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

Urinary intestinal alkaline phosphatase (EC 3.1.3.1; IAP) is a marker of the S3 segment of the human kidney proximal tubule. An accurate enzyme-antigen immunoassay (EAIA) with a high-affinity specific monoclonal antibody (IAP250) developed for this marker has a detection limit below the lowest IAP activity found in urine samples of normal subjects. The intra- and interassay CVs were less than 5%. Mean analytical recovery of pure IAP added to urine was 102% (SD 6%), and the EAIA results correlated well with immunoreactivity (measured by a sandwich ELISA), suggesting that the EAIA detected all of the IAP in urine. In healthy individuals (ages 20-80 years) the IAP concentrations, expressed as urinary creatinine ratios, ranged from 0.1 to 2.0 U/g (5-95 percentiles) without major differences related to sex and age. Workers exposed to mercury, which affects the S3 segment, showed an increased IAP elimination; abusers of analgesics, which affect more distal parts of the nephron, did not. As opposed to currently measured markers, the EAIA offers easy, accurate, and precise measurement of early alterations in the S3 segment.
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PMID:Immunoassay in urine of a specific marker for proximal tubular S3 segment. 158 13

Ochratoxin A, produced by a number of fungal species, has been found in many milieu, including porcine sera and coffee beans. It was therefore analysed by enzyme-linked immunosorbent assay (ELISA) in porcine sera, coffee products and fungal cultures, using monoclonal antibodies, a monoclonal antibody-linked immunoaffinity column (IAC) and high-performance liquid chromatography (HPLC). The chloroform extracts of acidified porcine sera were assayed directly by ELISA, with alkaline phosphatase and horseradish peroxidase as marker enzymes, at detection limits of 0.1 and 0.01 ng/ml, respectively. The presence of ochratoxin A in ELISA was confirmed by HPLC. The average contents in the five different lots tested were: 0.4 ng/ml in lot A (19 samples), 0.36 ng/ml in lot B (104 samples), 5.20 ng/ml in lot C (17 samples), 1.24 ng/ml in lot D (23 samples) and 0.22 ng/ml in lot E (24 samples). ELISA of methanol extracts of rice cultures showed the presence of more than 0.1 ng/g in 3 of 15 isolates of Aspergillus, in 16 of 67 isolates of Penicillum and in 7 of 17 isolates of Eupenicillum; none was found in an isolate of Emericella. IAC-HPLC analysis revealed that P. foetidus, which is similar to A. niger and is used for the production of a Japanese alcoholic drink (shou-chuu), also produced ochratoxin A. Use of IAC-HPLC to analyse coffee beans and instant coffee power resulted in the sharp resolution of ochratoxin A without complicated clean-up steps. The IAP-HPLC technique could thus be used for mass surveys of ochratoxin A residues in biological specimens.
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PMID:Use of monoclonal antibodies, enzyme-linked immunosorbent assay and immunoaffinity column chromatography to determine ochratoxin A in porcine sera, coffee products and toxin-producing fungi. 182 Mar 56

Rabbit liver and kidney tissues are known to produce an intestinal-like alkaline phosphatase (IAP-like enzyme) as a dominant isozyme, with a minor isozyme of tissue-unspecific type (UAP), unlike humans and other mammalians. We investigated immunohistochemically and biochemically these unique isozymes in the rabbit liver and bone, and compared them with the human isozyme. In rabbit liver, UAP was found to be localized only in the apical part of the membrane of cells lining the bile duct, whereas IAP-like enzyme was found in the sinusoidal membrane of hepatocytes. Rabbit liver UAP was separated from IAP-like enzyme by DEAE-cellulose column chromatography. Rabbit bone tissue contained only one UAP isozyme. The two UAPs were biochemically and physicochemically compared with human liver AP. Both UAPs reacted with an anti-human liver AP monoclonal antibody, not with an anti-human bone AP monoclonal antibody, indicating that both enzymes have the same antigenicity as human liver AP. Rabbit liver and bone UAPs had similar N-linked sugar-chain heterogeneities to the respective human enzymes. In addition, rabbit bone AP also had an O-linked sugar chain, as did human bone AP, unlike rabbit and human liver APs.
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PMID:Liver-like alkaline phosphatase in the tissue-unspecific type enzyme found in rabbit organs. 193 93

The clinical course of colorectal carcinoma may be monitored by tumor markers such as carcinoembryonic antigen (CEA), carcinoma antigen (CA) 19-9 and CA-50. Alkaline phosphatase isozymes were previously used to study the clinical course of testicular and gynecologic tumors. In this study we investigated 8 patients with advanced colorectal carcinoma. Their sera were analyzed for the tumor markers CEA, CA 19-9, CA-50 and three alkaline phosphatase isozymes: the nonspecific liver isozyme LAP, the intestinal isozyme IAP and the placental isozyme PLAP. Rising levels of CEA, CA 19-9 and CA-50 were seen as expected, and PLAP also showed rising levels during tumor progression. LAP remained elevated. This indicates an association between progression of colorectal carcinoma and a raised serum content of alkaline phosphatase isozymes.
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PMID:Significance of alkaline phosphatase isozymes in the monitoring of patients with colorectal carcinoma. 281 31

There are at least three alkaline phosphatase (AP) isoenzymes in man: a heat-stable placental enzyme (PLAP), a less heat-stable intestinal form (IAP), and the very heat-labile AP enriched in liver, bone and kidney. In addition to these enzymes, there is a heat-stable activity in the thymus and testis that is similar but not identical to the PLAP (the PLAP-like enzyme). Previous work has demonstrated a close structural relatedness among the IAP, PLAP and PLAP-like enzymes. Thus, it is possible that there are three human genes encoding heat-stable AP enzymes. To test this hypothesis, we have used a PLAP cDNA clone to screen a human genomic library cloned into the phage vector lambda EMBL-3. Three sets of clones were isolated, each bearing a distinct coding region homologous to the PLAP cDNA probe. Nucleotide sequence analysis of the 5' ends of these genes allowed comparison of their derived peptide sequences and positive identification of two of the genes. One of the genes encodes the PLAP (the PLAP-1 gene), another encodes the IAP, and a third closely resembles the PLAP-1 gene, but is distinct from it (the PLAP-2 gene). The PLAP-2 gene is highly homologous (greater than 95%) with the PLAP-1 except in the first exon, where sequences encoding the hydrophobic signal peptide are nearly identical with the same region of the IAP gene. These results demonstrate the existence of a small family of PLAP-related genes which is the result of at least two duplication events during the descent of man.
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PMID:Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. 344 2

Antibodies against placental alkaline phosphatase (PAP) share antigenic determinants with the intestinal isoenzyme (IAP) and vice versa. Both isoenzymes can be found as part of the total activity of alkaline phosphatase (AP) in the serum. Using antibody-coated polystyrene tubes, a simple and sensitive immunoassay was developed which allows the quantitative determination of IAP or PAP without interference of the cross-reacting isoenzyme. The presence and amount of IAP depends on the ABO blood group, secretory status and the oral fat intake. The serum IAP in healthy fasted individuals was found up to 8 U/I in secretors of blood group O and B and below 1 U/I in non-secretors and blood group A donors. In screening tests of various pathological sera. IAP was found elevated up to 100 U/I in idiopathic hyper-AP-aemia and some liver cirrhosis patients.
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PMID:Solid-phase direct immunoassay for serum intestinal and placental alkaline phosphatase. 686 36

The current information on the cloning and sequencing of four alkaline phosphatase genes (PLAP, GCAP, IAP, TNAP) has been reviewed. It has provided insights into their evolutionary history and the mechanisms of catalysis and of uncompetitive inhibition. The oncodevelopmental biology of the germ cell and its excessive GCAP eutopic expression in neoplasia are noted, and there is reason to suggest that the enzyme may serve to guide migratory cells and to transport specific molecules such as fat and immunoglobulins across membranes. The hyperexpression of all four genes has been observed in various human tumors and in their cell lines, particularly cancers of the testis and ovary. The membrane APs have been investigated as targets for immunolocalization and immunotherapy.
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PMID:Biology of human alkaline phosphatases with special reference to cancer. 774 66

