Literature DB >> 8542444

Immunohistochemical localization of NAD glycohydrolase in human and rabbit tissues.

M K Han1, J H Kim, D G Lee, U H Kim.   

Abstract

NAD glycohydrolase (NADase) is present in many organisms from bacteria to mammals. In any given organism, this enzyme is ubiquitous in many tissues. However, its precise localization and its physiological significance have not been defined. We have determined the distribution of NADase in normal human and rabbit tissues by immunoblotting and immunohistochemistry, using a polyclonal antibody raised in goats. Immunoblot analyses revealed that NADase was highly expressed in the heart, lung, stomach, and liver tissues of the rabbit. From immunohistochemical studies of NADase, high concentrations in both human and rabbit tissues were found in hepatocytes and sinusoidal lining cells, sinus histiocytes of the lymph node, spleen and thymus, glomerular capillary endothelial cells of the kidney, cardiac muscle, endothelium of blood vessels, and erythrocytes.

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Year:  1995        PMID: 8542444     DOI: 10.1007/bf01835151

Source DB:  PubMed          Journal:  Histochem Cell Biol        ISSN: 0948-6143            Impact factor:   4.304


  12 in total

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Authors:  P H Pekala; B M Anderson
Journal:  J Biol Chem       Date:  1978-10-25       Impact factor: 5.157

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Journal:  Science       Date:  1951-09-14       Impact factor: 47.728

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Authors:  M Artman; R J Seeley
Journal:  Science       Date:  1978-12-22       Impact factor: 47.728

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Journal:  J Biol Chem       Date:  1967-03-25       Impact factor: 5.157

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Authors:  W G Ng; G N Donnell; W Bergren
Journal:  Nature       Date:  1968-01-06       Impact factor: 49.962

6.  Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures.

Authors:  S M Hsu; L Raine; H Fanger
Journal:  J Histochem Cytochem       Date:  1981-04       Impact factor: 2.479

7.  Membrane-associated NAD+ glycohydrolase from rabbit erythrocytes is solubilized by phosphatidylinositol-specific phospholipase C.

Authors:  U H Kim; S F Rockwood; H R Kim; R A Daynes
Journal:  Biochim Biophys Acta       Date:  1988-04-14

8.  Purification and characterization of NAD glycohydrolase from rabbit erythrocytes.

Authors:  U H Kim; M K Kim; J S Kim; M K Han; B H Park; H R Kim
Journal:  Arch Biochem Biophys       Date:  1993-08-15       Impact factor: 4.013

9.  Topography, purification and characterization of thyroidal NAD+ glycohydrolase.

Authors:  M J De Wolf; G A Van Dessel; A R Lagrou; H J Hilderson; W S Dierick
Journal:  Biochem J       Date:  1985-03-01       Impact factor: 3.857

10.  Analytical study of microsomes and isolated subcellular membranes from rat liver. IX. Nicotinamide adenine dinucleotide glycohydrolase: a plasma membrane enzyme prominently found in Kupffer cells.

Authors:  A Amar-Costesec; M Prado-Figueroa; H Beaufay; J F Nagelkerke; T J van Berkel
Journal:  J Cell Biol       Date:  1985-01       Impact factor: 10.539

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  1 in total

1.  Regulation of NAD+ glycohydrolase activity by NAD(+)-dependent auto-ADP-ribosylation.

Authors:  M K Han; J Y Lee; Y S Cho; Y M Song; N H An; H R Kim; U H Kim
Journal:  Biochem J       Date:  1996-09-15       Impact factor: 3.857

  1 in total

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