Structural analysis of human adult and fetal alkaline phosphatases by cyanogen bromide peptide mapping.

Vockley, Jerry; D’Souza, M. Patricia; Foster, Carolyn; Harris, Harry

doi:10.1073/pnas.81.19.6120

Cited by 17 publications

(8 citation statements)

References 16 publications

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“…Its relationship to placental ALP is not yet clear, but it seems probable that it is the product of a separate locus (35). There is also evidence that the adult and fetal forms of intestinal ALP may be determined by separate loci (7,14,36). Thus it is possible that at least five different loci are involved in coding for the various ALPs.…”

Section: Discussionmentioning

confidence: 99%

“…In man and other higher primates, these membrane-bound glycoproteins appear to be the products of at least three related gene loci, named after the tissues in which they are characteristically expressed [placental, intestinal, and liver/bone/kidney (L/B/K) ALPs] (2-5). These conclusions are based on an abundance of biochemical, immunological, and direct protein sequence data, which also indicate that the placental and intestinal ALPs are more closely related to each other than either is to L/B/K ALP (2,(6)(7)(8). More recently, cDNA clones of placental and L/B/K ALPs have been isolated (9)(10)(11)(12).…”

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confidence: 99%

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Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase.

Henthorn

Raducha

Edwards

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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113

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A cDNA clone for human adult intestinal alkaline phosphatase (ALP) [orthophosphoric-monoester phosphohydrolase (alkaline optimum); EC 3.1.3.1] was isolated from a lambda gt11 expression library. The cDNA insert of this clone is 2513 base pairs in length and contains an open reading frame that encodes a 528-amino acid polypeptide. This deduced polypeptide contains the first 40 amino acids of human intestinal ALP, as determined by direct protein sequencing. Intestinal ALP shows 86.5% amino acid identity to placental (type 1) ALP and 56.6% amino acid identity to liver/bone/kidney ALP. In the 3'-untranslated regions, intestinal and placental ALP cDNAs are 73.5% identical (excluding gaps). The evolution of this multigene enzyme family is discussed.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase.

Henthorn

Raducha

Edwards

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

113

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“…ALP was isolated from single placentas by standard biochemical techniques as described (7) or by immunoaffinity chromatography as described (8).…”

Section: Methodsmentioning

confidence: 99%

Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids.

Henthorn¹,

Knoll²,

Raducha³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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Amino-terminal amino acid sequences (42 residues) were determined for the products of the three common alleles at the human placental alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] gene locus. The sequences differ at position 3, which is proline in types 1 and 2 but is leucine in type 3. cDNA libraries were constructed in phage Xgtl1 and used to isolate clones covering the coding regions of types 1 and 3 cDNAs. Comparison of the deduced amino acid sequences of the types 1 and 3 proteins showed 7 differences out of 513 amino acids, each due to a single base substitution. cDNA sequence comparisons showed three silent substitutions in the coding regions and three base differences in the greater than 1 kilobase pairs of 3' untranslated sequences.

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“…The rationale for this hypothesis is that the intestinal mucosa harbours a heterogeneous population of cells that could be discriminated according to their state of differentiation. Because differentiation of intestinal cells is accompanied by marked changes in the levels of oligosaccharyltransferases [30][31][32][33][34][35][36][37][38], it is reasonable to assume that the extent of glycosylation of ACE depends on the differentiation state of the various subpopulations of the intestinal cells.…”

Section: Secreted Ace Is Synthesized and Processed By Crypt Cellsmentioning

confidence: 99%

Secretion of human intestinal angiotensin-converting enzyme and its association with the differentiation state of intestinal cells

Naim

1996

Biochemical Journal

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Human angiotensin I-converting enzyme (ACE) exists in intestinal epithelial cells as a membrane-bound (ACEm) and secretory glycoprotein (ACEsec). The electrophoretic mobilities of ACEsec and ACEm on SDS/polyacrylamide gels are similar; the N-deglycosylated ACEsec and ACEm, in contrast, display slight differences in their apparent molecular masses, indicating that the carbohydrate contents of ACEsec and ACEm are different. Moreover, ACEsec is solely N-glycosylated whereas ACEm is N- and O-glycosylated, assessed by lectin binding studies. Spontaneous release of ACEsec is achieved by incubation of brush border membranes at 37 degrees C. Aprotinin, leupeptin and EDTA partly inhibit the generation of ACEsec, strongly suggesting that ACEsec is generated from ACEm by proteolytic cleavage. The expression levels of ACEsec in the intestine may be associated with the differentiation state of mucosal cells. Thus ACEsec is more abundant than ACEm in immature non-epithelial crypt cells of patients with coeliac disease. Well-differentiated epithelial cells, by contrast, contain predominantly ACEm. The variations in the proportions of cleaved ACEsec in differentiated and non-differentiated cells may be due to varying levels of the cleaving protease. Alternatively, because epithelial cell differentiation is accompanied by alterations in the levels of oligosaccharyltransferases, the results suggest a critical role for the glycosylation pattern of ACEm in its susceptibility to the putative cleaving protease.

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Structural analysis of human adult and fetal alkaline phosphatases by cyanogen bromide peptide mapping.

Abstract: The adult and fetal forms of human intestinal alkaline phosphatase (ALPase; orthophosphoric-monoester phosphohydrolase, EC 3.1.3

Cited by 17 publications

References 16 publications

Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase.

Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase.

Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids.

Secretion of human intestinal angiotensin-converting enzyme and its association with the differentiation state of intestinal cells

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