Lipoprotein lipase: cellular origin and functional distribution

Lipoprotein lipase (LPL, E.C. 3.3.1.34) is the enzyme responsible for hydrolysis of triacylglycerols in plasma lipoproteins, making the fatty acids available for use by subjacent tissues. LPL is functional at the surface of endothelial cells, but it is not clear which cells synthesize the enzyme and...

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Authors: Camps, Laura, Reina del Pozo, Manuel, Llobera i Sande, Miquel, Vilaró, Senén, 1956-2005, Olivecrona, Thomas
Format: article
Status:Versión aceptada para publicación
Publication Date:1990
Country:España
Institution:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repository:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/111307
Online Access:https://hdl.handle.net/2445/111307
Access Level:Open access
Keyword:Lipoproteïnes
Lipases
Lipoproteins
Lipase
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spelling Lipoprotein lipase: cellular origin and functional distributionCamps, LauraReina del Pozo, ManuelLlobera i Sande, MiquelVilaró, Senén, 1956-2005Olivecrona, ThomasLipoproteïnesLipasesLipoproteinsLipaseLipoprotein lipase (LPL, E.C. 3.3.1.34) is the enzyme responsible for hydrolysis of triacylglycerols in plasma lipoproteins, making the fatty acids available for use by subjacent tissues. LPL is functional at the surface of endothelial cells, but it is not clear which cells synthesize the enzyme and what its distribution is within tissues and vessels. We have searched for specific cell expression of the LPL gene by in situ hybridization using a RNA probe and for the corresponding protein distribution by immunocytochemistry on cryosections of some LPL-producing tissues of guinea pigs. In white and brown adipose tissues, heart and skeletal muscle, and lactating mammary gland, there was positive hybridization for LPL mRNA over all members of the major cell types, indicating that mature and immature adipocytes, muscle cells, and mammary epithelial cells are main sources of LPL. In large vessels, LPL expression was detected in some smooth muscle cells in the media layer. There was no positive hybridization for LPL mRNA over endothelial cells in any of the tissues studied, but there was immunoreaction for LPL protein at endothelial surfaces of all blood vessels. In the kidney, there was strong immunofluorescence at the vascular endothelium, particularly in the glomeruli, but little or no LPL mRNA was detected in the surrounding cells. These observations suggest that in some tissues LPL is synthesized by parenchymal cells and spreads along the vascular mesh. Transfer to the vascular endothelium is, however, not the only route taken by LPL. In the mammary gland most of the enzyme protein appeared to be secreted, partly in association with milk fat droplets.American Physiological Society2017201719902017info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion9 p.application/pdfhttps://hdl.handle.net/2445/111307Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió postprint del document publicat a: http://ajpcell.physiology.org/content/258/4/C673American Journal of Physiology, 1990, vol. 258, num. 4, p. 673-681(c) American Physiological Society, 1990info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1113072026-05-29T05:05:01Z
dc.title.none.fl_str_mv Lipoprotein lipase: cellular origin and functional distribution
title Lipoprotein lipase: cellular origin and functional distribution
spellingShingle Lipoprotein lipase: cellular origin and functional distribution
Camps, Laura
Lipoproteïnes
Lipases
Lipoproteins
Lipase
title_short Lipoprotein lipase: cellular origin and functional distribution
title_full Lipoprotein lipase: cellular origin and functional distribution
title_fullStr Lipoprotein lipase: cellular origin and functional distribution
title_full_unstemmed Lipoprotein lipase: cellular origin and functional distribution
title_sort Lipoprotein lipase: cellular origin and functional distribution
dc.creator.none.fl_str_mv Camps, Laura
Reina del Pozo, Manuel
Llobera i Sande, Miquel
Vilaró, Senén, 1956-2005
Olivecrona, Thomas
author Camps, Laura
author_facet Camps, Laura
Reina del Pozo, Manuel
Llobera i Sande, Miquel
Vilaró, Senén, 1956-2005
Olivecrona, Thomas
author_role author
author2 Reina del Pozo, Manuel
Llobera i Sande, Miquel
Vilaró, Senén, 1956-2005
Olivecrona, Thomas
author2_role author
author
author
author
dc.subject.none.fl_str_mv Lipoproteïnes
Lipases
Lipoproteins
Lipase
topic Lipoproteïnes
Lipases
Lipoproteins
Lipase
description Lipoprotein lipase (LPL, E.C. 3.3.1.34) is the enzyme responsible for hydrolysis of triacylglycerols in plasma lipoproteins, making the fatty acids available for use by subjacent tissues. LPL is functional at the surface of endothelial cells, but it is not clear which cells synthesize the enzyme and what its distribution is within tissues and vessels. We have searched for specific cell expression of the LPL gene by in situ hybridization using a RNA probe and for the corresponding protein distribution by immunocytochemistry on cryosections of some LPL-producing tissues of guinea pigs. In white and brown adipose tissues, heart and skeletal muscle, and lactating mammary gland, there was positive hybridization for LPL mRNA over all members of the major cell types, indicating that mature and immature adipocytes, muscle cells, and mammary epithelial cells are main sources of LPL. In large vessels, LPL expression was detected in some smooth muscle cells in the media layer. There was no positive hybridization for LPL mRNA over endothelial cells in any of the tissues studied, but there was immunoreaction for LPL protein at endothelial surfaces of all blood vessels. In the kidney, there was strong immunofluorescence at the vascular endothelium, particularly in the glomeruli, but little or no LPL mRNA was detected in the surrounding cells. These observations suggest that in some tissues LPL is synthesized by parenchymal cells and spreads along the vascular mesh. Transfer to the vascular endothelium is, however, not the only route taken by LPL. In the mammary gland most of the enzyme protein appeared to be secreted, partly in association with milk fat droplets.
publishDate 1990
dc.date.none.fl_str_mv 1990
2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/111307
url https://hdl.handle.net/2445/111307
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: http://ajpcell.physiology.org/content/258/4/C673
American Journal of Physiology, 1990, vol. 258, num. 4, p. 673-681
dc.rights.none.fl_str_mv (c) American Physiological Society, 1990
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) American Physiological Society, 1990
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 9 p.
application/pdf
dc.publisher.none.fl_str_mv American Physiological Society
publisher.none.fl_str_mv American Physiological Society
dc.source.none.fl_str_mv Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.812455

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