Glycosylation of lipoprotein lipase in human subcutaneous lipomas

J. W. Park; J. Y. Yang; S. R. Rhee; C. G. Cho; B. H. Park; H. W. Rho; J. S. Kim; H. R. Kim

doi:10.1055/s-2007-979120

Glycosylation of lipoprotein lipase in human subcutaneous lipomas

J. W. Park^*
, J. Y. Yang
, S. R. Rhee
, C. G. Cho
, B. H. Park
, H. W. Rho
, J. S. Kim
, H. R. Kim

^*Corresponding author for this work

Department of Medicine

Jeonbuk National University
Wonkwang University

Research output: Contribution to journal › Journal article › peer-review

8 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	7-10
Number of pages	4
Journal	Hormone and Metabolic Research
Volume	28
Issue number	1
DOIs	https://doi.org/10.1055/s-2007-979120
State	Published - 1996

Keywords

Glycosyration
Human
Lipoma
Lipoprotein lipase

Quacquarelli Symonds(QS) Subject Topics

Medicine
Biological Sciences

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10.1055/s-2007-979120

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title = "Glycosylation of lipoprotein lipase in human subcutaneous lipomas",

abstract = "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.",

keywords = "Glycosyration, Human, Lipoma, Lipoprotein lipase",

author = "Park, \{J. W.\} and Yang, \{J. Y.\} and Rhee, \{S. R.\} and Cho, \{C. G.\} and Park, \{B. H.\} and Rho, \{H. W.\} and Kim, \{J. S.\} and Kim, \{H. R.\}",

year = "1996",

doi = "10.1055/s-2007-979120",

language = "English",

volume = "28",

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journal = "Hormone and Metabolic Research",

issn = "0018-5043",

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TY - JOUR

T1 - Glycosylation of lipoprotein lipase in human subcutaneous lipomas

AU - Park, J. W.

AU - Yang, J. Y.

AU - Rhee, S. R.

AU - Cho, C. G.

AU - Park, B. H.

AU - Rho, H. W.

AU - Kim, J. S.

AU - Kim, H. R.

PY - 1996

Y1 - 1996

N2 - 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.

AB - 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.

KW - Glycosyration

KW - Human

KW - Lipoma

KW - Lipoprotein lipase

UR - https://www.scopus.com/pages/publications/0030045559

U2 - 10.1055/s-2007-979120

DO - 10.1055/s-2007-979120

M3 - Journal article

C2 - 8820986

AN - SCOPUS:0030045559

SN - 0018-5043

VL - 28

SP - 7

EP - 10

JO - Hormone and Metabolic Research

JF - Hormone and Metabolic Research

IS - 1

ER -

Glycosylation of lipoprotein lipase in human subcutaneous lipomas

Abstract

Keywords

Quacquarelli Symonds(QS) Subject Topics

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