Selective Protein Kinase C Isoforms Are Involved in Endothelin-1-Induced Human Uterine Contraction at the End of Pregnancy

Eude, Isabelle; Paris, Brigitte; Cabrol, D.; Ferré, Françoise; Breuiller-Fouché, Michelle

doi:10.1095/biolreprod63.5.1567

Cited by 32 publications

(24 citation statements)

References 34 publications

(38 reference statements)

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“…In the human myometrium, it has been reported that the PKC isozyme distribution is different between the nonpregnant and the pregnant myometrium (Hurd et al 2000), and that agonist-induced contraction is mediated by PKC isozyme activation (Eude et al 2000). Recently, we have found that PKC activation, especially PKCb activation, stimulated the activation processes of the smooth muscle contractile element in the human myometrium, and that the expression of PKCb in the pregnant myometrium was significantly increased at the late stage of pregnancy (37-40 weeks of gestation) when compared with that in the nonpregnant myometrium (Ozaki et al 2003).…”

Section: Discussionmentioning

confidence: 99%

Role of protein kinase Cβ in rhythmic contractions of human pregnant myometrium

Yasuda

Nakamoto²,

Yasuhara³

et al. 2007

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To assess the role of protein kinase Cb (PKCb) in human myometrial contractions during pregnancy, we evaluated the effect of a PKCb inhibitor (LY333531) on the pregnant and nonpregnant myometrial contractions and compared the level of PKCb in the pregnant myometrium with that in the nonpregnant myometrium. The effects of LY333531 on the myometrial contractions were examined by measuring contractile activity (frequency and amplitude). PKCb in human myometrium was assessed at mRNA level using real-time PCR method. The characteristics of contractile activity were different between the pregnant and the nonpregnant myometrium. The amplitude of rhythmic contractions in the preterm and term myometrium was increased 2-to 2.5-fold when compared with that in the nonpregnant myometrium, but the frequency of rhythmic contractions was decreased by about half. LY333531 (10 K6 M) reduced the increased amplitude in the preterm and term myometrium by about 50%, and the inhibitory effects of LY333531 in the pregnant myometrium were significantly greater than that in the nonpregnant myometrium (about 50 vs 25%). However, the frequency in the pregnant and nonpregnant myometrium was not influenced by LY333531. Real-time PCR revealed a significant, five-to sevenfold increase in the expression of PKCb mRNA in the preterm and term myometrium when compared with the nonpregnant myometrium. These findings suggest that the increased amplitude of human myometrial contractions during pregnancy is related to the increased level of PKCb. A PKCb inhibitor may reduce preterm uterine contractions and prevent preterm delivery.

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Section: Discussionmentioning

confidence: 99%

Role of protein kinase Cβ in rhythmic contractions of human pregnant myometrium

Yasuda

Nakamoto²,

Yasuhara³

et al. 2007

Reproduction

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“…HSCs have properties similar to vascular smooth muscle cells [29]. Some authors contend that PKC-d and PKC-z are necessary for ET-1 induced myometrial contraction [31] whereas others suggest that there is a role for PKC-1 as a regulator of smooth muscle contraction [32]. Dessy et al implicate PKC-a in myogenic contractions of the coronary microcirculation [33].…”

Section: Discussionmentioning

confidence: 99%

Transforming growth factor-β induces contraction of activated hepatic stellate cells

Kharbanda

Rogers²,

Wyatt

et al. 2004

Journal of Hepatology

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“…We showed that exposure to PMA for 24 h downregulated DAG-sensitive PKCs but not atypical PKC-. Although Calphostin C competitively inhibits binding at the DAG and the phorbol ester-binding site, several studies have shown Calphostin C can also inhibit the function of PKC- (55)(56)(57)(58). Previous reports suggest that MC PKC-may be activated in HG (26) and that activation of ERK1/2 in HG (without agonist) is inhibited by Calphostin C (32,59).…”

Section: Discussionmentioning

confidence: 99%

High Glucose–Enhanced Mesangial Cell Extracellular Signal–Regulated Protein Kinase Activation and α1(IV) Collagen Expression in Response to Endothelin-1

et al. 2001

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D iabetic nephropathy is characterized by glomerular mesangial expansion through increased synthesis and decreased degradation of extracellular matrix (ECM) proteins, particularly ␣1(IV) collagen, fibronectin, and laminin ␤ 1 (1-7). Accumulation of ECM proteins progressively obliterates the glomerular capillaries, ultimately resulting in renal failure. Sustained hyperglycemia is the major cause of diabetic nephropathy (8,9). The response of mesangial cells (MCs) to high glucose (HG) includes activation of protein kinase C (PKC) and aberrant synthesis of growth factors, including vasomodulatory agents, such as endothelin-1 (ET-1), which contribute to ECM expression (10 -16).PKC isozymes are a family of serine/threonine protein kinases encoded by at least 12 different genes (17-22). The conventional PKCs (␣, ␤, and ␥) are stimulated by diacylglycerol (DAG) and phosphatidylserine and require Ca 2ϩ . The novel PKCs (␦, ⑀, , and ) are activated by DAG and phosphatidylserine but are insensitive to Ca 2ϩ . The atypical PKCs (, , and ) and PKC-/protein kinase D are sensitive only to phosphatidylserine. MCs express PKC-␣, -␤, -␦, -⑀, and -in culture (23,24) and PKC-␣, -␤ ⌱⌱ , -␦, and -⑀ in vivo, as identified through immunogold labeling of rat glomerular cells in situ (25). HG alters the subcellular distribution of PKC isozymes in cultured MCs (26,27) and increases PKC activity in glomeruli of streptozotocininduced diabetic rats (25,28,29) through de novo synthesis of DAG (5,30). To date, the exact role of specific PKC isozymes mediating HG-enhanced ECM expression by MCs is unknown. We and others (31,32) have reported that in HG, MC extracellular signal-regulated protein kinase (ERK1/2) signaling responses to autocoid growth factors, e.g., ET-1, are enhanced and PKC-dependent. Recently, the importance of mitogen-activated protein kinases (MAPKs) in diabetic complications has been reviewed (33)(34)(35).Endothelins are involved in the pathogenesis of glomerular disease (36 -39). A direct role for ET-1 in the progression of diabetic nephropathy is suggested by enhanced endothelin mRNA expression in cultured cells (40) and diabetic animals (41,42) and by stimulation of MC mitogenesis, a known response to 37). ET-1 binding to its G-protein-coupled receptors stimulates phospholipase C hydrolysis of phosphatidylinosital bisphosphate to generate two second messengers, inositol trisphosphate and DAG, which stimulate release of Ca 2ϩ and PKC activation, respectively (38). ET-1 activates PKC-␣, -␦, and -⑀ in primary-cultured rat MCs (43). ET-1 signal transduction also involves MAPKs, including ERK1/2, with the subsequent regulation of immediate-early genes (44,45).The purpose of this study was to identify the specific PKC isozymes that mediate the effects of HG on MC ERK1/2 signaling and ␣1(IV) collagen expression in reFrom the

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Selective Protein Kinase C Isoforms Are Involved in Endothelin-1-Induced Human Uterine Contraction at the End of Pregnancy

Cited by 32 publications

References 34 publications

Role of protein kinase Cβ in rhythmic contractions of human pregnant myometrium

Role of protein kinase Cβ in rhythmic contractions of human pregnant myometrium

Transforming growth factor-β induces contraction of activated hepatic stellate cells

High Glucose–Enhanced Mesangial Cell Extracellular Signal–Regulated Protein Kinase Activation and α1(IV) Collagen Expression in Response to Endothelin-1

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