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

Henthorn, Paula S.; Raducha, Michael; Edwards, Yvonne H.; Weiss, Mitchell J.; Slaughter, Clive A.; Lafferty, Mary Ann; Harris, Harry

doi:10.1073/pnas.84.5.1234

Cited by 113 publications

(46 citation statements)

References 32 publications

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“…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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Section: General Molecular Propertiesmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

890

922

View full text Add to dashboard Cite

show abstract

“…The lactase probe was provided by R. Grand (New England Medical Center, Boston, MA) and is a 1.8-kb EcoRI/PstI fragment derived from the rat cDNA clone (24). An intestinal alkaline phosphatase (IAP) probe was obtained from the American Type Culture Collection and is a 1.9-kb PstI fragment derived from human IAP cDNA (25). The villin probe is a 530-bp fragment from human cDNA and was provided by M. Arpin (Institut Pasteur, Paris, France) (26).…”

Section: Methodsmentioning

confidence: 99%

Na-K-2Cl cotransporter gene expression and function during enterocyte differentiation. Modulation of Cl- secretory capacity by butyrate.

Matthews

Hassan²,

Meng³

et al. 1998

J. Clin. Invest.

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“…Oligonucleotide screening of phage plaques was carried out essentially as described by Vinson et al (39) with a Agtl 1 cDNA library generated from HeLa cells (12). The oligonucleotide used as the probe contained the ,uE5 and ,uE2 sites of the IgH enhancer and was described previously (30).…”

Section: Methodsmentioning

confidence: 99%

Displacement of an E-box-binding repressor by basic helix-loop-helix proteins: implications for B-cell specificity of the immunoglobulin heavy-chain enhancer.

Genetta¹,

Ruezinsky²,

Kadesch³

1994

Mol. Cell. Biol.

159

197

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The activity of the immunoglobulin heavy-chain (IgH) enhancer is restricted to B cells, although it binds both B-cell-restricted and ubiquitous transcription factors. Activation of the enhancer in non-B cells upon overexpression of the basic helix-loop-helix (bHLH) protein E2A appears to be mediated not only by the binding of E2A to its cognate E box but also by the resulting displacement of a repressor from that same site.We have identified a "two-handed" zinc finger protein, denoted ZEB, the DNA-binding specificity of which mimics that of the cellular repressor. By employing a derivative E box that binds ZEB but not E2A, we have shown that the repressor is active in B cells and the IgH enhancer is silenced in the absence of binding competition by bHLH proteins. Hence, we propose that a necessary prerequisite of enhancer activity is the B-cell-specific displacement of a ZEB-like repressor by bHLH proteins.

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

Cited by 113 publications

References 32 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Na-K-2Cl cotransporter gene expression and function during enterocyte differentiation. Modulation of Cl- secretory capacity by butyrate.

Displacement of an E-box-binding repressor by basic helix-loop-helix proteins: implications for B-cell specificity of the immunoglobulin heavy-chain enhancer.

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