Developmental change in human intestinal alkaline phosphatase.

Mulivor, R.A.; Hannig, Vickie; Harris, Harry

doi:10.1073/pnas.75.8.3909

Cited by 84 publications

(50 citation statements)

References 27 publications

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“…a difference in the polypeptide chain expression of a fetal gene, as described for instance for myosin (14) or hemoglobin (9), or to differences in the glycosylated part of the molecules. Fetal intestinal alkaline phosphatase has a different electrophoretic mobility than the adult enzyme, which disappears after neuraminidase treatment (6). Preliminary results of analysis of meconial brush-border enzymes have shown a modified affinity for Concanavalin A (2).…”

Section: ;mentioning

confidence: 99%

Maturation of Sucrase-Isomaltase Complex in Human Fetal Small and Large Intestine during Gestation

Triadou

Zweibaum

1985

Pediatr Res

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ABSTRACT. Sucrase-isomaltase complex is expressed in human small intestine throughout gestation and in the large intestine between 12 and 30 wk. The molecular form of the enzyme was studied in the brush-border membrane fractions by the immunoblotting method. Before 30 wk of gestation, the enzyme is present only as the high molecular weight prosucrase-isomaltase, while from 30 wk until birth the two subunits are also present. The fetal enzyme, as its proform and as its two subunits, has a faster mobility in sodium-dodecylsulfate polyacrylamide gel electrophoresis, than the adult enzyme (removal of sialic acid residues from fetal enzymes emphasizes this difference Sucrose a-D-glucohydrolase complex (EC 3.2.1.48) is the main marker of enterocytic differentiation, and one of the primary intestinal brush-border enzymes (4). Recently it has been shown in mammals to be synthetized as a single chain secondarily split to two subunits by pancreatic proteases (3,7,13). In early human fetal small intestine the enzyme is present as high molecular weight single chain (8), which is split in vitro by pancreatic elastase. This enzyme also is expressed at a lower level in human fetal colonic mucosa between 10 and 30 wk. The activity disappears at term and is not expressed in adult colon (5, 15). We studied the spontaneous maturation of human fetal small intestinal and colonic sucrase-isomaltase complex throughout gestation, and compared the fetal and adult enzymes. MATERIALS AND METHODSSmall intestinal samples ( n = 6) and colon samples ( n = 4) from human fetuses between 16 and 39 wk of gestation were obtained after spontaneous or legal therapeutic abortion afid stored at -80" C until use. Adult intestinal fragments were obtained from irreversibly brain damaged kidney donors as previously described (1 2, 15). Purification of sucruse complex and antibodies production.Sucrase-isomaltase from a blood group 0 human small intestine was purified as previously described (10, 15). Briefly brushborders were digested with papain; the papain supernatant was applied on sequential chromatographic columns including anion exchange chromatography, gel filtration, and Sephadex G 200 chromatography. The homogeneity of the preparation was assessed by polyacrylamide gel electrophoresis and crossed immunoelectrophoresis against an antihuman brush-border antiserum (1 2). Rabbits were immunized by sc injections at 15-day intervals with 0.2 mg of purified enzyme and bled 7 days after the fourth injection. Immunoglobulins G were prepared by ion exchange chromatography (1 0, 15). Brush-border separation, transjer, and identification of antigen.Preparations of the brush-border fractions of small and large intestine were obtained by the calcium precipitation method as previously described (12). The proteins were separated on polyacrylamide slab gel electrophoresis, with molecular weight markers (myosin: 200 k, 0-galactosidase 116 k, phosphorylase b 94 k). The proteins were then transferred on nitrocellulose sheets as previously described (1 1). The nitroce...

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Section: ;mentioning

confidence: 99%

Maturation of Sucrase-Isomaltase Complex in Human Fetal Small and Large Intestine during Gestation

Triadou

Zweibaum

1985

Pediatr Res

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“…Three structurally distinct ALPase isoenzymes (placenta, intestine, and bone/ kidney/liver types) have been well characterized. The type of these enzymes can be determined by specific inhibitors (21). The bone/kidney/liver type are known to be inhibited by L-homoarginine drastically and by L-phenylalanine or L-leucine slight ly.…”

Section: Discussionmentioning

confidence: 99%

Increase in the Activity of Alkaline Phosphatase by L-Ascorbic Acid 2-Phosphate in a Human Osteoblast Cell Line, HuO-3N1.

Hitomi

Torii

Tsukagoshi

1992

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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SummaryThe activity of alkaline phosphatase (ALPase) was signifi cantly enhanced in a human osteoblast cell line, Hu0-3N1, when it was cultured in the presence of L-ascorbic acid 2-phosphate (ASA-P; a stable ascorbic acid derivative). With AsA-P in the culture, the level of ALPase activity increased approximately 3-fold without any effect on either the morphology or growth rate. This increase was dependent on the AsA-P concentration in the range of 0.2-2 mM and required at least 48 h incuba tion with AsA-P. The ALPase mRNA level, however, remained rather constant irrespective of the enzyme activity. Removal of AsA-P from the precultured medium decreased the stimulatory effect of ascorbic acid on the ALPase activity, indicating that the effect was reversible. Dexametha sone, an inducer for osteoblastic differentiation, enhanced the level of ALPase activity irreversibly, in parallel with the increase in the level of its mRNA. The enhancement of the ALPase activity by ascorbic acid in this cell line appeared to be independent of cell differentiation.

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“…In part, this is due to the presence of sialic acid residues in the fetal form and their absence in the adult forms. But even after desialation, they still show small but significant differences in electrophoretic mobility [5]. It is not at present clear whether this arises from structural differences in the protein or in the carbohydrate moieties.…”

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confidence: 91%

“…Two forms of normal intestinal ALP have been identified : adult and fetal [5,6]. They are indistinguishable in terms of their inhibition characteristics with various amino acid and peptide inhibitors and in thermostability, by which criteria they are sharply differentiated from placental or liver/bone/ kidney ALPs [6].…”

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confidence: 99%

Monoclonal antibodies against placental‐like and intestinal‐like alkaline phosphatases in a malignant human cell line

Wray

Harris

1984

European Journal of Biochemistry

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Monoclonal antibodies were raised against alkaline phosphatase (ALP) from the malignant human cell line Hep2, a derivative of HeLa, which was established from a cervical carcinoma. Two forms of ALP are found in Hep2 cells resembling, but not identical to, the normal placental and intestinal ALPs. Seven monoclonal antibodies were raised against Hep2 ALP. All of these reacted nearly identically with normal placental ALP and the placental‐like ALP from Hep2 cells. Three of these antibodies exhibited reduced reactivities for either the common type 2 or 3 allelic variants of placental ALP. From these binding studies, the placental‐like ALP from Hep2 cells appears to be a slightly modified form of the normal type 1 placental ALP. One of the seven antibodies bound to the adult and fetal intestinal ALPs, but more strongly to the adult form, suggesting that the Hep2 intestinal‐like ALP is a form of the normal adult intestinal ALP.

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Developmental change in human intestinal alkaline phosphatase.

Cited by 84 publications

References 27 publications

Maturation of Sucrase-Isomaltase Complex in Human Fetal Small and Large Intestine during Gestation

Maturation of Sucrase-Isomaltase Complex in Human Fetal Small and Large Intestine during Gestation

Increase in the Activity of Alkaline Phosphatase by L-Ascorbic Acid 2-Phosphate in a Human Osteoblast Cell Line, HuO-3N1.

Monoclonal antibodies against placental‐like and intestinal‐like alkaline phosphatases in a malignant human cell line

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