Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.27.1 (RNase)
 16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Changes in the activities of three gastric and nine pancreatic enzymes plus colipase were determined during postnatal development and weaning in calves. In calves exclusively milk-fed for 2, 7, 28, 56, 70 and 119 d, the enzyme activities per kilogram of empty live weight increased with age for chymotrypsin, elastase, carboxypeptidases A and B, ribonuclease and alpha-amylase, decreased for chymosin, lysozyme and colipase but showed no change in the case of pepsin, trypsin, lipase and phospholipase A2 compared with animals at birth. The greatest increase was that in alpha-amylase activity (about 50-fold between d 2 and 119). In calves weaned between d 28 and 56, all the activities were higher than in milk-fed animals, except that of chymosin (which was slightly lower) and that of colipase (which did not change). At 119 d of age, chymotrypsin, carboxypeptidase A, alpha-amylase and lipase were 1.6- to fourfold higher in ruminants than in preruminants. Thus, most enzyme activities were modified first by colostrum and milk intake, and again upon weaning by development of the forestomachs and ingestion of solid food. These ontogenic patterns might be under the control of many gut regulatory peptides, the plasma concentrations of which changed simultaneously. Some gastric and pancreatic enzymes were correlated to plasma concentrations of these gut regulatory peptides.
 ...
PMID:Gastric and pancreatic enzyme activities and their relationship with some gut regulatory peptides during postnatal development and weaning in calves. 137 46

This study was performed to investigate the behavior of phospholipase A2 (PLA2) in serum and urine of patients with chronic pancreatic diseases and to ascertain whether any factors influenced the results. In 30 controls, 45 patients with pancreatic cancer, 54 with chronic pancreatitis, and 64 with extrapancreatic diseases, serum and urinary PLA2, pancreatic isoamylase and RNase, and urinary N-acetylglucosaminidase (NAG) were measured. Serum PLA2 levels were higher in patients with chronic pancreatitis than in all the other groups. In our patients, only occasionally was urinary PLA2 elevated, the increase occurring almost exclusively in the presence of an acute inflammatory disease, e.g., relapsed chronic pancreatitis or active inflammatory bowel disease. A correlation was found between serum PLA2 and serum RNase, an indicator of tissue damage, but not between serum PLA2 and pancreatic isoamylase. Urinary PLA2 output was correlated with its renal input and with RNase output. No correlation was found between PLA2 output and pancreatic isoamylase or NAG urinary excretion. In conclusion, (1) the determination of serum PLA2 activity may be an aspecific test of pancreatic disease; (2) PLA2 urinary excretion occasionally increases, especially in the presence of severe phlogosis, which occurs in chronic pancreatitis, in particular during relapse; and (3) irrespective of the tissue origin of urinary PLA2, its increased excretion may be accounted for in part by its increased circulating levels. It is, however, more likely the consequence of a renal tubular dysfunction, which is sometimes found in patients with pancreatic diseases.
 ...
PMID:Urinary phospholipase A2 excretion in chronic pancreatic diseases. 151 57

The electron microscopy cytochemical detection of phospholipids in well-defined areas in the interphase nuclei of hepatocytes has been obtained by the acid haematein test, modified for electron microscopy and by the phospholipase A2-colloidal gold method. The specificity of both methods were controlled by enzymatic digestion with phospholipase. The main intra-nuclear localization of phospholipids is at the border between the condensed and dispersed chromatin, where non-ribosomal RNA is also revealed by RNase-gold labelling. Phospholipids are detected, too, over the clusters of interchromatin granules and in the fibrillar component of the nucleolus.
 ...
PMID:TEM cytochemical study of the localization of phospholipids in interphase chromatin in rat hepatocytes. 156 72

In order to study the biochemical changes associated with the cell body response to axonal crush injury, two systems, hypoglossal nucleus and spinal cord ventral horn, were used. The time intervals chosen were 7, 14, and 28 days after unilateral crushing of the right hypoglossal nerve and cervicothoracic nerves of the rabbit. Non-crushed, contralateral nerves were used as controls. Three groups of enzyme activities were tested: (a) phospholipase A2, acyl CoA:2-acyl-sn-glycero-3-phosphocholine acyltransferase, and choline phosphotransferase, as indicators of phospholipid degradation and biosynthesis; (b) seven hydrolases, namely, beta-D-glucuronidase, beta-N-acetyl-D-hexosaminidase, arylsulfatase A, galactosylceramidase, GM1-ganglioside beta-galactosidase, and acid RNase, as indicators of lysosomal activity; and (c) free and inhibitor-bound alkaline RNase, as an index of RNA metabolism. Changes could be grouped into three distinct patterns. Compared to contralateral control, choline phosphotransferase showed a slight increase, whereas phospholipase A2 and most lysosomal hydrolases showed a significant increase of activity, especially evident in the ventral spinal cord neurons 14-28 days after crushing. These changes correlate with known increases of membrane and organelle numbers, including lysosomes, in motor and sensory neurons during peripheral regeneration. In contrast, free and acid alkaline RNase activity significantly decreased in the injured sides compared to the controls. This change can probably be correlated with a stabilization of RNAs needed for increased protein synthesis. No changes in total alkaline RNase and acyltransferase activities in either regeneration model were observed.
 ...
PMID:Changes of phospholipid-metabolizing and lysosomal enzymes in hypoglossal nucleus and ventral horn motoneurons during regeneration of craniospinal nerves. 283 34

