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

Henthorn, Paula S.; Knoll, Brian J.; Raducha, Michael; Rothblum, Katrina; Slaughter, Clive A.; Weiss, Mitchell J.; Lafferty, Mary Ann; Fischer, Tom T.; Harris, Harry

doi:10.1073/pnas.83.15.5597

Cited by 69 publications

(51 citation statements)

References 29 publications

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“…The signal peptide for human intestinal ALP has 19 amino acid residues (Berger et al, 1987), whereas different values have been given for that of placental ALP, 17 (Kam et al, 1985) and 22 amino acid residues (Millan, 1986;Henthorn et al, 1986), though the reason for this discrepancy is not clear. The active site 'Asp-Ser-Ala' is well conserved at similar positions in human intestinal (Ser92), placental (Ser92) and liver-type (Ser93) ALPs as well as in rat liver ALP (Ser93), except that its third residue Ala is replaced by Gly in human placental ALP, probably considered to be one of data supporting the view that human placental ALP is a new evolutionary gene product (Goldstein et al, 1980).…”

Section: Discussionmentioning

confidence: 97%

“…5). Such a hydrophobic domain at the C-terminus (17-23 amino acid residues) is also commonly observed in primary structures of human ALP isoenzymes predicted by their cDNAs (Kam et al, 1985;Millan, 1986;Henthorn et al, 1986;Weiss et al, 1986;Berger et al, 1987). This domain could be involved in attachment of the ALP molecule to membranes at least during or just after its synthesis.…”

Section: Discussionmentioning

confidence: 99%

“…In the present study we constructed a Agtl1 liver cDNA library using poly(A)+ RNA prepared from the treated rat liver, and isolated an ALP cDNA clone. During the progress of this study many efforts have been successfully made for elucidating the molecular detail of human ALPs by cloning and sequencing of cDNAs for the isoenzymes in placenta (Kam et al, 1985;Millan, 1986;Henthorn et al, 1986), intestine (Berger et al, 1987) and osteosarcoma cells . All of these tissues and cells are known to possess extremely high ALP activity.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Primary structure of rat liver alkaline phosphatase deduced from its cDNA

Misumi

Tashiro

Hattori

et al. 1988

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…The sequences of the cDNAs for the human APs were published in the 1980s (PLAP [522][523][524], IAP [525,526], TNAP [527,528], and GCAP [529,530]). This was followed by the cloning and characterization of the corresponding genes.…”

Section: General Molecular Propertiesmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

890

922

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Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

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“…To distinguish these possibilities, β-galactosidase was replaced by the mammalian reporter gene human PLAP. Previous studies have demonstrated that PLAP functions as a robust reporter in transgenic mice and can be detected in tissue sections as well as by FACS [32,[40][41][42][43][44][45][46][47][48][49][50].…”

Section: Scl +19 Core Enhancer Targets Plap Expression To Endotheliummentioning

confidence: 99%

Transgenic Analysis of the Stem Cell Leukemia +19 Stem Cell Enhancer in Adult and Embryonic Hematopoietic and Endothelial Cells

et al. 2005

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Appropriate transcriptional regulation is critical for the biological functions of many key regulatory genes, including the stem cell leukemia (SCL) gene. As part of a systematic dissection of SCL transcriptional regulation, we have previously identified a 5,245-bp SCL +18/19 enhancer that targeted embryonic endothelium together with embryonic and adult hematopoietic progenitors and stem cells (HSCs). This enhancer is proving to be a powerful tool for manipulating hematopoietic progenitors and stem cells, but the design and interpretation of such transgenic studies require a detailed understanding of enhancer activity in vivo. In this study, we demonstrate that the +18/19 enhancer is active in mast cells, megakaryocytes, and adult endothelium. A 644-bp +19 core enhancer exhibited similar temporal and spatial activity to the 5,245-bp +18/19 fragment both during development and in adult mice. Unlike the +18/19 enhancer, the +19 core enhancer was only active in adult mice when linked to the eukaryotic reporter gene human placental alkaline phosphatase. Activity of a single core enhancer in HSCs, endothelium, mast cells, and megakaryocytes suggests possible overlaps in their respective transcriptional programs. Moreover, activity in a proportion of thymocytes and other SCL-negative cell types suggests the existence of a silencer elsewhere in the SCL locus.

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

Cited by 69 publications

References 29 publications

Primary structure of rat liver alkaline phosphatase deduced from its cDNA

Primary structure of rat liver alkaline phosphatase deduced from its cDNA

Cellular function and molecular structure of ecto-nucleotidases

Transgenic Analysis of the Stem Cell Leukemia +19 Stem Cell Enhancer in Adult and Embryonic Hematopoietic and Endothelial Cells

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