Phospholipase Cβ4 isozyme is expressed in human, rat, and murine heart left ventricles and in HL-1 cardiomyocytes

Otaegui, David; Querejeta, Ramón; Arrieta, Ander; Lazkano, Ane; Bidaurrazaga, Ángel; Arriandiaga, J R; Aldazábal, P; Garro, M. Asier

doi:10.1007/s11010-009-0296-x

Cited by 13 publications

(12 citation statements)

References 31 publications

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“…Cardiomyocytes express three subtypes of the PLCβ family at the protein level, PLCβ1, PLCβ3 and PLCβ4 [14,15]. Importantly, PLCβ1 exists as two splice variants (PLCβ1a and PLCβ1b) that differ only in the extreme C-terminal sequence, 32 amino acids for the PLCβ1b sequence ( Fig.…”

Section: Introductionmentioning

confidence: 99%

The atypical ‘b’ splice variant of phospholipase Cβ1 promotes cardiac contractile dysfunction

Grubb

Crook

et al. 2015

Journal of Molecular and Cellular Cardiology

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Section: Introductionmentioning

confidence: 99%

The atypical ‘b’ splice variant of phospholipase Cβ1 promotes cardiac contractile dysfunction

Grubb

Crook

et al. 2015

Journal of Molecular and Cellular Cardiology

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“…67 Additionally, PLC β 4 gene expression levels have been reported to be increased in response to hypertrophic stimuli in mouse HL-1 cardiomyocytes thus indicating that PLC β 4 may also have a role to play in hypertrophic response in cardiomyocytes. 31 It was reported earlier that NE increases in ANF gene expression and protein synthesis in adult rat cardiomyocytes, which are attenuated by a PLC inhibitor, U73122. 68 It was also observed that the NE-induced increase in ANF gene expression and protein synthesis were inhibited by prazosin, an α 1 -AR blocker.…”

Section: Phospholipase C Isozymes and Their Regulationmentioning

confidence: 89%

Involvement of phospholipase C in the norepinephrine-induced hypertrophic response in Cardiomyocytes

Tappia¹,

Elimban²,

Dhalla³

2022

Scripta Medica

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Norepinephrine (NE) is known to mediate cardiomyocyte hypertrophy through the G protein coupled a1 -adrenoceptor (a1 -AR) and the activation of the phosphoinositide-specific phospholipase C (PLC). Since the by-products of PLC activity are important downstream signal transducers for cardiac hypertrophy, the role of and the regulatory mechanisms involved in the activation of PLC isozymes in cardiac hypertrophy are highlighted in this review. The discussion is focused to underscore PLC in different experimental models of cardiac hypertrophy, as well as in isolated adult and neonatal cardiomyocytes treated with NE. Particular emphasis is laid concerning the a1 -AR-PLC-mediated hypertrophic signalling pathway. From the information provided, it is evident that the specific activation of PLC isozymes is a primary signalling event in the a1 -AR mediated response to NE as well as initiation and progression of cardiac hypertrophy. Furthermore, the possibility of PLC involvement in the perpetuation of cardiac hypertrophy is also described. It is suggested that specific PLC isozymes may serve as viable targets for the prevention of cardiac hypertrophy in patient population at-risk for the development of heart failure.

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“…There are four isozymes of PLCβ. PLCβ4 has been shown to be expressed in neurologic tissue but also in liver cells and in the heart [ 22 , 23 ], and is activated by the G q class of the Gα subunit but not by Gβγ subunits [ 24 ]. Here, we found that PLCβ4 is expressed in adipocytes and the enzyme is also regulated by the G q class of G proteins, as indicated by the inhibition by YM25490, a specific inhibitor of G q/11 proteins.…”

Section: Discussionmentioning

confidence: 99%

Angiotensin II Reduces Lipoprotein Lipase Expression in Visceral Adipose Tissue via Phospholipase C β4 Depending on Feeding but Increases Lipoprotein Lipase Expression in Subcutaneous Adipose Tissue via c-Src

et al. 2015

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Metabolic syndrome is characterized by visceral adiposity, insulin resistance, high triglyceride (TG)- and low high-density lipoprotein cholesterol-levels, hypertension, and diabetes—all of which often cause cardiovascular and cerebrovascular diseases. It remains unclear, however, why visceral adiposity but not subcutaneous adiposity causes insulin resistance and other pathological situations. Lipoprotein lipase (LPL) catalyzes hydrolysis of TG in plasma lipoproteins. In the present study, we investigated whether the effects of angiotensin II (AngII) on TG metabolism are mediated through an effect on LPL expression. Adipose tissues were divided into visceral adipose tissue (VAT) and subcutaneous adipose tissue (SAT) for comparison. AngII accelerated LPL expression in SAT but, on the contrary, suppressed its expression in VAT. In both SAT and VAT, AngII signaled through the same type 1 receptor. In SAT, AngII increased LPL expression via c-Src and p38 MAPK signaling. In VAT, however, AngII reduced LPL expression via the Gq class of G proteins and the subsequent phospholipase C β4 (PLCβ4), protein kinase C β1, nuclear factor κB, and inducible nitric oxide synthase signaling pathways. PLCβ4 small interfering RNA experiments showed that PLCβ4 expression is important for the AngII-induced LPL reduction in VAT, in which PLCβ4 expression increases in the evening and falls at night. Interestingly, PLCβ4 expression in VAT decreased with fasting, while AngII did not decrease LPL expression in VAT in a fasting state. In conclusion, AngII reduces LPL expression through PLCβ4, the expression of which is regulated by feeding in VAT, whereas AngII increases LPL expression in SAT. The different effects of AngII on LPL expression and, hence, TG metabolism in VAT and SAT may partly explain their different contributions to the development of metabolic syndrome.

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Phospholipase Cβ4 isozyme is expressed in human, rat, and murine heart left ventricles and in HL-1 cardiomyocytes

Cited by 13 publications

References 31 publications

The atypical ‘b’ splice variant of phospholipase Cβ1 promotes cardiac contractile dysfunction

The atypical ‘b’ splice variant of phospholipase Cβ1 promotes cardiac contractile dysfunction

Involvement of phospholipase C in the norepinephrine-induced hypertrophic response in Cardiomyocytes

Angiotensin II Reduces Lipoprotein Lipase Expression in Visceral Adipose Tissue via Phospholipase C β4 Depending on Feeding but Increases Lipoprotein Lipase Expression in Subcutaneous Adipose Tissue via c-Src

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