Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pure human pepsins 1 and 3 are inactivated by incubation at pH 7.1-7.3 for 30 minutes, losing 90% or more of activity. Pepsin 5 is alkali-stable, retaining 100% of activity. Mixtures of pure pepsins 1 and/or 3 with pepsin 5 were found to have greater alkali-stable activity than predicted. Two published methods for determining the alkali-stable fraction of the peptic activity of gastric juice gave, respectively, in our hands values of 45.4-80.0% and 27.5-43.9% of the total activity. These values seemed too high to be attributable only to pepsin 5 in gastric juice, as agar gel electrophoresis shows pepsin 3 to have the principal activity. Electrophoretograms of alkaline incubated gastric juice revealed that large amounts of pepsin 3 retained activity as well as pepsin 5, and a proteolytic zone "4" appeared between them. Alkali inactivation thus does not allow the estimation of pepsin 5 individually in gastric juice. Pepstatin, at a final concentration of 100 to 170 pmol/ml, may be used to estimate pepsin 5 in gastric juice and gave values of 18.0 to 27.6% of the total peptic activity. Pepsin 5, in gastric juice and in mixtures of pepsins, appears to protect pepsin 3 from alkaline-inactivation, and to a lesser extent from pepstatin inhibition.
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PMID:Pepsin 5 in gastric juice: determination and relationship to the alkali-stable peptic activity. 4 73

Mouse antibodies to soluble bovine skin (type I) collagen react with determinants which are located in the rigid triple-helical portion of the antigen and become destroyed upon unfolding the molecule. Helical antigenic determinants are dependent on the genuine chain assembly, e.g. alpha[1(I)]2alpha2. Artefactual triplehelical structures of the composition [alpha1(I)]3 or [alpha2]3 or a genetically distinct type II collagen from cartilage showed no or only weak cross-reactivity. Pepsin treatment of type I collagen known to remove short, non-helical sequences at both ends of the molecule had virtually no effect on antigenicity and immunogenic activity. A radioimmunoassay failed to detect antibodies in three congenic resistant mouse strains immunized with denatured type I collagen. These strains had been previously classified as high or low responders to native type I collagen. Agglutination titres vs denatured collagen culd already be demonstrated in nonimmune sera. The agglutinating activity was labile against heating at 56 degrees and could not be increased by immunization. Two out of five inbred strains showed a high response against pepsin-dissolved bovine type II collagen with the chain composition [alpha1(II)]3. Lack of correlation in the responder state to both collagen types indicated control by different immune response genes. Antibodies to type II collagen also reacted against triple-helical antigenic determinants and showed neglible cross-reaction with type I collagen.
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PMID:Specificity of the antibody response in inbred mice to bovine type I and type II collagen. 5 15

Metiamide, 25 mg, antagonized the action of histamine on acid and pepsin secretion from both denervated pouches and innervated stomachs in dogs. In the same preparations its action on pepsin following food, pentagastrin or 2 deoxy-d-glucose was nonsignificant. Following pilocarpine or secretin, metiamide augmented pouch pepsin. The action of every acid stimulant was depressed by metiamide including the direct vagal action of deoxy-d-glucose on the innervated stomach. H2 receptors seem, therefore, to be involved in some form in acid stimulated by the vagi, histamine, pentagastrin and pilocarpine. Pepsin stimulation does not seem to be via H2 receptors with the esception of stimulation by histamine itself.
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PMID:Metiamide: an antagonist of histamine-stimulated gastric acid secretion. 5 35

