Glycosylation of lipoprotein lipase in human subcutaneous and omental adipose tissues.
Human adipose tissues from the abdomen (subcutaneous), thigh (subcutaneous) and omentum were incubated for 2 h with [35S]methionine. Then glycosylation of lipoprotein lipase (LPL) was analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of endoglycosidase H (endo H)-digested subunits of the 35S-labeled lipase. Adipose tissues from the abdomen, thigh, and omentum all synthesized LPL subunits with Mr = 57,000 composed of two types of subunits. One type was partially endo H-sensitive yielding a product with Mr = 55,000, indicating that it had one endo H-resistant and one endo H-sensitive oligosaccharide chain. The other type of subunit was totally endo H-sensitive yielding a product with Mr = 52,000. Subcutaneous adipose tissues contained nearly equal amounts of partially and totally endo H-sensitive subunits of LPL, whereas omental adipose tissues contained mainly partially endo H-sensitive subunits of LPL.
Sakayama
K
K
Department of Orthopaedic Surgery, School of Medicine, Ehime University, Japan.
Masuno
H
H
Okumura
H
H
Shibata
T
T
Okuda
H
H
D000273:Adipose Tissue / Q000201:enzymology*; D006026:Glycoside Hydrolases; D006031:Glycosylation; D006801:Humans; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008715:Methionine; D009852:Omentum; D010446:Peptide Fragments / Q000032:analysis; D012867:Skin; D013462:Sulfur Radioisotopes
D010446:Peptide Fragments; D013462:Sulfur Radioisotopes; D008715:Methionine; D008071:Lipoprotein Lipase; D006026:Glycoside Hydrolases