but not by DNase I, RNase A, or the nonionic detergent Nonidet P-40 [4].
• Interestingly, the perchloric acid-soluble protein inhibited cell-free protein synthesis in the rabbit reticulocyte lysate system in a different manner from RNase A [5].
• The uptake of RNase A by lysosomes appears to involve an intermediate step in which approximately 2 kDa of the polypeptide's COOH terminus remains outside lysosomes while the remainder is inside the lysosomal lumen [6].
• To assess a possible role of the nuclear matrix in glucocorticoid action, purified rat liver nuclei containing glucocorticoid-receptor complexes were treated with DNase I +/- RNase A followed by 1.6 M NaCl, thus yielding salt-extractable and salt-resistant (nuclear matrix) fractions [7].

Biological context of Rnase1

• RL1 has the highest specific activity for the hydrolysis of long-chain acyl-CoA [8].
• Their binding sites on TAR RNA were assigned by RNase A, uranyl nitrate, and lead acetate footprinting [9].
• Both catalytic sites are comprised of two histidine side chains acting as a general base-general acid pair and a phosphate-activating residue: an arginine in the case of PI-PLC and a lysine in RNase A [10].
• The cell line, designed RL1, retains sufficient metabolic enzyme activity to detect chromosome damage induced by a variety of chemical mutagens and carcinogens without the incorporation of an extrinsic metabolising system [11].
• We observed that addition of a specific RNase A preparation to the detergent-based lysing buffer increased the fluorescence of toxicant-induced apoptotic nuclei to the level of untreated diploid nuclei [12].

Anatomical context of Rnase1

• The amount of RL1 in male rats was decreased by castration but recovered to almost the level in sham-operated rat liver microsomes after treatment of the castrated rats with testosterone [8].
• When rat liver nuclei are isolated in the presence of the irreversible sulfhydryl-blocking reagent iodoacetamide, digested with DNase I and RNase A, and extracted with 1.6 M NaCl, nuclear envelope (NE) spheres depleted of intranuclear material, as analysed by thin-section electron microscopy, are obtained [13].
• Treatment of cytosol with RNase A in the absence of molybdate, partially shifted the untransformed receptor towards the 5.2-nm transformed receptor form [14].
• Results showed that the type II fiber-predominant plantaris muscle exhibited a significant increase in total RNase, RNase A and RNase T1L activities (increases ranged from +59% to +196%; P-values between 0.025 and 0.01) concomitant with large falls in RNA and protein content [15].
• The DF with high viscosity significantly suppressed RNA digestion by RNase A and decreased uptakes of 14C-labeled adenosine and adenosine 5'-monophosphate (5'-AMP) in rat jejunum [16].

Associations of Rnase1 with chemical compounds

• RL1 has the highest specific activities toward p-nitrophenylacetate and malathion [8].
• On the other hand, phenobarbital treatment of male and female rats caused a significant increase in the amounts of RH1 and RL2, whereas RL1 was not affected [8].
• Conversely, in ovariectomized female rats, the amount of RL1 was increased as compared to that in sham-operated rats, and treatment of the ovariectomized rats with estradiol tended to decrease the quantity of RL1 [8].
• In contrast, RL1 and RH1 were decreased by dexamethasone, but not by the other steroids [17].
• To test this hypothesis, we measured the total tissue and plasma RNase activities as well as the activities of general (RNase A) and specific or "restriction" RNases (T1L, T2L) in ethanol-treated rats [15].

Other interactions of Rnase1

• Examples are provided where ionizable side chain position (protein G), Asn orientation (lysozyme), His tautomer distribution (RNase A), and phosphate ion binding (RNase A and H) change with pH [18].
• In the present study the enzymatic profile of these regions has been investigated by the immunofluorescent technique using antibodies against nine pancreatic enzymes (alpha-amylase, lipase, chymotrypsinogen A, trypsinogen, elastase, carboxypeptidase A and B, DNase and RNase A) [19].

Analytical, diagnostic and therapeutic context of Rnase1

• To investigate the hormonal regulation of carboxylesterase activities, we have quantitated RL1, RL2, and RH1 in liver microsomes from male and female rats using a radial immunodiffusion assay [8].
• To determine whether these forms were associated with RNA, the 7.7S form was incubated with RNase A and analyzed by density gradient centrifugation [20].
• RT-PCR and Rnase protection assay detected different amounts of Pgamma-rod mRNA in adult and embryonic rat tissues [21].
• Two approaches in molecular morphology were applied on rat pancreatic tissue: in situ hybridization and RNase A-gold [22].
• Rnase protection assay, RT-PCR and western blot analysis were used to detect Pgamma-rod expression in various rat tissues [21].

References