Lipoprotein lipase isoelectric point isoforms in humans

Badia-Villanueva, Miriam; Carulla, Pere; Carrascal, Montserrat; Abián, Joaquín; Llobera, Miquel; Casanovas, Albert; López‐Tejero, M. Dolores

doi:10.1016/j.bbrc.2014.02.028

Cited by 4 publications

(5 citation statements)

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“…Future studies should therefore investigate other functional aspects of individual LPL proteoforms such as their interaction with regulatory proteins or potential differences in their specific activity. In addition, the existence of LPL proteoforms in humans (Badia-Villanueva et al, 2014) and the functional regulation of LPL proteoforms in physiological conditions described here, open the door to further research aimed at investigating the regulation of LPL proteoforms in pathological conditions in humans, as well as their potential impact on pharmacological treatments that modulate LPL activity. Finally, from a broader perspective, our work argues for the need to characterize proteome diversity to advance our understanding of biochemical, physiological and pathological processes, which is aligned with recent initiatives proposed to systematically map all human proteoforms (Smith et al, 2021).…”

Section: Discussionmentioning

confidence: 88%

“…Indeed, early work from Soteriou and Cryer resolved LPL with different pI values in 2DE gels ( Soteriou and Cryer, 1993 ) but tentatively attributed this to the potential binding of ampholytes to LPL in IEF, on the basis of a previous study that suggested ampholyte binding to bovine LPL when IEF was conducted under native conditions ( Bengtsson and Olivecrona, 1977 ). Subsequent studies, carried out in our group using denaturing conditions and IPG strips for IEF, ruled out the possibility of ampholite binding and, in combination with Western blot and MS, demonstrated the existence of LPL proteoforms in rat heart, bovine milk and human post-heparin plasma ( Casanovas et al, 2009a ; Badia-Villanueva et al, 2014 ). Extending these findings, in the present study we report the existence of LPL proteoforms in different rat tissues and WAT of cynomolgus monkey, which further denotes the ubiquitous nature of LPL proteoforms in mammals and suggests conserved features in LPL proteoforms across species.…”

Section: Discussionmentioning

confidence: 98%

“…Further expanding the complexity of LPL biology, our previous work revealed that LPL comprises a group of proteoforms with different isoelectric points (pI) both in rat heart ( Casanovas et al, 2009a ) and human post-heparin plasma ( Badia-Villanueva et al, 2014 ). Knowledge on the molecular origin of LPL proteoforms has thus far been limited to the partial contribution of glycans to LPL pI heterogeneity ( Casanovas et al, 2009a ).…”

Section: Introductionmentioning

confidence: 99%

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The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms

Carulla,

Badia-Villanueva,

Civit

et al. 2023

Front. Physiol.

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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 downregulation 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 downregulation 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.

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Section: Discussionmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms

Carulla,

Badia-Villanueva,

Civit

et al. 2023

Front. Physiol.

Self Cite

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“…Interestingly, this phenomenon is very common in our results, where another five proteins, namely muscle actin OlMA1 (spots A7, A8, A9, and A10), beta-enolase (spots A11, A12, and A13), creatine kinase M-type (spots A14, A15, A16 and, A17), apolipoprotein A-I (spots A21 and A22) and beta-crystallin B1 (spots A25 and A28) also showed similar pI shifts in the 2-DE images. These spots may come from different pI isoforms [34] or charge-altering PTM-derived products [35].…”

Section: Acute Tissue Injury Mediated By Oxidase Stressmentioning

confidence: 99%

Proteome Analysis of Whole-Body Responses in Medaka Experimentally Exposed to Fish-Killing Dinoflagellate Karenia mikimotoi

Kwok

Lai

Lam

et al. 2021

IJMS

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Karenia mikimotoi is a well-known harmful algal bloom species. Blooms of this dinoflagellate have become a serious threat to marine life, including fish, shellfish, and zooplanktons and are usually associated with massive fish death. Despite the discovery of several toxins such as gymnocins and gymnodimines in K. mikimotoi, the mechanisms underlying the ichthyotoxicity of this species remain unclear, and molecular studies on this topic have never been reported. The present study investigates the fish-killing mechanisms of K. mikimotoi through comparative proteomic analysis. Marine medaka, a model fish organism, was exposed to K. mikimotoi for a three-part time period (LT25, LT50 and LT90). Proteins extracted from the whole fish were separated by using two-dimensional gel electrophoresis, and differentially expressed proteins were identified with reference to an untreated control. The change in fish proteomes over the time-course of exposure were analyzed. A total of 35 differential protein spots covering 19 different proteins were identified, of which most began to show significant change in expression levels at the earliest stage of intoxication. Among the 19 identified proteins, some are closely related to the oxidative stress responses, energy metabolism, and muscle contraction. We propose that oxidative stress-mediated muscle damage might explain the symptoms developed during the ichthyotoxicity test, such as gasping for breath, loss of balance, and body twitching. Our findings lay the foundations for more in-depth studies of the mechanisms of K. mikimotoi’s ichthyotoxicity.

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“…How these mutations affect clinical outcome in CLL is still unclear, but whether these SNPs might have a role—if any—in LPL non-metabolic functions has not been explored yet. Furthermore, at least nine isoelectric point isoforms of LPL have been described in human blood of healthy individuals [ 66 ], thus opening a new dimension of studies to come for LPL in CLL and other pathologies.…”

Section: Lpl In Chronic Lymphocytic Leukemiamentioning

confidence: 99%

Lipoprotein Lipase Expression in Chronic Lymphocytic Leukemia: New Insights into Leukemic Progression

Prieto

Oppezzo

2017

Molecules

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Lipoprotein lipase (LPL) is a central enzyme in lipid metabolism. Due to its catalytic activity, LPL is involved in metabolic pathways exploited by various solid and hematologic malignancies to provide an extra energy source to the tumor cell. We and others described a link between the expression of LPL in the tumor cell and a poor clinical outcome of patients suffering Chronic Lymphocytic Leukemia (CLL). This leukemia is characterized by a slow accumulation of mainly quiescent clonal CD5 positive B cells that infiltrates secondary lymphoid organs, bone marrow and peripheral blood. Despite LPL being found to be a reliable molecular marker for CLL prognosis, its functional role and the molecular mechanisms regulating its expression are still matter of debate. Herein we address some of these questions reviewing the current state of the art of LPL research in CLL and providing some insights into where currently unexplored questions may lead to.

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Lipoprotein lipase isoelectric point isoforms in humans

Cited by 4 publications

References 38 publications

The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms

The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms

Proteome Analysis of Whole-Body Responses in Medaka Experimentally Exposed to Fish-Killing Dinoflagellate Karenia mikimotoi

Lipoprotein Lipase Expression in Chronic Lymphocytic Leukemia: New Insights into Leukemic Progression

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