PXD043704

PXD043704 is an original dataset announced via ProteomeXchange.

Title	The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms
Description	Lipoprotein lipase (LPL) is responsible for the intravascular catabolism of triglyceride-rich lipoproteins and plays a central role in whole-body energy balance and lipid homeostasis. As such, LPL is subject to tissue-specific regulation in different physiological conditions, but the mechanisms of this regulation remain incompletely characterized. Previous work revealed that LPL comprises a set of proteoforms with different isoelectric points, but their regulation and functional significance have not been studied thus far. Here we studied the distribution of LPL proteoforms in different rat tissues and their regulation under physiological conditions. First, analysis by two-dimensional electrophoresis and Western blot showed different patterns of LPL proteoforms (i.e., different pI or relative abundance of LPL proteoforms) in different rat tissues under basal conditions, which could be related to the tissue-specific regulation of the enzyme. Next, the comparison of LPL proteoforms from heart and brown adipose tissue between adults and 15-day-old rat pups, two conditions with minimal regulation of LPL in these tissues, yielded virtually the same tissue-specific patterns of LPL proteoforms. In contrast, the pronounced down-regulation of LPL activity observed in white adipose tissue during fasting is accompanied by a prominent reconfiguration of the LPL proteoform pattern. Furthermore, refeeding reverts this down-regulation of LPL activity and restores the pattern of LPL proteoforms in this tissue. Importantly, this reversible proteoform-specific regulation during fasting and refeeding indicates that LPL proteoforms are functionally diverse. Further investigation of potential differences in the functional properties of LPL proteoforms showed that all proteoforms exhibit lipolytic activity and have similar heparin-binding affinity, although other functional aspects remain to be investigated. Overall, this study demonstrates the ubiquity, differential distribution and specific regulation of LPL proteoforms in rat tissues and underscores the need to consider the existence of LPL proteoforms for a complete understanding of LPL regulation under physiological conditions.
HostingRepository	PRIDE
AnnounceDate	2024-01-26
AnnouncementXML	Submission_2024-01-26_09:41:43.965.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Montserrat Carrascal
SpeciesList	scientific name: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey); NCBI TaxID: 9541;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2023-07-12 02:33:40	ID requested
⏵ 1	2024-01-26 09:41:45	announced

10.3389/fphys.2023.1271149;

Carulla P, Badia-Villanueva M, Civit S, Carrascal M, Abian J, Ricart-Jan, é D, Llobera M, Casanovas A, L, ó, pez-Tejero MD, The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms. Front Physiol, 14():1271149(2023) [pubmed]

submitter keyword: lipoprotein lipase,lipid metabolism, proteoform, tissue-specific regulation

M.Dolores López-Tejero
contact affiliation	1Department of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona, Barcelona, Spain
contact email	dolopez@ub.edu
lab head
Montserrat Carrascal
contact affiliation	IIBB-CSIC
contact email	montserrat.carrascal.csic@uab.cat
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD043704
     1. Label: PRIDE project
     2. Name: The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms