Profile of protein kinase C isozymes and their possible role in mammalian egg activation

Raz, Tamar; Eliyahu, Efrat; Yesodi, Vered; Shalgi, Ruth

doi:10.1016/s0014-5793(98)00806-0

Cited by 48 publications

(33 citation statements)

References 37 publications

(48 reference statements)

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“…Luria et al (2000) demonstrated the activation of PKC-a aPKC-b 1 in fertilized mouse oocytes. Raz et al (1998) observed relocalization of cPKC isotypes PKC-a and PKC-b during activation of rat oocytes. Fan et al (2002b) observed PKC-a, b 1 and g in matured pig oocytes and described the relocalization of these PKCs after oocyte fertilization or oocyte parthenogenetic activation using calcium ionophore A23187.…”

Section: Discussionmentioning

confidence: 74%

“…Various authors have detected calcium-dependent isotypes PKC-a, -b I , -b II , -g; calcium-independent isotypes PKC-d, -e, -m, or atypical isotypes PKC -l and -z in matured rodent oocytes (Gangeswaran and Jones, 1997;Raz et al, 1998;Luria et al, 2000;Pauken and Capco, 2000;Downs et al, 2001;Eliyahu and Shalgi, 2002;Viveiros et al, 2003). However, the data concerning the spectra of PKC isotypes are contradictory.…”

Section: Introductionmentioning

confidence: 99%

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Activation of protein kinase C suppresses fragmentation of pig oocytes aged in vitro

Petr

Krejčová

Rajmon

et al. 2011

Animal

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When cultured for an extended time, pig oocytes that matured in vitro to the stage of metaphase II undergo the complex process designated as ageing. Under our conditions, some pig oocytes aged 3 days remained at the stage of metaphase II (22%), but others underwent spontaneous parthenogenetic activation (45%), and still others perished through fragmentation (28%) or lysis (5%). Activation of protein kinases C (PKCs) using phorbol-12-myristate-13-acetate (PMA) protects oocytes from fragmentation. None of the oocytes were fragmented after 3 days of aging in 50 nM of PMA. A similar effect (8% of fragmented oocytes) was observed after a 3-day treatment of aging oocytes with 100 mM of 1-stearoyl-2arachidonoyl-sn-glycerol (STEAR). PMA and STEAR activate both calcium-dependent and calcium-independent PKCs. This combined effect on PKCs seems to be essential for the protection of oocytes from fragmentation. Neither the specific activator of calcium-dependent PKCs 1-oleoyl-2-acetyl-sn-glycerol (OLE) nor the specific activator of calcium-independent PKCs dipalmitoyl-L-a-phosphatidylinositol-3,4,5-triphosphate heptaammonium salt (DIPALM) suppressed the fragmentation of aging pig oocytes. Twenty-one percentage of oocytes fragmented when aged for 3 days in 10 mM OLE and 26% of aged oocytes fragmented in 100 nM of DIPALM. However, fragmentation was significantly suppressed to 7% when the oocytes were exposed to the combination of both 10 mM OLE and 100 nM DIPALM. Aging pig oocytes cultured for 1 day with PMA maintained a high capability of being parthenogenetically activated (86% of activated oocytes), using calcium ionophore with 6-dimethylaminopurine. Ageing oocytes treated with PMA also had high capability of cleavage (82%) after their artificial parthenogenetic activation. However, their ability to develop to the stage of blastocyst (12%) was suppressed when compared with oocytes activated immediately after their maturation (29%).

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Section: Discussionmentioning

confidence: 74%

Section: Introductionmentioning

confidence: 99%

Activation of protein kinase C suppresses fragmentation of pig oocytes aged in vitro

Petr

Krejčová

Rajmon

et al. 2011

Animal

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“…Several studies reported that CGE, a major process in preventing polyspermy, can be triggered either by [Ca 2C ] i rise or by PKC activation (Gangeswaran & Jones 1997, Johnson & Capco 1997, Raz et al 1998a,1998b, Luria et al 2000, Pauken & Capco 2000. We have previously demonstrated that upon egg activation, MARCKS could either be phosphorylated by activated PKC or be bound by Ca 2C -activated CaM (Eliyahu et al 2005.…”

Section: Discussionmentioning

confidence: 99%

“…Both Ca 2C -dependent and Ca 2C -independent PKC isoforms were identified in rodent eggs (Gangeswaran & Jones 1997, Raz et al 1998b. The change in the intracellular distribution of various PKC isoforms, as manifested by its translocation from the cytoplasm to the plasma membrane of the egg, was followed during fertilization as well as during parthenogenetic activation of eggs (Gallicano et al 1995.…”

