Lipoprotein lipase isoelectric point isoforms in humans
| Autor: | Albert Casanovas, Pere Carulla, Miquel Llobera, Joaquín Abián, Montserrat Carrascal, M. Dolores López-Tejero, Miriam Badia-Villanueva |
|---|---|
| Přispěvatelé: | Ministerio de Educación y Ciencia (España), Universidad de Barcelona |
| Rok vydání: | 2014 |
| Předmět: |
Adult
Male Proteomics Gene isoform Blotting Western Biophysics Biochemistry Chromatography Affinity pI isoforms Young Adult chemistry.chemical_compound Pi Glycerol Animals Humans Protein Isoforms Electrophoresis Gel Two-Dimensional Isoelectric Point Molecular Biology Heparin-Sepharose affinity chromatography Lipoprotein lipase Mass spectrometry Chemistry Cell Biology Rat heart Molecular biology 2DE Rats Blot Lipoprotein Lipase Isoelectric point Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization 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 LPL |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname Badia-Villanueva, M, Carulla, P, Carrascal, M, Abian, J, Llobera, M, Casanovas, A & Lopez-Tejero, M D 2014, ' Lipoprotein lipase isoelectric point isoforms in humans ', Biochemical and Biophysical Research Communications, vol. 445, no. 2, pp. 480-485 . https://doi.org/10.1016/j.bbrc.2014.02.028 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2014.02.028 |
| Popis: | 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. © 2014 Elsevier Inc. All rights reserved. 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) |
| Databáze: | OpenAIRE |
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