In conscious and unrestrained cats the gastric secretion and ulcer formation induced by i.v. infusion of pentagastrin can be inhibited by synthetic salmon calcitonin given simultaneously. The volume and various constituents of gastric juice are proportionally diminished. Pepsin alone is definitely more inhibited, which may be of significance in respect to the mode of action of calcitonin. These effects are dose dependent in the range of 0.01 mug - 1.0 mug/kg/h salmon calcitonin, corresponding to 0.05 - 5.0 MRC units. Based on the finding that such minute doses have effects, it may be speculated that calcitonin has a regulatory function in gastric secretion of cats. In Shay-rats a dose dependent inhibitory effect of salmon calcitonin on ulcer formation and gastric secretion is demonstrated. Besides the volume, the acid concentration of gastric juice is reduced, which may explain the high efficacy of salmon calcitonin to prevent ulcer formation in this species. Ulcerations induced by pylorus ligation, stress and phenylbutazone can be inhibited to a similar degree by calcitonin, suggesting interference with a basal mechanism common to all three types of ulcerogenesis.
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PMID:Effects of synthetic salmon calcitonin on gastric secretion and ulcer formation in conscious cats and rats. 6 54

Chemical modification of standard gammaglobulin with enzyme treatment (pepsin) or stabilization (beta-propiolactone) is able to influence elimination, fragmentation and organ distribution of intravenously administered gammaglobulins as shown in 36 dogs after i.v. application of allogenic and xenogenic gammaglobulin preparations. Pepsin-gammaglobulin was eliminated and fragmented most rapidly. Gammaglobulin concentrations of all preparations in the skin showed as slower decrease than comparable blood concentrations. The highest skin concentrations 10 days after i.v. application were found for beta-propiolactone gammaglobulin with 6.2 +/- 1.6 microgram/g compared to a blood level of 7.9 +/- 0.9 microgram/ml.
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PMID:[Concentration of intravenously administered gammaglobulin preparations in dog skin (author's transl)]. 7 82

Bovine colostral IgG1 was subjected to both papain and pepsin hydrolysis. Papain digestion appeared to be optimal at pH 7.4 in the presence of 0.01 M cysteine. The molecule was split at the COOH-terminal side of the interchain disulfide bond(s), and in addition to Fab fragments, two Fc fragments, designated Fc(I) and Fc(II), were obtained. Both Fc fragments had an identical NH2-terminal sequence, but differed in m.w. by about 10,000, with Fc(II) being the smaller one. Differences were also observed in their circular dichroism (CD) spectra and in their susceptibility to carboxypeptidase hydrolysis. These results suggested that the distinguishing characteristics of the two Fc fragments resided in the COOH-terminal parts of the molecules. Pepsin hydrolysis yielded the expected F(ab')2 and pFc' fragments. This hydrolysis was found to be dependent upon substrate concentration leading to aggregate formation at IgG1 concentrations below 3%.
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PMID:Characterization of the proteolytic fragments of bovine colostral IgG1. 7 49

Testicular interstitial cells were utilized to study the effects of prostaglandins (PG) on in vitro testosterone production and to examine the role of cyclic adenosine-3',5'-monophosphate (cAMP) in this process. Testosterone production was assessed after 3 hour incubations while cAMP accumulation was examined after a 0.5 hour incubation period. Testosterone and cAMP were measured by radioimmunoassay. None of the PGs tested (PGA, PGA2, PGB1, PGE1, PGE2, PGF1alpha PGF2alpha) altered basal testosterone production when present in incubates at concentrations of 1.3 X 10(-8) M to 1.3 X 10(-4). However, at concentrations of 1.3 X 10(-4) M all of these PGs were capable of decreasing Luteinizing Hormone (LH; 100ng)-induced testosterone production. The inhibition of LH-induced testosterone production by the B, E and F series PGs was less pronounced than that for the A series. PGA1 and PGA2 exhibited 80% and 95% inhibition, respectively, at 1.3 X 10(4) M. The inhibitory action of 4 X 10(5) M PGA1 or PGA2 was evident within 30 minutes. Preincubation of interstitial cells with indomethacin (10(-5) or 10(-6) M) for 30 minutes did not alter subsequent basal or LH (100ng)-induced testosterone production. Accumulation of cAMP was stimulated by LH (10 microgram) or by PGs (1.3 X 10(-4) M PGA1, PGA2, PGB1, PGE1 or PGF2alpha). The PG-induced cAMP accumulation thus occurred at concentrations where LH-stimulated testosterone production was inhibited. Furthermore, PGA1 and PGA2 (1.3 X 10(-4) M) inhibited testosterone production induced by either 3-isobutyl-1-methyl xanthine (MIX; 10(-4) M or 10(-3) M) or dibutyryl cAMP (dbcAMP; 10(-4) M or 10(-3) M). These results indicate that PGs can block testosterone production by a direct effect on testicular interstitial cells and suggest that PGs exert their inhibitory action distal to stimulation of cAMP formation. PGs do not appear to play a role in the mechanism of LH action.
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PMID:Prostaglandin inhibition of testosterone production induced by luteinizing hormone, dibutyryl cyclic AMP or 3-isobutyl-1-methyl xanthine in dispersed rat testicular interstitial cells. 8 81

