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Lipoprotein lipase isoelectric point isoforms in humans

AutorBadía-Villanueva, Míriam; Carulla, Pere; Carrascal, Montserrat ; Abián, Joaquín ; Llobera, Miquel; Casanovas, Albert; López-Tejero, M. Dolores
Palabras clave2DE
Heparin-Sepharose affinity chromatography
LPL
Mass spectrometry
pI isoforms
Proteomics
Fecha de publicación7-mar-2014
EditorAcademic Press
CitaciónBiochemical and Biophysical Research Communications 445(2): 480-485 (2014)
ResumenLipoprotein 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. © 2014 Elsevier Inc. All rights reserved.
Versión del editorhttp://dx.doi.org/10.1016/j.bbrc.2014.02.028
URIhttp://hdl.handle.net/10261/124952
DOI10.1016/j.bbrc.2014.02.028
Identificadoresdoi: 10.1016/j.bbrc.2014.02.028
issn: 1090-2104
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