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rdf:type |
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lifeskim:mentions |
umls-concept:C0008385,
umls-concept:C0023764,
umls-concept:C0086418,
umls-concept:C0162775,
umls-concept:C0205225,
umls-concept:C0237881,
umls-concept:C0678594,
umls-concept:C0750502,
umls-concept:C1032387,
umls-concept:C1517495,
umls-concept:C2305039
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pubmed:issue |
11
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pubmed:dateCreated |
1993-7-7
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pubmed:databankReference |
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pubmed:abstractText |
The human hormone-sensitive lipase (HSL) gene encodes a 786-aa polypeptide (85.5 kDa). It is composed of nine exons spanning approximately 11 kb, with exons 2-5 clustered in a 1.1-kb region. The putative catalytic site (Ser423) and a possible lipid-binding region in the C-terminal part are encoded by exons 6 and 9, respectively. Exon 8 encodes the phosphorylation site (Ser551) that controls cAMP-mediated activity and a second site (Ser553) that is phosphorylated by 5'-AMP-activated protein kinase. Human HSL showed 83% identity with the rat enzyme and contained a 12-aa deletion immediately upstream of the phosphorylation sites with an unknown effect on the activity control. Besides the catalytic site motif (Gly-Xaa-Ser-Xaa-Gly) found in most lipases, HSL shows no homology with other known lipases or proteins, except for a recently reported unexpected homology between the region surrounding its catalytic site and that of the lipase 2 of Moraxella TA144, an antarctic psychrotrophic bacterium. The gene of lipase 2, which catalyses lipolysis below 4 degrees C, was absent in the genomic DNA of five other Moraxella strains living at 37 degrees C. The lipase 2-like sequence in HSL may reflect an evolutionarily conserved cold adaptability that might be of critical survival value when low-temperature-mobilized endogenous lipids are the primary energy source (e.g., in poikilotherms or hibernators). The finding that HSL at 10 degrees C retained 3- to 5-fold more of its 37 degrees C catalytic activity than lipoprotein lipase or carboxyl ester lipase is consistent with this hypothesis.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1329567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1427819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1539724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1570336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1701111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1818588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1862346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1907455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-1974251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-2106079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-2159025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-2342563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-2537200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-2557074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-2602366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-2611229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-3345839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-3420405,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-3733612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-5097177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-563231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-6317686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-6374655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-6476149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-6779661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-6895751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-7106123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-7108955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8506334-7240206
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4897-901
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8506334-Adipose Tissue,
pubmed-meshheading:8506334-Amino Acid Sequence,
pubmed-meshheading:8506334-Animals,
pubmed-meshheading:8506334-Antarctic Regions,
pubmed-meshheading:8506334-Base Sequence,
pubmed-meshheading:8506334-Blotting, Southern,
pubmed-meshheading:8506334-DNA,
pubmed-meshheading:8506334-DNA, Bacterial,
pubmed-meshheading:8506334-Exons,
pubmed-meshheading:8506334-Gene Library,
pubmed-meshheading:8506334-Genes, Bacterial,
pubmed-meshheading:8506334-Humans,
pubmed-meshheading:8506334-Kinetics,
pubmed-meshheading:8506334-Lipase,
pubmed-meshheading:8506334-Molecular Sequence Data,
pubmed-meshheading:8506334-Moraxella,
pubmed-meshheading:8506334-Oligodeoxyribonucleotides,
pubmed-meshheading:8506334-Rats,
pubmed-meshheading:8506334-Restriction Mapping,
pubmed-meshheading:8506334-Sequence Homology, Amino Acid,
pubmed-meshheading:8506334-Sterol Esterase,
pubmed-meshheading:8506334-Substrate Specificity,
pubmed-meshheading:8506334-Thermodynamics
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pubmed:year |
1993
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pubmed:articleTitle |
Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium.
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pubmed:affiliation |
Department of Medical and Physiological Chemistry 4, Lund University, Sweden.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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