Luteinizing hormone (LH) and follicle stimulating hormone (FSH) stimulated the accumulation of adenosine 3',5'-monophosphate (cAMP) within 30 minutes of addition to human testicular incubates. The phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine acted synergistically with FSH and to a lesser degree with LH to enhance cAMP accumulation. The findings indicate that cAMP accumulation may be involved in the mechanism of action of LH and FSH in the human testes, as has been proposed for rats. The prostaglandins (PG) PGE-1, PGE-2, PGA-1, and PGF-2-alpha stimulated cAMP levels at a concentration of 1/10,000 M in human testes. The E type prostaglandins were the most potent; they induced half-maximal stimulation of cAMP at 7/10,000,000 M.
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PMID:Stimulation of cyclic adenosine 3':5'-monophosphate accumulation in human testes in vitro by luteinizing hormone, follicle-stimulating hormone, and prostaglandins. 8 21

Pepsin-treated human gammaglobulin, 150 mg/kg body weight, was administered intravenously to 14 healthy volunteers. Before and after the infusion the nitroblue tetrazolium (NBT)-reduction of granulocytes was studied in all and the bactericidial capacity in 12 subjects. An increase of NBT reduction (p less than 0.05) and of bacterial capacity (p less than 0.01) of granulocytes was found after the infusion. The effects may be due to an opsonising action of F (ab')2 components.
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PMID:Granulocytic function after administration of pepsin treated human gammaglobulin. 8 4

The C-terminal region-sepcific anti-glucagon sera were raised in rabbits using as immunogen, and conjugate of BSA and a C-terminal fragment of pancreatic glucagon. The hapten was prepared by trypsin digestion of the glucagon, which was proved to be a 1:3 mixture of glucagon (18--29) and (19--29). Six rabbits were immunized by subcutaneous injection of an emulsion of the conjugate with complete Freund's adjuvant and five of the rabbits produced antibodies to the glucagon (GC-1, GC-2, GC-3, GC-5 and GC-6). For comparison, rabbit antisera were also produced against glucagon polymer (GA-10) and syrupy glucagon fibrils (PGA-2). All these antisera as well as the pancreatic glucagon-specific antiserum 30 K were characterized with dog gut-extract (gut-GLI) and glucagon-related peptide fragments in the radioimmunoassay systems. The assay systems utilized 125 I-monosubstituted pancreatic glucagon as tracer and human mono-component glucagon as standard. All sera of the GC-series crossreacted with the dog gut-extract very weakly and antisera GC-5 and GC-6 exhibited the lowest crossreactivities with the extract, which were shown to be as low as that of 30k. Characterization of the antiserum GC-5 with purified glucagon related fragments indicated that the major antigenic determinant located exactly in the C-terminal region of glucagon. The present results clearly showed high efficiency of the use of the glucagon C-terminal fragment as hepatenic immunogen in obtaining the C-terminal region-specific, i.e., pancreatic glucagon-specific antisera.
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PMID:Production of anti-glucagon sera with a C-terminal fragment of pancreatic glucagon. 8 40


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