Lipoprotein lipase isoelectric point isoforms in humans

M. Badia-Villanueva; P. Carulla; M. Carrascal; J. Abian; M. Llobera; A. Casanovas; M. D. Lopez-Tejero

doi:10.1016/j.bbrc.2014.02.028

Lipoprotein lipase isoelectric point isoforms in humans

M. Badia-Villanueva
, P. Carulla
, M. Carrascal
, J. Abian
, M. Llobera
, A. Casanovas
, M. D. Lopez-Tejero

Institut for Biokemi og Molekylær Biologi

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

Lipoprotein lipase (LPL) hydrolyzes circulating triacylglycerols (TAG) into free fatty acids and glycerol. It is present in almost all tissues and its tissue-specific regulation directs the flow of circulating TAG in the body. We demonstrated in a previous study that, in rat heart and post-heparin plasma (PHP), LPL consists of a pattern of more than 8 forms of the same apparent molecular weight, but different isoelectric point (pI). In the present study we describe, for the first time, the existence of at least nine LPL pI isoforms in human PHP, with apparent pI between 6.8 and 8.6. Separation and characterization of these forms was carried out by 2DE combined with Western blotting and mass spectrometry (MALDI-TOF/MS and LC-MS/MS). Further studies are needed to discover their molecular origin, the pattern of pI isoforms in human tissues, their possible physiological functions and possible modifications of their pattern in different pathologies. (C) 2014 Elsevier Inc. All rights reserved.

Originalsprog	Engelsk
Tidsskrift	Biochemical and Biophysical Research Communications
Vol/bind	445
Udgave nummer	2
Sider (fra-til)	480-485
ISSN	0006-291X
DOI	https://doi.org/10.1016/j.bbrc.2014.02.028
Status	Udgivet - 7. mar. 2014

Bibliografisk note

ISI Document Delivery No.: AD4NV Times Cited: 0 Cited Reference Count: 40 Badia-Villanueva, Miriam Carulla, Pere Carrascal, Montserrat Abian, Joaquin Llobera, Miquel Casanovas, Albert Dolores Lopez-Tejero, M. Casanovas, Albert/L-9930-2014; Abian, Joaquin/M-1965-2014 Casanovas, Albert/0000-0001-5986-4258; Abian, Joaquin/0000-0003-2823-5429 Spanish Ministry of Education and Science [BFU2007-65247/BMC]; University of Barcelona (APIF); Genoma Spain The authors thank J.D. Brunzell (University of Washington, Seattle, WA, USA) for providing 5D2 antibody, Rosa Ma Antonijoan (Centre for Drug Research (CIM), Sant Pau Hospital, Barcelona, Spain) for research support, and the Language Advisory Service of the University of Barcelona for editorial help. This study was funded by Spanish Ministry of Education and Science (BFU2007-65247/BMC). Miriam Badia-Villanueva was the recipient of a fellowship from the University of Barcelona (APIF). The Proteomics Laboratory CSIC/UAB is a member of ProteoRed, is funded by Genoma Spain and follows the quality criteria set up by ProteoRed standards. 0 ACADEMIC PRESS INC ELSEVIER SCIENCE SAN DIEGO BIOCHEM BIOPH RES CO

Dokumenter og links

10.1016/j.bbrc.2014.02.028

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Citationsformater

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title = "Lipoprotein lipase isoelectric point isoforms in humans",

abstract = "Lipoprotein lipase (LPL) hydrolyzes circulating triacylglycerols (TAG) into free fatty acids and glycerol. It is present in almost all tissues and its tissue-specific regulation directs the flow of circulating TAG in the body. We demonstrated in a previous study that, in rat heart and post-heparin plasma (PHP), LPL consists of a pattern of more than 8 forms of the same apparent molecular weight, but different isoelectric point (pI). In the present study we describe, for the first time, the existence of at least nine LPL pI isoforms in human PHP, with apparent pI between 6.8 and 8.6. Separation and characterization of these forms was carried out by 2DE combined with Western blotting and mass spectrometry (MALDI-TOF/MS and LC-MS/MS). Further studies are needed to discover their molecular origin, the pattern of pI isoforms in human tissues, their possible physiological functions and possible modifications of their pattern in different pathologies. (C) 2014 Elsevier Inc. All rights reserved.",

keywords = "2DE Heparin-Sepharose affinity chromatography LPL Mass spectrometry pI isoforms Proteomics HEPATIC TRIGLYCERIDE LIPASE HUMAN-MILK POLYACRYLAMIDE-GELS POSTHEPARIN PLASMA MASS-SPECTROMETRY GENE-THERAPY HEPARIN PROTEINS CELLS DEFICIENCY, Heparin-Sepharose affinity chromatography, pI isoforms, 2DE, Proteomics, LPL, Mass spectrometry, Lipoprotein Lipase/chemistry, Protein Isoforms/chemistry, Humans, Rats, Electrophoresis, Gel, Two-Dimensional, Male, Blotting, Western, Young Adult, Animals, Chromatography, Affinity, Isoelectric Point, Adult, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization",

author = "M. Badia-Villanueva and P. Carulla and M. Carrascal and J. Abian and M. Llobera and A. Casanovas and Lopez-Tejero, \{M. D.\}",

