Perspectives on alkaline phosphatase isoenzymes

Fishman, William H.

doi:10.1016/0002-9343(74)90631-7

Cited by 393 publications

(130 citation statements)

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“…Since tissue-unspecific ALP is more sensitive than I-ALP to heat treatment at 65°C for 10 min, while P-ALP is most stable, and the activities of I-ALP and P-ALP, but not tissue-unspecific ALP, are strongly inhibited by L-phenylalanine, 25,26) our results suggest that neither tissue-unspecific ALP nor P-ALP is a main component of the total ALP (data not shown). Considering the fair comparability between values for I-ALP and total ALP, we can therefore conclude that a considerable part of the total ALP activity in gastric carcinomas is due to I-ALP itself.…”

Section: Discussionmentioning

confidence: 71%

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Increased Expression of Sucrase and Intestinal‐type Alkaline Phosphatase in Human Gastric Carcinomas with Progression

Nakamura

Inada

Hirano

et al. 1998

Japanese Journal of Cancer Research

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The activities of sucrase, total alkaline phosphatase (total ALP) and intestinal-type alkaline phosphatase (I-ALP) were assayed in gastric carcinomas and in their surrounding mucosae from 57 patients with advanced cancers, and the localization of sucrase in 203 carcinomas, including 86 early cancers, was examined immunohistochemically using polyclonal anti-sucrase antibody. All three enzymes were active in the 57 carcinomas as well as in their surrounding mucosae, but the levels were fairly low as compared to those in normal jejunum mucosa. A considerable part of the total ALP activity in tumor specimens was assumed to be due to I-ALP itself. Increased sucrase and I-ALP were found with greater depth of invasion by undifferentiated-type carcinomas. The pattern of immunohistochemical localization of sucrase in the 203 carcinomas also clearly indicated increased expression with greater depth of invasion even in differentiated-type carcinomas.

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Section: Discussionmentioning

confidence: 71%

“…The residual enzyme activities after heat treatments at 60°C for 10 min and 65°C for 10 min were found to be about 60% and 35% of the initial enzyme activities, respectively. In the presence of 20 mM L-phenylalanine the 25. Thus, considerable variability was noted for all three parameters.…”

Section: Enzyme Activitiesmentioning

confidence: 90%

Increased Expression of Sucrase and Intestinal‐type Alkaline Phosphatase in Human Gastric Carcinomas with Progression

Nakamura

Inada

Hirano

et al. 1998

Japanese Journal of Cancer Research

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“…Alkaline phosphatase (ALP) (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) in mammalian cells is a membrane-bound glycoprotein and a marker enzyme for the plasma membrane (Pekarthy et al, 1972;Fishman, 1974). The enzyme has many interesting aspects to be investigated because of its inducibility, genetic polymorphism, ectopic expression etc.…”

Section: Introductionmentioning

confidence: 99%

“…(McComb et al, 1979). At least three types of ALP (isoenzymes) are identified in human tissues: placental, intestinal and tissue-unspecific (referred to below as the liver-type) isoenzymes (Fishman, 1974). Available evidence, however, indicates that only two types of ALP are detectable in other animals, including the rat, where ALP in placenta is the liver-type isoenzyme (Goldstein et al, 1980).…”

Section: Introductionmentioning

confidence: 99%

Primary structure of rat liver alkaline phosphatase deduced from its cDNA

Misumi

Tashiro

Hattori

et al. 1988

Biochemical Journal

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Rat liver alkaline phosphatase (ALP) was markedly induced by treatment of rats by bile-duct ligation and colchicine injection. Taking this advantage for enrichment of ALP mRNA, we constructed a Agtl 1 liver cDNA library using polyadenylated RNA prepared from the treated rat liver, and isolated an ALP cDNA clone. The 2165 bp cDNA contained an open reading frame that encodes a 524-amino-acid-residue polypeptide with a predicted molecular mass of 57737 Da. The precursor protein contained a presumed signal peptide of 17 amino acid residues followed by 28 amino acid residues identical with the N-terminal sequence determined from the purified rat liver ALP. It was also confirmed that amino acid sequences of two CNBr-cleavage peptides obtained from liver ALP were contained within the cDNA-encoded protein.Five possible N-linked glycosylation sites were found in the molecule and a highly hydrophobic amino acid sequence at the C-terminus. The deduced polypeptide of rat liver ALP showed 88 % homology to that of the human liver-type enzyme in osteosarcoma cells. RNA blot hybridization analysis identified a single species of ALP mRNA with 2.7 kb in both the control and the treated rat livers. An approx. 20-fold increase of the mRNA was detected in the treated liver at 12 h after the onset of stimulation, compared with that in the control liver.

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“…One codes for the tissue unspecific alkaline phosphatase (liver-bone-kidney type), at least one for the intestinal alkaline phosphatase and at least one for PLAP [1,2]. These three isoenzymes show quite different peptide maps on two-dimensional gels [2,3], and can be distinguished from each other immunochemically and on catalytic grounds [4 -61 (for review see [7,8]). PLAP and the intestinal alkaline phosphatase seem to be more closely related to each other than to the tissue unspecific enzyme.…”

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confidence: 99%

Antigenic determinants of human placental and testicular placental‐like alkaline phosphatases as mapped by monoclonal antibodies

Millán

Stigbrand

1983

European Journal of Biochemistry

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Placental alkaline phosphatase (PLAP) in humans shows a high degree of genetic polymorphism as disclosed by electrophoretic analysis. Human testes contain trace amounts of a PLAP-like enzyme, that although immunologically cross-reactive with PLAP, shows unique catalytic properties.As an alternative approach to study enzyme polymorphism we have developed monoclonal antibodies to purified allelic variants of PLAP. Five different monoclonal antibodies are described in this report. The antibodies react with different epitopes on the PLAP molecule. Both conformational dependent and independent determinants are detected. Two epitopes are modified when comparing the S and F allelic variants of PLAP. One epitope is common to PLAP and the intestinal isoenzyme of alkaline phosphatase. The five epitopes appear to be mapped on two rather distant antigenic domains. Combinations of any two antibodies binding to different domains give immunoprecipitates with PLAP on Ouchterlony tests and give good response in sandwich enzyme-linked immunosorbent assays.A study of PLAP-like enzyme in 32 individual testis samples indicates differences in four of the epitopes when compared with PLAP. Four types of testicular enzymes can be distinguished based on their reactivities. These results indicate structural differences between the testicular PLAP-like enzyme and PLAP. These differences are compatible with an underlying genetic mechanism.Alkaline phosphatases in humans are encoded by at least three different structural gene loci. One codes for the tissue unspecific alkaline phosphatase (liver-bone-kidney type), at least one for the intestinal alkaline phosphatase and at least one for PLAP [1,2]. These three isoenzymes show quite different peptide maps on two-dimensional gels [2,3], and can be distinguished from each other immunochemically and on catalytic grounds [4 -61 (for review see [7,8]). PLAP and the intestinal alkaline phosphatase seem to be more closely related to each other than to the tissue unspecific enzyme. They are cross-reactive with polyclonal antibodies against either of them. PLAP is particularly interesting, since it is a rather late evolutionary gene product, detectable only in orangutan, chimpanzee and human placentae [9, lo]. It displays a high degree of genetic polymorphism. Three common and more than 15 rare allelic variants have been described by use of electrophoresis on starch gels [l I]. PLAP is a dimeric enzyme, composed of subunits of approximately 65 kDa. The three common alleles Pis, PIF and PI' (new nomenclature PI', PI2 and PI3) give rise to six homozygous and heterozygous phenotypes S, FS, F, SI, FI, I (new nomenclature l, 2-1,2,3-1,3-2,3)that comprise approximately 98 % of all the placental variants.The structural difference between these allelic variants has as yet not been elucidated.Further interest in the placental enzyme stems from the demonstration that PLAP and PLAP-like enzymes are proAbbreviations. PLAP, placental alkaline phosphatase; ELISA, enzyme-linked immunosorbent assay; HRP, horse-radish ...

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Perspectives on alkaline phosphatase isoenzymes

Cited by 393 publications

References 258 publications

Increased Expression of Sucrase and Intestinal‐type Alkaline Phosphatase in Human Gastric Carcinomas with Progression

Increased Expression of Sucrase and Intestinal‐type Alkaline Phosphatase in Human Gastric Carcinomas with Progression

Primary structure of rat liver alkaline phosphatase deduced from its cDNA

Antigenic determinants of human placental and testicular placental‐like alkaline phosphatases as mapped by monoclonal antibodies

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