Testosterone-treated calf thymocytes produce increased amounts of proteins, termed lipokinins, that stimulate phospholipase A2 from snake venom and mammalian tissue. The induction of these proteins by testosterone is blocked by cycloheximide and, thus, requires new protein synthesis. These proteins activate phospholipase A2 stoichiometrically. They are inactivated by boiling, trypsin or alkaline phosphatase but not by deoxyribonuclease or ribonuclease. Lipokinins significantly repair the failure of masculinization in the Tfm mouse with an X-linked deficiency of androgen-receptor. Thus, the post-receptor effects of testosterone on embryonic genitalia may be mediated through stimulation of phospholipase A2 by lipokinins. Moreover, lipokinins may be involved as stimulators of the arachidonic acid cascade, as lipocortins are inhibitors.
 ...
PMID:John Lattimer lecture. Lipokinins: novel phospholipase A2 activators mediate testosterone effects on embryonic genitalia. 318 94

In the present study an improved method of reversed-phase high-performance liquid chromatography (HPLC) for separation of rat pancreatic juice proteins is introduced. Aliquots of pancreatic juice were saved from conscious rats during basal secretion. The secretory proteins were separated on a wide-pore silica column by use of a multistep acetonitrile/water gradient. Up to 14 individual peaks could be separated by one run. Molecular weight analysis by sodium dodecyl sulfate (SDS)-gels allowed identification of peaks representing amylase, lipase, procarboxypeptidases, proelastase, chymotrypsinogen, and trypsinogen. Injection of pure rat amylase increased one specific peak which was assumed to represent amylase in the juice profile. Small amounts of residual enzymatic activities were measured for amylase, trypsin, and chymotrypsin in material of certain peaks. Activities of lipase, ribonuclease, and carboxypeptidases were not found, which reflected degradation of these enzymes by the separation procedure. High activities of phospholipase A2 were detected in one specific, early-eluting peak. Reversed-phase HPLC offers precise, reproducible, and rapid separation of the major proteins of rat pancreatic juice.
 ...
PMID:Identification of rat pancreatic secretory proteins after separation by high-performance liquid chromatography. 337 29

Antibodies prepared against the phospholipase A2 stimulatory peptide melittin were used to identify and isolate a novel mammalian protein with similar functional and antigenic properties. The mammalian protein of Mr 28,000 was isolated from cell sonicates by high performance immunoaffinity chromatography and size exclusion chromatography. This stimulatory protein was stable for several months when frozen at -70 degrees C. The purified protein selectively stimulated phospholipase A2 when phosphatidylcholine was used as a substrate but had no effect on phospholipase A2 activity when phosphatidylethanolamine was used as a substrate. Furthermore, this protein had no effect on phospholipase C activity or on pancreatic or snake venom phospholipase A2. The stimulatory activity was unaffected by RNase or DNase treatment. However, boiling or trypsin digestion inactivated the phospholipase stimulatory activity. The mechanism of phospholipase A2 stimulation appeared to result from an increase in the apparent Vmax of the enzyme.
 ...
PMID:Identification and isolation of a mammalian protein which is antigenically and functionally related to the phospholipase A2 stimulatory peptide melittin. 354 34