Section: Introductionmentioning

confidence: 99%

“…However, it should be noted that activation of PKC by 12-O-tetradecanoylphorbol 13-acetate (TPA) triggered only CGE but had no effect on either RMII or [Ca 2C ] i rise (Raz et al 1998a), and that Ca 2C chelators had almost no effect on PKC activation at fertilization (Tatone et al 2003). RMII can be triggered only by [Ca 2C ] i rise, whereas CGE can be triggered either by [Ca 2C ] i rise or by PKC activation (Gangeswaran & Jones 1997, Johnson & Capco 1997, Raz et al 1998b, Pauken & Capco 2000.…”

Section: Introductionmentioning

confidence: 99%

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Myristoylated alanine-rich C kinase substrate, but not Ca2+/calmodulin-dependent protein kinase II, is the mediator in cortical granules exocytosis

Tsaadon¹,

Kaplan-Kraicer²,

Shalgi³

2008

Reproduction

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Sperm-egg fusion induces cortical granules exocytosis (CGE), a process that ensures the block to polyspermy. CGE can be induced independently by either a rise in intracellular calcium concentration or protein kinase C (PKC) activation. We have previously shown that myristoylated alanine-rich C kinase substrate (MARCKS) cross-links filamentous actin (F-actin) and regulates its reorganization. This activity is reduced either by PKC-induced MARCKS phosphorylation (PKC pathway) or by its direct binding to calmodulin (CaM; CaM pathway), both inducing MARCKS translocation, F-actin reorganization, and CGE. Currently, we examine the involvement of Ca 2C /CaM-dependent protein kinase II (CaMKII) and MARCKS in promoting CGE and show that PKC pathway can compensate for lack of Ca 2C /CaM pathway. Microinjecting eggs with either overexpressed protein or complementary RNA of constitutively active aCaMKII triggered resumption of second meiotic division, but induced CGE of an insignificant magnitude compared with CGE induced by wt aCaMKII. Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Moreover, we were able to demonstrate cPKCs involvement in ionomycin-induced MARCKS translocation and CGE. These results led us to propose that MARCKS, rather than CaMKII, as a key mediator of CGE. Reproduction (2008) 135 613-624

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Molecular cloning of rat sperm galactosyl receptor, a C-type lectin with in vitro egg binding activity

et al. 2000

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Rat sperm galactosyl receptor is a member of the C‐type animal lectin family showing preferential binding to N‐acetylgalactosamine compared to galactose. Binding is mediated by a Ca2+‐dependent carbohydrate‐recognition domain (CRD) identical to that of the minor variant of rat hepatic lectin receptor 2/3 (RHL‐2/3). The molecular organization of the genomic DNA, cDNA, and derived amino acid sequence of rat testis galactosyl receptor have been determined and in vitro fertilization studies were conducted to ascertain its role. We have determined that the rat testis galactosyl receptor gene generates two mRNA species: one species, designated liver‐type, is identical to RHL‐2/3; the other, designated testis‐type, contains one unspliced intron (86 nt) which alters the reading frame and changes the amino acid sequence of the carboxyl terminus. As a result, the CRD (glutamine‐proline‐aspartic acid/QPD) and flanked Ca2+‐binding amino acid sequences were not present in the testis‐type protein. Northern and Southern blots demonstrated presence of transcripts with unspliced intron in rat sperm but not liver. Similarly, antibody, raised against a synthetic 12‐amino acid peptide (p12) encoded by the unspliced intron, recognized in immunoblots a 54 kDa receptor protein in protein extracts from testis but not from liver. Immunofluorescence and immunogold electron microscopy studies demonstrated that both protein species localized on the plasma membrane surface of the head and tail of rat sperm. Furthermore, capacitated rat sperm preincubated with polyclonal antisera to RHL‐2/3 or to the CRD of the liver‐type galactosyl receptor showed a statistically significant decrease in the in vitro fertilization rate. We conclude that rat sperm galactosyl receptor may play a role in egg binding and that an undetermined molecular mechanism operates to generate two proteins with identical intracellular amino terminal domain but only one of them displays a CRD and associated Ca2+‐binding sites at the carboxyl terminal extracellular domain. Mol. Reprod. Dev. 56:401–411, 2000. © 2000 Wiley‐Liss, Inc.

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Profile of protein kinase C isozymes and their possible role in mammalian egg activation

Cited by 48 publications

References 37 publications

Activation of protein kinase C suppresses fragmentation of pig oocytes aged in vitro

Activation of protein kinase C suppresses fragmentation of pig oocytes aged in vitro

Myristoylated alanine-rich C kinase substrate, but not Ca2+/calmodulin-dependent protein kinase II, is the mediator in cortical granules exocytosis

Molecular cloning of rat sperm galactosyl receptor, a C-type lectin with in vitro egg binding activity

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