Glycosylation of lipoprotein lipase in human subcutaneous lipomas.
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 subunit was 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.
Park
J W
JW
Department of Biochemistry, Chonbuk National University Medical School, Chonju, Republic of Korea.
Yang
J Y
JY
Rhee
S R
SR
Cho
C G
CG
Park
B H
BH
Rho
H W
HW
Kim
J S
JS
Kim
H R
HR
D000273:Adipose Tissue / Q000201:enzymology; D000328:Adult; D005343:Fibrinolytic Agents / Q000494:pharmacology; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D015151:Immunoblotting; D008067:Lipoma / Q000201:enzymology*; D008071:Lipoprotein Lipase / Q000378:metabolism*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000494:pharmacology; D008875:Middle Aged; D012878:Skin Neoplasms / Q000201:enzymology*
D005343:Fibrinolytic Agents; D006493:Heparin; D008071:Lipoprotein Lipase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase