Source:http://linkedlifedata.com/resource/pubmed/id/18068104
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2007-12-10
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pubmed:abstractText |
Tamm-Horsfall glycoprotein (THP) is synthesized in the particular sites of renal tubules acting as a defense molecule in the urinary system. In the present study, we found that THP contained high amount of Siaalpha(2,3)Gal/GalNAc, moderate amount of beta(1,4)GlcNAc oligomers and GlcNAc/branched mannose, and low amount of mannose residues, but no Siaalpha(2,6)Gal/GalNAc, in the side-chains of the molecule. THP exhibited high binding affinity with human TNF-alpha, IgG, C1q and BSA, moderate binding affinity with IL-8, and low binding affinity with IL-6 and IFN-gamma. For exploring the role of carbohydrate side-chains and protein core in the protein-binding and cell-stimulating activities, THP was enzyme-digested with carbohydrate-specific [neuraminidase (Nase), beta-galactosidase (Gase)], protein-specific [V8 protease (V8), proteinase K (PaseK)] and glycoconjugate-specific [carboxypeptidase Y (Case), O-sialoglycoprotein endopeptidase (Oase)] degrading enzymes. We found that THP digested with V8, Oase, and PaseK, significantly reduced its protein-binding, mononuclear cell proliferating, and neutrophil phagocytosis-enhancing activities. These results suggest that the intact protein core structure, but not carbohydrate side-chains, is essential for pleotropic functions of THP molecule.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1567-5769
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
90-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18068104-Animals,
pubmed-meshheading:18068104-Carbohydrate Sequence,
pubmed-meshheading:18068104-Cattle,
pubmed-meshheading:18068104-Cell Proliferation,
pubmed-meshheading:18068104-Glycosylation,
pubmed-meshheading:18068104-Humans,
pubmed-meshheading:18068104-Leukocytes, Mononuclear,
pubmed-meshheading:18068104-Molecular Sequence Data,
pubmed-meshheading:18068104-Mucoproteins,
pubmed-meshheading:18068104-Neutrophils,
pubmed-meshheading:18068104-Phagocytosis,
pubmed-meshheading:18068104-Protein Binding,
pubmed-meshheading:18068104-Uromodulin
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pubmed:year |
2008
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pubmed:articleTitle |
Intact protein core structure is essential for protein-binding, mononuclear cell proliferating, and neutrophil phagocytosis-enhancing activities of normal human urinary Tamm-Horsfall glycoprotein.
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pubmed:affiliation |
Institute of Clinical Medicine and Section of Nephrology, National Yang-Ming University College of Medicine, Taipei, Taiwan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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