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Horm Metab Res 1996; 28(1): 7-10
DOI: 10.1055/s-2007-979120
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© Georg Thieme Verlag Stuttgart · New York

Glycosylation of Lipoprotein Lipase in Human Subcutaneous Lipomas

J.-W. Park1 , J.-Y. Yang1 , S.-R. Rhee2 , C.-G. Cho3 , B.-H. Park1 , H.-W. Rho1 , J.-S. Kim1 , H.-R. Kim1
  • 1Department of Biochemistry, Chonbuk National University Medical School, and Institute for Medical Science, Chonju, Republic of Korea
  • 2Department of Surgery, Chonbuk National University Medical School, and Institute for Medical Science, Chonju, Republic of Korea
  • 3Department of Internal Medicine, Wonkwang University, School of Medicine, Iri, Republic of Korea
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Publication History

1995

1995

Publication Date:
23 April 2007 (online)

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Glycosylation of lipoprotein lipase (LPL) was studied in human subcutaneous lipomas. Heparin-releasable LPL activities were higher in lipomas than those in adjacent normal adipose tissues, and showed good correlation with cellular LPL protein mass. Molecular weight of LPL subunitwas 57 kDa in both tissues. After endoglycosidase H-digestion, two types of LPL subunits were found in normal adipose tissues; partially sensitive (55 kDa) and totally sensitive (52 kDa) form. In lipoma tissues, the fraction of partially sensitive form (55 kDa) was increased comparing with control adipose tissues. These results suggest that partially sensitive subunits constitute the major secretable form of LPL in human subcutaneous lipomas.

Key words

Lipoprotein Lipase - Human - Lipoma - Glycosylation

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