Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. To characterize the development of peptide hydrolysis the activities of pancreatic carboxypeptidase A (CPA) and intestinal glycylleucine dipeptidase (GLDP) were registered in 1-45 days old chicks, as well as GLDP activities in newborn and adult guinea pigs. 2. The highest values of CPA and GLDP relative activities were found immediately after hatching, maximal decrease of activities took place during the first week. 3. GLDP activities gradient on the surface of the small intestine of chicks has two maximums: one in the upper jejunum, the other one--in the lower ileum. The development of proximo-distal gradient began at the age of 7 days and finished at the end of the first month. 4. Total CPA and GLDP activities decreased during the first week; up to the 15-20 day they reached the initial level and later exceeded it. 5. Relative GLDP activity in guinea pigs declined with aging, while the total activity increased, as it was demonstrated for chicks. 6. GLDP activity was distributed equally along the surface of the small intestine in newborn guinea pigs as well as in mature animals.
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PMID:Early postnatal development of peptide hydrolysis in chicks and guinea pigs. 167 37

The effects of pretreatments of BALB/c mice with several conjugates of MDP and MDP-Lys to ovalbumin before immunization with ovalbumin (OA) were tested on the anti-OA IgE responses. Pretreatment with MDP-Lys-OA, but not with MDP-OA, induced an inhibition of the anti-OA primary and secondary responses, as measured by passive cutaneous anaphylaxis (PCA) and also by mast cell degranulation. The inhibition by pretreatment with MDP-Lys-OA was obtained whether it was administered in Freund's incomplete adjuvant (FIA) or in saline. This IgE suppression was accompanied by an enhancement of IgG2a and IgG2b anti-OA antibodies, with no change in the specific IgG1 levels. Loss of antigenicity of OA, detected by the lack of degranulation of peritoneal mast cells sensitized by IgE anti-OA, was observed in the MDP-Lys-OA but not in the MDP-OA conjugates. This loss of antigenicity appears to correlate with the ability of the conjugate to induce suppression of the specific IgE response.
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PMID:In vivo effects of ovalbumin-conjugated muramyl peptides on the anti-ovalbumin IgE and IgG responses in mice. 650 Jul 80

Leukotrienes (LTs) are 5-lipoxygenase (5-LO)-derived arachidonic metabolites that constitute a potent set of lipid mediators produced by inflammatory cells. Leukotriene A(4), a labile allylic epoxide formed from arachidonic acid by dual 5-LO activity, is the precursor for LTB(4) and LTC(4) synthesis. LTC(4) is further transformed enzymatically by the sequential action of gamma-glutamyltranspeptidase and dipeptidase to LTD(4) and LTE(4), respectively. In this report, we present evidence that bovine pancreatic carboxypeptidase A (CPA), which shares significant sequence homology with CPA in mast cell granules, catalyzes the conversion of LTC(4) to LTF(4) via the hydrolysis of an amide bond. The identity of CPA-catalyzed LTC(4) hydrolysis product as LTF(4) was confirmed by several analytical criteria, including enzymatic conversion to conjugated tetraene by soybean LO, conversion to LTE(4) by gamma-glutamyltranspeptidase, cochromatography with the standard LTF(4) and positive-ion fast-atom bombardment mass spectral analysis. Thus, it appears that the physiological significance of this single-step transformation may point toward a major cellular homeostatic mechanism of metabolizing LTC(4), a potent bronco- and vasoconstrictor, to a less potent form of cysteinyl LTs.
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PMID:Carboxypeptidase A-catalyzed direct conversion of leukotriene C4 to leukotriene F4. 1272 12

1. Two experiments were performed on broiler chicks to determine the effect of either quantitative feed restriction (QFR) from 5 to 11 d of age or meal-feeding (MF) from d 5 to 17 on development of activity of enzymes associated with protein digestion. 2. Proteolytic activity of the proventriculus was reduced by QFR but unaffected by MF. 3. General proteolytic and carboxypeptidase A activities of the pancreas were reduced by QFR and MF. 4. Amino- and dipeptidase activities of the small intestine were increased by QFR. Dipeptidase activity was unaffected by MF. 5. Nitrogen retention of QFR chicks was lower immediately following feed restriction but not in the 2 weeks following return to ad libitum access to feed. 6. Feeding regimen alters functional development of the enzymes of protein digestion and may therefore influence growth rate of broilers.
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PMID:Quantitative feed restriction or meal-feeding of broiler chicks alter functional development of enzymes for protein digestion. 1496 90

The purpose of the present study was to evaluate the effect of cadmium on some protein digestive and absorption enzymes in rats. Thirty-six rats were grouped into three groups of 12 animals each; one group received deionised water and acted as control. One group received 445 microM Cd and the last group received 890 microM Cd in their drinking water for a period of one month. The results obtained indicate that increasing the level of cadmium from 445 microM to 890 microM in the drinking water of the rats led to 29% and 23% increase in accumulated cadmium in the proximal and distal small intestine respectively. The body weight gain of rats exposed to 445 microM and 890 microM Cd was decreased by about 24% and 43% respectively when compared with the control. The activities of carboxypeptidase A, dipeptidase and Na+/K+ ATPase were reduced in the mucosa of the proximal end of the small intestine of cadmium exposed rats. The reduction was dose dependent; with the 890 microM Cd exposed rats displaying the least activities. In the distal small intestine, the activities of these enzymes were restored in the 445 microM Cd exposed rats to levels that were not statistically different (P > 0.05) from those observed in the controls. In the 890 microM Cd exposed rats, dipeptidase activity improved by about 80% compared with the activity of the enzyme in the proximal small intestine. Likewise, Na+/K+ ATPase activity increased by about 125% compared with the observed level in the proximal small intestine. The study suggests that cadmium given to rats in drinking water compromise protein digestion and absorption of nutrients particularly in the proximal region of small intestine and could account for weight reduction associated with cadmium toxicity.
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PMID:Changes in carboxypeptidase A, dipeptidase and Na+/K+ ATPase activities in the intestine of rats orally exposed to different doses of cadmium. 1586 4