note = "ISI Document Delivery No.: AD4NV Times Cited: 0 Cited Reference Count: 40 Badia-Villanueva, Miriam Carulla, Pere Carrascal, Montserrat Abian, Joaquin Llobera, Miquel Casanovas, Albert Dolores Lopez-Tejero, M. Casanovas, Albert/L-9930-2014; Abian, Joaquin/M-1965-2014 Casanovas, Albert/0000-0001-5986-4258; Abian, Joaquin/0000-0003-2823-5429 Spanish Ministry of Education and Science [BFU2007-65247/BMC]; University of Barcelona (APIF); Genoma Spain The authors thank J.D. Brunzell (University of Washington, Seattle, WA, USA) for providing 5D2 antibody, Rosa Ma Antonijoan (Centre for Drug Research (CIM), Sant Pau Hospital, Barcelona, Spain) for research support, and the Language Advisory Service of the University of Barcelona for editorial help. This study was funded by Spanish Ministry of Education and Science (BFU2007-65247/BMC). Miriam Badia-Villanueva was the recipient of a fellowship from the University of Barcelona (APIF). The Proteomics Laboratory CSIC/UAB is a member of ProteoRed, is funded by Genoma Spain and follows the quality criteria set up by ProteoRed standards. 0 ACADEMIC PRESS INC ELSEVIER SCIENCE SAN DIEGO BIOCHEM BIOPH RES CO",

year = "2014",

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doi = "10.1016/j.bbrc.2014.02.028",

language = "English",

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TY - JOUR

T1 - Lipoprotein lipase isoelectric point isoforms in humans

AU - Badia-Villanueva, M.

AU - Carulla, P.

AU - Carrascal, M.

AU - Abian, J.

AU - Llobera, M.

AU - Casanovas, A.

AU - Lopez-Tejero, M. D.

N1 - ISI Document Delivery No.: AD4NV Times Cited: 0 Cited Reference Count: 40 Badia-Villanueva, Miriam Carulla, Pere Carrascal, Montserrat Abian, Joaquin Llobera, Miquel Casanovas, Albert Dolores Lopez-Tejero, M. Casanovas, Albert/L-9930-2014; Abian, Joaquin/M-1965-2014 Casanovas, Albert/0000-0001-5986-4258; Abian, Joaquin/0000-0003-2823-5429 Spanish Ministry of Education and Science [BFU2007-65247/BMC]; University of Barcelona (APIF); Genoma Spain The authors thank J.D. Brunzell (University of Washington, Seattle, WA, USA) for providing 5D2 antibody, Rosa Ma Antonijoan (Centre for Drug Research (CIM), Sant Pau Hospital, Barcelona, Spain) for research support, and the Language Advisory Service of the University of Barcelona for editorial help. This study was funded by Spanish Ministry of Education and Science (BFU2007-65247/BMC). Miriam Badia-Villanueva was the recipient of a fellowship from the University of Barcelona (APIF). The Proteomics Laboratory CSIC/UAB is a member of ProteoRed, is funded by Genoma Spain and follows the quality criteria set up by ProteoRed standards. 0 ACADEMIC PRESS INC ELSEVIER SCIENCE SAN DIEGO BIOCHEM BIOPH RES CO

PY - 2014/3/7

Y1 - 2014/3/7

N2 - Lipoprotein lipase (LPL) hydrolyzes circulating triacylglycerols (TAG) into free fatty acids and glycerol. It is present in almost all tissues and its tissue-specific regulation directs the flow of circulating TAG in the body. We demonstrated in a previous study that, in rat heart and post-heparin plasma (PHP), LPL consists of a pattern of more than 8 forms of the same apparent molecular weight, but different isoelectric point (pI). In the present study we describe, for the first time, the existence of at least nine LPL pI isoforms in human PHP, with apparent pI between 6.8 and 8.6. Separation and characterization of these forms was carried out by 2DE combined with Western blotting and mass spectrometry (MALDI-TOF/MS and LC-MS/MS). Further studies are needed to discover their molecular origin, the pattern of pI isoforms in human tissues, their possible physiological functions and possible modifications of their pattern in different pathologies. (C) 2014 Elsevier Inc. All rights reserved.

AB - Lipoprotein lipase (LPL) hydrolyzes circulating triacylglycerols (TAG) into free fatty acids and glycerol. It is present in almost all tissues and its tissue-specific regulation directs the flow of circulating TAG in the body. We demonstrated in a previous study that, in rat heart and post-heparin plasma (PHP), LPL consists of a pattern of more than 8 forms of the same apparent molecular weight, but different isoelectric point (pI). In the present study we describe, for the first time, the existence of at least nine LPL pI isoforms in human PHP, with apparent pI between 6.8 and 8.6. Separation and characterization of these forms was carried out by 2DE combined with Western blotting and mass spectrometry (MALDI-TOF/MS and LC-MS/MS). Further studies are needed to discover their molecular origin, the pattern of pI isoforms in human tissues, their possible physiological functions and possible modifications of their pattern in different pathologies. (C) 2014 Elsevier Inc. All rights reserved.

KW - 2DE Heparin-Sepharose affinity chromatography LPL Mass spectrometry pI isoforms Proteomics HEPATIC TRIGLYCERIDE LIPASE HUMAN-MILK POLYACRYLAMIDE-GELS POSTHEPARIN PLASMA MASS-SPECTROMETRY GENE-THERAPY HEPARIN PROTEINS CELLS DEFICIENCY

KW - Heparin-Sepharose affinity chromatography

KW - pI isoforms

KW - 2DE

KW - Proteomics

KW - LPL

KW - Mass spectrometry

KW - Lipoprotein Lipase/chemistry

KW - Protein Isoforms/chemistry

KW - Humans

KW - Rats

KW - Electrophoresis, Gel, Two-Dimensional

KW - Male

KW - Blotting, Western

KW - Young Adult

KW - Animals

KW - Chromatography, Affinity

KW - Isoelectric Point

KW - Adult

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

U2 - 10.1016/j.bbrc.2014.02.028

DO - 10.1016/j.bbrc.2014.02.028

M3 - Journal article

C2 - 24530399

SN - 0006-291X

VL - 445

SP - 480

EP - 485

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -