Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of corticosteroid have been studied in rats submitted to oral administration of prednisone (5 mg. per kg. per day) during 8, 15, 30, and 90 days. The results were compared to those obtained after parenteral administration of hydrocortisone acetate (50 mg. per kg. per day intramuscularly). The morphometric changes of the villus-crypt axis and the brush border enzymic content of the mucosa (sucrase, enterokinase, alkaline phosphatase, and aminopeptidase) were the parameters investigated at the duodenal, jejunal, and ileal levels. Oral administration of prednisone resulted in a significant increase of the duodenal villous height at the 15th (+ 13 per cent, p less than 0.01), 30th (+ 33 per cent, p less than 0.001), and 90th day (+ 56 per cent, p less than 0.001), whereas in the jejunum a constant decrease of the villous height was noted. Parenteral hydrocortisone administration did not affect intestinal morphology. Effects of oral corticosteroids on the microvillous enzymic activities were related to both intestinal level and duration of corticoids administration: (1) in the duodenum increase of sucrase, alkaline phosphatase, and aminopeptidase during 30 days followed by normalization at the 90th day, (2) an initial increase of sucrase, alkaline phosphatase, and aminopeptidase limited to the first 8 days in the jejunum, and (3) a significant rise of alkaline phosphatase (greater than 100 per cent, p less than 0.001) and enterokinase (greater than 100 per cent, p less than 0.001) in the ileum at the 15th day of treatment. Parenteral corticosteroid administration was associated with a significant increase of both sucrase and enterokinase activities. The present study suggests that: (1) Corticosteroids exert a direct effect on the intestinal morphology varying with the intestinal level and duration of treatment. (2) No correlation could be established between anatomic and functional changes. (3) Oral corticosteroids exert an enhancing effect of the brush border enzymic activities, even in the adult mucosa and particularly at the ileal level where they stimulate significantly the enterokinase mucosal activity. (4) Parenteral corticosteroids exert a more specific effect limited to sucrase and enterokinase enhancement.
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PMID:Effects of oral and parenteral corticosteroids on intestinal villous morphology and brush border enzymes in the rat. 31 75

The subcellular localization of aminopeptidase N (previously called aminoendopeptidase) has been investigated. This enzyme was found to be partially released (30-40%) by osmotic shock or by converting Escherichia coli K10 cells to spheroplasts. However, in all other E. coli strains (K12, B/r, MRE 600, ML 308) tested, this enzyme is not released at all by these procedures and thus behaves like a cytoplasmic enzyme. The crypticity of aminopeptidase N is surprisingly low, 75-85% of the enzyme activity is directly assayable in intact cells of any E. coli strain. Various inhibitors of transport systems do not interfer with this assay. Aminopeptidase activity could also be assayed in spheroplasts, even when an insolubilized substrate was used, which suggests a surface location of this enzyme. As well, N-ethylmaleimide (0.4 mM), under conditions which do not allow penetration in the cytoplasm, caused 70% inhibition of aminopeptidase N. Binding of 125I-labeled antiaminopeptidase N antibody to spheroplasts (from K12 strain) was used to assay the orientation of aminopeptidase N in the membrane. This enzyme is exposed on the outer surface of the cytoplasmic membrane. Confirmation of this orientation was obtained by comparing the accessibility of aminopeptidase, alkaline phosphatase and beta-galactosidase to fluorescamine in intact cells. Only 16% of the total beta-galactosidase was labeled with this fluorescent reagent whereas 44-45% of the aminopeptidase N and 59% of the alkaline phosphatase were labeled. Electron microscopic visualization of insolubilized reaction products of aminopeptidase N within the cells showed that these products are located at the poles of the cells. Neither mutant cells which were devoid of aminopeptidase N activity nor parental strains with the enzyme activity inhibited with phenylmercuric chloride contained the characteristic black caps. Thus, it appears that the periplasm is enlarged at the poles of the cells and that the reaction product is mainly located in these places. Investigation of the type of interactions of aminopeptidase N with the plasma membrane only revealed that aminopeptidase N has mainly an electrostatic interaction with the outer surface, probably mediated by magnesium ion bridges. Additional interactions are involved since disruption of the integrity of the cytoplasmic membrane is required to totally release this enzyme.
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PMID:Aminopeptidase N from Escherichia coli. Unusual interactions with the cell surface. 32 10