A computer aided multivariate pattern analysis system (CAMPAS) OV-1, which consisted of 10 discriminant functions based on eight tumor markers including CA125, IAP, TPA, LDH, CRP, CEA, amylase and alkaline phosphatase was developed to effectively diagnose patients with epithelial ovarian carcinoma. One hundred twenty-two patents with epithelial ovarian carcinoma and 215 patients with benign ovarian tumors were examined by using CAMPAS OV-1 retrospectively or prospectively. The clinical significance of CAMPAS OV-1 was compared with CA125 alone, and with a combined assay employing the eight tumor markers used in CAMPAS OV-1. The following results were obtained. 1. When CAMPAS OV-1 was applied to patients in which the value for each tumor marker was used to make the discriminant functions, the sensitivity, specificity and accuracy were 84.5%, 97.5% and 91.3%, respectively. The accuracy of CAMPAS OV-1 (91.3%) was significantly better than those of CA125 (80.0%) and combined assay (74.0%) [p < 0.001]. CAMPAS OV-1 showed relatively better sensitivity (63.3%) than CA125 (50.0%) in patients with stage I disease. Also CAMPAS OV-1 showed relatively better sensitivity (85.7%) than both CA125 (64.3%) and combined assay (78.6%) in patients with mucinous type tumors. Furthermore, the specificity of CAMPAS OV-1 (94.4%) was significantly better than those of CA125 (66.7%) and combined assay (55.6%) in patients with endometrial cysts [p < 0.05]. 2. When CAMPAS OV-1 was applied to the patients prospectively, whose values for each tumor marker were not used to make the discriminant functions, the sensitivity, specificity and accuracy were 88.2%, 83.8% and 85.0% respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Development and clinical research of computer aided multivariate pattern analysis system (CAMPAS) OV-1 for diagnosis of ovarian carcinoma]. 849 11

Treatment of rat parotid tissues with 1 microM isoproterenol (IPR) for 10 min caused a 60% decrease in pertussis toxin (IAP)-catalyzed ADP-ribosylation of Gi alpha and resulted in supersensitivity of amylase secretion from the tissues. However, conversely, IPR treatment for 30 min caused a 40% increase in IAP-catalyzed ADP-ribosylation of Gi alpha, coupled with desensitization of amylase secretion. No changes in Gs function were observed in IPR-induced phenomena. Pretreatment with okadaic acid induced enhancement of the supersensitivity of amylase secretion and disappearance of the desensitization. These phenomena were accompanied with decreases in IAP-catalyzed ADP-ribosylation of Gi alpha. IPR treatment for 30 min caused a 50% decrease in phosphorylation of Gi2 alpha immunoprecipitated with anti-G protein antiserum (AS/7) from [32P]Pi-labeled cells, but such treatment for 10 min caused a 40% increase in phosphorylation in the cells pretreated with okadaic acid. Phosphorylation and dephosphorylation of immunoprecipitates with AS/7 by protein kinase A (PKA) and alkaline phosphatase caused decreases and increases in IAP-catalyzed ADP-ribosylation, respectively, indicating the presence of PKA-mediated phosphorylation sites on Gi2 alpha. Thus, the control of the phosphorylation of Gi2 alpha is of importance and relevance in the regulation of biological processes and cellular responses.
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PMID:Regulation of phosphorylation of Gi2 alpha protein controls the secretory response to isoproterenol in rat parotid tissues. 878 62

The effect of retinoic acid and dexamethasone on alkaline phosphatase (AP) expression was investigated in human breast cancer MCF-7 cells. Cellular AP activity was induced significantly by retinoic acid or dexamethasone in a time-dependent and dose-dependent fashion. A marked synergistic induction of AP activity was observed when the cells were incubated with both agents simultaneously. Two AP isozymes, tissue-nonspecific (TNAP) and intestinal (IAP), were shown to be expressed in MCF-7 cells as confirmed by the differential rate of thermal inactivation of these isozymes and RT-PCR. Based on the two-isozyme thermal-inactivation model, the specific activities for TNAP and IAP in each sample were analyzed. TNAP activity was induced only by retinoic acid and IAP activity was induced only by dexamethasone. Whereas dexamethasone conferred no significant effect on TNAP activity, retinoic acid was shown to inhibit IAP activity by approximately 50%. Interestingly, TNAP was found to be the only isozyme activity superinduced when the cells were costimulated with retinoic acid and dexamethasone. Northern blot and RT-PCR analysis were then used to demonstrate that the steady-state TNAP mRNA level was also superinduced, which indicates that the superinduction is regulated at the transcriptional or post-transcriptional levels. In the presence of the glucocorticoid receptor antagonist RU486, the dexamethasone-mediated induction of IAP activity was blocked completely as expected. However, the ability of RU486 to antagonize the action of glucocorticoid was greatly compromised in dexamethasone-mediated superinduction of TNAP activity. Furthermore, in the presence of retinoic acid, RU486 behaved as an agonist, and conferred superinduction of TNAP gene expression in the same way as dexamethasone. Taken together, these observations suggest that the induction of IAP activity by dexamethasone and the superinduction of TNAP by dexamethasone were mediated through distinct regulatory pathways. In addition, retinoic acid plays an essential role in the superinduction of TNAP gene expression by enabling dexamethasone to exert its agonist activity, which otherwise has no effect.
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PMID:Expression and regulation of alkaline phosphatases in human breast cancer MCF-7 cells. 1069 70


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