A macromolecule binding 3H-methylcholanthrene (3H-MCA) and 3H-benzo(a)pyrene (3H-BaP) and sedimenting in the 4-5 S region of sucrose gradient (4.5 S) was identified in rat liver cytosol. The binding was displaced by 100-fold molar excess unlabeled ligands whereas 2,3,7,8-tetrachloro-dibenzo-p-dioxin (TCDD) was ineffective. The dissociation constant for both polycyclic aromatic hydrocarbons (PAHs) was of the order of 10(-8) M or lower. Both 3H-MCA and 3H-BaP bound to 4.5 S in a non covalent manner, since 92% of the bound radioactivity was extractable with ethyl ether. Furthermore the binding was strongly reduced by urea 8 M and by guanidine. HCl 4 M (99 and 70% respectively). Thin layer chromatography of the ethyl ether-solubilized radioactivity showed a peak comigrating with PAHs used as standards. When chromatographed on Sephadex G-200, 4.5 S was eluted as a sharp peak with an apparent molecular weight of 50-60,000 daltons. Enzyme treatment of liver cytosol showed that the 4.5 S binding sites were destroyed by micrococcal nuclease (92% of inhibition). Papain and phosphodiesterase I and II reduced the binding to 50%, whereas DNase I, DNase II, RNase, phospholipase A2 and C and trypsin were ineffective. These data suggest that the PAHs binding macromolecule of rat liver cytosol is a protein associated with a polynucleotide. The binding of both PAHs was enhanced by increasing the incubation temperature, the maximum being reached after 20-30 min at 37 degrees C. After 2.5 min at 65 degrees C, binding sites were completely destroyed. The same temperature-induced "activation" was obtained also by prewarming the cytosol at 37 degrees C in the absence of ligands.
 ...
PMID:Polycyclic aromatic hydrocarbon binding macromolecules. Identification, characterization and temperature activation of a 4.5 S binding nucleoprotein. 406 Feb 44

The mechanisms involved in the activation of autolytic enzymes in Staphylococcus aureus, by leukocyte extracts, cationic proteins, phospholipase A2, amines, and membrane-damaging agents was studied in a resting cell system as well as by growing staphylococci. The bacteria were labeled with [14C]N-acetylglucosamine and were subjected to a variety of agents either in 0.1 M acetate buffer, pH 5.0, or in phosphate buffer, pH 7.4. While intact log-phase cultures were found to undergo partial autolysis at pH 5.0 and almost complete lysis at pH 7.4, both heat-killed bacteria and bacterial cell walls were completely resistant to autolysis in buffers. Autolysis at pH 5.0 can be further activated by leukocyte extracts, nuclear histone, crystalline ribonuclease, egg-white and human lysozyme, phospholipase A2, as well as by spermine, spermidine, and polymyxins B and E. The addition of viable log-phase bacteria to radiolabeled heat-killed staphylococci or to radiolabeled cell walls which had been cleaned off autolytic enzymes resulted in degradation of the radiolabeled targets. The data suggest that the various inducers of autolysin activation caused leakage of autolytic enzymes from the intact bacteria which attacked the depolymerized the bacterial cell walls. Anionic polyelectrolytes like heparin, dextran sulfate, suramine, polyglutamic acid, and liquid (polyanethole sulfonic acid) markedly inhibited both spontaneous and induced lysis. Staphylococci which had grown in the presence of anionic polyelectrolytes became highly resistant to lysis triggered by any of the inducers of autolysis. Since inflammatory exudates are known to be rich in anionic polyelectrolytes, it is suggested that the prolonged survival of intact bacterial cells in such a milieu may be due to the inactivation of autolytic enzymes. It is also postulated that the degradation of certain bacterial species following phagocytosis or extracellular degradation may not be the result of the action of hydrolytic enzymes but rather the result of activation by leukocyte factors of autolytic enzymes which lead to bacteriolysis.
 ...
PMID:Effect of leukocyte hydrolases on bacteria XVI. Activation by leukocyte factors and cationic substances of autolytic enzymes in Staphylococcus aureus: modulation by anionic polyelectrolytes in relation to survival of bacteria in inflammatory exudates. 618 97

Pancreatic amylase, elastase 1, elastase 2, cationic trypsin, chymotrypsin, ribonuclease (RNase), phospholipase A2, gamma-glutamyl transpeptidase (gamma-GTP) and pancreatic secretory trypsin inhibitor (PSTI) were purified and characterized from human pancreatic juice and pancreatic tissue. During the purification of these enzymes, two enzymes previously not reported were found. A pancreatic deamidase and a renal endopeptidase were purified and characterized. Specific and reliable radioimmunoassays (RIAs) were developed for all pancreatic enzymes and inhibitor. The purpose of immunoassay for pancreatic enzymes and inhibitor was discussed, and clinical application for the diagnosis of pancreatic diseases was demonstrated. Messenger RNA (mRNA) of amylase was isolated from human pancreas and parotid gland, and used to prepare a complementary DNA (cDNA). The nucleotide sequence and the predicted amino acid sequence of these clones were now being determined. The application of the present investigation to elucidation of pathogenesis of pancreatic enzyme-producing diseases was discussed.
 ...
PMID:[Purification and development of immunoassay of pancreatic enzymes and trypsin inhibitor, and their application to elucidation of pathogenesis of various pancreatic and pancreatic enzyme-producing diseases]. 620 25


1 2 3 Next >>