The distribution of lysozyme, alkaline phosphatase, aminopeptidase, maltase and amylase was studied throughout the small intestine of the adult rat. Lysozyme activity increases along the length of the small intestine and the behaviour of this enzyme slightly differs from the mucosal enzymes reported in this investigation. A positive correlation is found between the percentage of crypts with granulated Paneth cells and the lysozyme activity. This corroborates with the secretory origin of this enzyme from these intestinal cells.
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PMID:The quantitative distribution of certain enzymes along the small intestine of the rat and its correlation with the villous area and the Paneth cells. 35 72

The human small intestinal brush border proteins were studied qualitatively by crossed immunoelectrophoresis. Brush border membranes were purified from human jejunum and the proteins released by Triton X-100. Rabbits were immunized with the released proteins and by using a double layer immunofluorescence technique the obtained antisera were shown to be specific against the brush border proteins. The precipitates obtained in crossed immunoelectrophoresis were identified by enzymatic staining techniques. Sucrase (EC 3.2.1.48), isomaltase EC 3.2.1.10), maltase (EC 3.2.1.20), phloretin-glucosidase (EC 3.2.1.62), lactase (EC3.2.1.23), microvillus aminopeptidase (aminopeptidase (microsomal), EC 3.4.11.2), dipeptidyl peptidase IV (EC 3.4.14.X), and alkaline phosphatase (EC 3.1.3.1) were identified while asparate aminopeptidase (EC 3.4.11.7), gamma-glutamyl transferase (EC 2.3.2.2) and trehalase (EC 3.2.1.28) could not be visualized. This work demonstrates that cross immunoelectrophoresis can be used in the study of human small intestinal brush border proteins.
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PMID:Immunoelectrophoretic studies on human small intestinal brush border proteins. A qualitative study of the protein composition. 36 59

Male rats were housed singly in metabolic cages, injected i.v. with cephaloridine, 24 h urine samples collected successively; then the rats were killed for obtaining the kidneys of corresponding animals. The concentrations of protein, aminopeptidase (AP), alkaline phosphatase (aPP), lactic dehydrogenase (LDH), and aldolase (ALD) were determined in urine and the percentages of injured proximal tubules counted in sections stained for aPP. The results from individual animals were: (1) After placing animals singly in metabolic cages large but not systematic changes of urinary enzyme concentrations occurred. After 6-10 days the enzymes reached steady state levels. (2) After a single injection of cephaloridine a dose dependent injury of proximal tubules was observed, the urinary LDH content correlating best with the tubular injury (r greater than 0.93) and giving up to 1,000 fold increases above normal values. (3) A circadian rhythm of the susceptibility of rat kidney for cephaloridine was observed, the smallest response was seen when the animals were injected at 7 a.m. and the largest after injection at 7 p.m. (4) In subacute toxicity studies urinary LDH was increased on day 2 above the extent after a single dose, but declined on day 3 to reach normal levels after 8 to 10 days (time of sacrifice). The kidneys revealed practically normal histology. The other enzymes studied had also returned to normal values. This indicates some adaptation mechanism.
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PMID:Relevance of enzyme evaluations in 24h urine to rat kidney injury caused by i.v. cephaloridine injection. 44 88

