Intra- and extracellular forms of lipoprotein lipase in adipose tissue
(1976) In Biochimica et Biophysica Acta 431(1). p.147-156- Abstract
- The location of lipoprotein lipase activity in rat adipose tissue was studied using intact epididymal fat pads, isolated adipocytes, and lipoprotein lipase activity secreted from adipocytes as enzyme sources. The enzyme activities of these preparations were characterized by gel filtration. The method used for isolation of adipocytes had been modified to minimize activation of lipoprotein lipase during the procedures. Extracts of intact adipose tissue separated into two major lipoprotein lipase activity peaks, designated "a" and "b", the "a" fraction representing about 30 (fasted rats) to 50% (fed rats) of the total enzyme activity. An intermediate fraction (designated "i") was frequently observed. Extracts of isolated adipocytes from fed... (More)
- The location of lipoprotein lipase activity in rat adipose tissue was studied using intact epididymal fat pads, isolated adipocytes, and lipoprotein lipase activity secreted from adipocytes as enzyme sources. The enzyme activities of these preparations were characterized by gel filtration. The method used for isolation of adipocytes had been modified to minimize activation of lipoprotein lipase during the procedures. Extracts of intact adipose tissue separated into two major lipoprotein lipase activity peaks, designated "a" and "b", the "a" fraction representing about 30 (fasted rats) to 50% (fed rats) of the total enzyme activity. An intermediate fraction (designated "i") was frequently observed. Extracts of isolated adipocytes from fed rats contained about 35% and those from fasted rats about 65% of the lipoprotein lipase activity present in intact tissue. The "b" fraction constituted 80--97% of the adipocyte lipoprotein lipase activity. In contrast, the enzyme activity secreted from the adipocytes contained only the "a" and "i" fractions. These data implicate the existance of one intracellular form of lipoprotein lipase (corresponding to the "b" fraction), different from extracellular forms of the enzyme (corresponding to fractions "a" and "i"). A transformation of the intracellular to the extracellular forms appears to occur in conjunction with secretion of enzyme from the fat cell. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1102625
- author
- Nilsson-Ehle, Peter LU ; Garfinkel, Arlene S and Schotz, Michael C
- organization
- publishing date
- 1976
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochimica et Biophysica Acta
- volume
- 431
- issue
- 1
- pages
- 147 - 156
- publisher
- Elsevier
- external identifiers
-
- pmid:1268239
- scopus:0017273508
- ISSN
- 0006-3002
- DOI
- 10.1016/0005-2760(76)90269-1
- language
- English
- LU publication?
- yes
- id
- 5a0b5a06-4e09-4a23-a38a-02712684b3d8 (old id 1102625)
- date added to LUP
- 2016-04-01 16:57:06
- date last changed
- 2021-01-03 09:47:30
@article{5a0b5a06-4e09-4a23-a38a-02712684b3d8,
abstract = {{The location of lipoprotein lipase activity in rat adipose tissue was studied using intact epididymal fat pads, isolated adipocytes, and lipoprotein lipase activity secreted from adipocytes as enzyme sources. The enzyme activities of these preparations were characterized by gel filtration. The method used for isolation of adipocytes had been modified to minimize activation of lipoprotein lipase during the procedures. Extracts of intact adipose tissue separated into two major lipoprotein lipase activity peaks, designated "a" and "b", the "a" fraction representing about 30 (fasted rats) to 50% (fed rats) of the total enzyme activity. An intermediate fraction (designated "i") was frequently observed. Extracts of isolated adipocytes from fed rats contained about 35% and those from fasted rats about 65% of the lipoprotein lipase activity present in intact tissue. The "b" fraction constituted 80--97% of the adipocyte lipoprotein lipase activity. In contrast, the enzyme activity secreted from the adipocytes contained only the "a" and "i" fractions. These data implicate the existance of one intracellular form of lipoprotein lipase (corresponding to the "b" fraction), different from extracellular forms of the enzyme (corresponding to fractions "a" and "i"). A transformation of the intracellular to the extracellular forms appears to occur in conjunction with secretion of enzyme from the fat cell.}},
author = {{Nilsson-Ehle, Peter and Garfinkel, Arlene S and Schotz, Michael C}},
issn = {{0006-3002}},
language = {{eng}},
number = {{1}},
pages = {{147--156}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta}},
title = {{Intra- and extracellular forms of lipoprotein lipase in adipose tissue}},
url = {{http://dx.doi.org/10.1016/0005-2760(76)90269-1}},
doi = {{10.1016/0005-2760(76)90269-1}},
volume = {{431}},
year = {{1976}},
}