The determination of the activity of alkaline phosphatase (AP)--orthophosphate-monoesterphosphohydrolase, EC.3.1.3.1.--and alanine-aminopeptidase (ANA)--alpha-aminoacyl-peptide hydrolase (microsomal), EC.3.4.11.2--in the serum of non-gravid and gravid women has shown that in non-gravid women normal ANA values range from 17.0 to 32.0 I. U. and normal AP values from 14.4 to 26.0 I. U., the ANA/AP quotient amounting to 1.28 (S = +/- 0.301 I. U., KV = 23.5%, n = 29). The determination of the activity of the above quoted enzymes has shown that in the course of pregnancy the values of both enzymes increased by the exponential curve which allowed the calculation of the ANA/AP quotient for each month of pregnancy. The ANA/AP quotient determined in this way is proposed to serve as a diagnostic parameter in the routine control of pregnant women.
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PMID:[Relationship between the activity of alanine aminopeptidase and alkaline phosphatase in the blood of pregnant women]. 61 66

The activity and distribution of acid phosphatase, alkaline phosphatase, nonspecific esterases, beta-glucuronidase, and aminopeptidase were examined in the transplantable R-3327 rat prostatic adenocarcinoma and compared with those in the four prostatic lobes of the rat. Both the well and poorly differentiated tumor cells in R-3327 carcinoma were characterized by high activities of beta-glucuronidase and aminopeptidase. The poorly differentiated cells had a high alkaline phosphatase activity. The enzymatic profile of the R-3327 adenocarcinoma closely resembled that of the anterior and dorsal prostate. The origin of the tumor in one of these prostatic lobes is probable, but not certain.
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PMID:Enzyme activity and distribution in rat prostatic adenocarcinoma. 63 35

Three hundred and forty-seven tissue specimens were studied from 23 patients with male pattern alopecia. Characteristic features of pattern alopecia included: the presence of miniature or vellus follicles; a marked enlargement of the sebaceous glands and arrectores pilorum muscles; the presence of connective tissue streamers beneath the vellus follicles; and the thinning of the dermis. A mild perivascular infiltrate of mononuclear cells and mild capillary dilatation was sometimes seen. An increased number of mast cells was often a prominent feature. Histochemical procedures were performed for glycogen, acid mucosaccharides, inorganic substances, and enzymes including alkaline phosphatase, acid phosphatase, beta glucuronidase, cholinesterase, aminopeptidase, oxidases and dehydrogenases. Histochemical studies did not reveal any significantly abnormal enzyme changes other than the altered vascular and nerve supply to the the miniature follicles.
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PMID:Male pattern alopecia a histopathologic and histochemical study. 77 55

Reports on correlations between the activity of so-called "marker enzymes of cholestasis" in serum and the ultrastructural changes of the liver are rare. Therefore studies of ultrastructural changes were carried out in 40 patients with intrahepatic cholestasis. In the patients' serum activity of alkaline phosphatase, bile duct alkaline phosphatase, leucine-aminopeptidase (LAP), and 5'-nucleotidase (5'-Nu) as well as the concentration of bilirubin were determined. The results showed a significant correlation between the morphometry of the bile canaliculi and the serum activity of LAP and 5'-Nu. In patients with elevated LAP, an enlargement of the bile canaliculi could be proved. An increased serum activity of 5'-Nu correlated with a higher incidence of bile canaliculi in the ultrastructural picture. The results suggest an investigation of the ultrastructure of bile canaliculi and the determination of marker enzymes of cholestasis in the serum may both contribute to the assessment of cholestatic liver disease.
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PMID:[Ultrastructural-morphometric analysis of liver biopsies in patients with intrahepatic cholestasis. I. Correlations between morphometry of bile canaliculi and so-called "marker enzymes of cholestasis" (author's transl)]. 80 5

Rat small bowel was perfused in vivo and ex vivo in the absence of biliary and pancreatic secretion. Intraluminal release of sucrase, alkaline phosphatase, aminopeptidase and enterokinase was significantly increased after administration of PG E1 and E2 1 and 5 microgram/kg. This suggests a direct stimulation of the intestinal mucosa, which might be mediated through cyclic AMP; dibutyryl cAMP significantly stimulates intraluminal release of proteins, sucrase and enterokinase.
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PMID:Prostaglandins E1 and E2 stimulate release of intestinal brush border enzymes. 90 72


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