Quantitative studies of changes in cortical granule number and distribution in the mouse oocyte during meiotic maturation

Ducibella, Tom; Anderson, Everett; Albertini, David F.; Aalberg, Jeff; Rangarajan, Sathyabhama

doi:10.1016/0012-1606(88)90425-3

Cited by 181 publications

(152 citation statements)

References 43 publications

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“…Fluorescent lectins have been used recently to localize specific sugars microscopically in mammalian CG and to demonstrate the appearance of glycosylated material (presumably of CG origin) on the oolemma and within the PVS following the cortical reaction (Gordon et al, 1975;Cherr et al, 1988;Ducibella et al, 1988Ducibella et al, , 1990Ducibella et al, , 1994Lee et al, 1988;Tam et al, 1990;Byers et al, 1992;Hoodbhoy and Talbot, 1993a, b;Yoshida et al, 1993). Lectins used in fluorescence microscopy studies are either conjugated directly to a fluorochrome, such as fluorescein isothiocyanate (FITC), or are biotinylated and are demonstrated by the addition of a streptavidin conjugated fluorochrome.…”

Section: T Hoodbhoy and P Talbotmentioning

confidence: 99%

“…Only five of the lectin studies localized glycosylated material to the CG of unfertilized oocytes (Cherr et al, 1988;Hoodbhoy and Talbot, 1993a, b;Ducibella et al, 1988Ducibella et al, , 1990Ducibella et al, , 1994Byers et al, 1992;Yoshida et al, 1993). CG of unactivated, permeabilized mouse, hamster, and cat oocytes label with Lens culinaris agglutinin (LCA) (Cherr et al, 1988;Ducibella et al, 1988Ducibella et al, , 1990Ducibella et al, , 1994Byers et al, 1992;Hoodbhoy and Talbot, 1993a, b), Concanavalin agglutinin (Con A), Dolichos biflorus agglutinin (DBA) (Hoodbhoy and Talbot, 1993b), and Ricinus communis agglutinin I (RCAIzo) (Hoodbhoy and Talbot, 1993a).…”

Section: T Hoodbhoy and P Talbotmentioning

confidence: 99%

“…CG of unactivated, permeabilized mouse, hamster, and cat oocytes label with Lens culinaris agglutinin (LCA) (Cherr et al, 1988;Ducibella et al, 1988Ducibella et al, , 1990Ducibella et al, , 1994Byers et al, 1992;Hoodbhoy and Talbot, 1993a, b), Concanavalin agglutinin (Con A), Dolichos biflorus agglutinin (DBA) (Hoodbhoy and Talbot, 1993b), and Ricinus communis agglutinin I (RCAIzo) (Hoodbhoy and Talbot, 1993a). These lectins are specific for a-D mannose (LCA and Con A), a-D-GalNAc (DBA), and galactose (RCA,,,) respectively.…”

Section: T Hoodbhoy and P Talbotmentioning

confidence: 99%

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Mammalian cortical granules: Contents, fate, and function

Hoodbhoy

Talbot

1994

Molecular Reproduction Devel

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Recent studies have extended our knowledge regarding the contents of mammalian cortical granules (CG) and their function in postfertilization events. Cytochemical staining has demonstrated the presence of carbohydrates within mammalian CG, and lectin-binding studies have shown that these carbohydrates include a-Dmannose, a-D-GalNAc, and galactose residues in the hamster, a-D-mannose in the mouse and cat, and P-D-Gal(l,3)-D-GalNAc in the pig. Following fertilization and artificial activation, mannosylated material is released from CG and can be found on the oolemma and within the perivitelline space (PVS) of hamster oocytes. Fertilized or artificially activated rabbit, mouse, and human oocytes also release mannosylated, fucosylated and sialylated, and fucosylated material, respectively, which localizes to the oolemma. These glycosylated materials are probably of CG origin, although they have not been directly localized to the CG in rabbit, mice, and humans. The function(s) of the glycosylated material released from mammalian oocytes is not known, although it may participate in blocking polyspermy at the level of the plasma membrane, PVS, and/or zona pellucida (ZP), or it may facilitate preimplantation embryonic development. Proteinases, including tissue plasminogen activator, are also released from mammalian oocytes following fertilization and artificial activation, suggesting that they are of CG origin. These proteinases modify the ZP such that it is no longer receptive to sperm, and some proteinases have been suggested to bring about ZP hardening (an increased resistance to denaturing agents) by an unknown mechanism. Mouse ZP may also be hardened by an ovoperoxidase (cross-links tyrosine residues) cytochemically identified in mouse CG and CG exudate. The phenomena of ZP hardening in mammalian zygotes is not well understood but is likely to function in blocking polyspermic penetration of the ZP and/or in protecting embryos during preirnplantation development. Recently, a 75 kD protein (p75) has been immunocytochemically localized to mouse CG and to the PVS of fertilized oocytes and two-cell embryos. The identity and function of p75 remains to be determined. Heparin binding placental protein may also be a CG component, since it is released from hamster oocytes following fertilization. It has not, however, been directly demonstrated to be a CG component, and its functions in 0 1994 WILEY-LISS, INC.fertilization and/or early embryonic development have yet to be defined. 0 1994 Wlley-Llss, Inc.

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Section: T Hoodbhoy and P Talbotmentioning

confidence: 99%

Section: T Hoodbhoy and P Talbotmentioning

confidence: 99%

Section: T Hoodbhoy and P Talbotmentioning

confidence: 99%

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Mammalian cortical granules: Contents, fate, and function

Hoodbhoy

Talbot

1994

Molecular Reproduction Devel

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“…Fixed eggs were labeled with 5 mg/ml Lens culinaris agglutinin (LCA)-biotin (B-1045; Vector, Burlingame, CA, USA), which binds specifically to CGs exudate (Cherr et al 1988, Ducibella et al 1988, washed, and labeled with 1 mg/ml Texas Red Streptavidin (SA-5006; Vector) for detection of CGE, and with 1 mg/ml Hoechst 33342 (Sigma) for determining cell cycle or fertilization status. Labeled eggs were visualized and photographed with a Zeiss confocal laser scanning microscope (LSM 410 CLSM; Zeiss, Oberkochen, Germany).…”

Section: Western Blot Analysismentioning

confidence: 99%

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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“…Cortical granule exudate was detected by labeling fixed eggs with lens culinaris aectin-biotin (Vector Laboratories, Burlingame, CA, USA; 5 mg/ml in DPBS supplemented with 1% BSA), which interacts with cortical granule content (Ducibella et al 1988). The eggs were then washed and stained with Texas Red -streptavidin (Vector Laboratories; 1 mg/ml in DPBS supplemented with 1% BSA).…”

Section: Assessment Of Crmentioning

confidence: 99%

Expression and possible involvement of calpain isoforms in mammalian egg activation

Ben‐Aharon

Haim²,

Shalgi³

et al. 2005

Reproduction

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At fertilization in mammals, the spermatozoon triggers a unique signal transduction mechanism within the egg, leading to its activation. It is well accepted that the earliest event observed in all activated eggs is an abrupt rise in intracellular calcium concentrations. However, little is known regarding the downstream proteins that are activated by this rise in calcium. Calpains constitute a family of intracellular calcium-dependent cysteine proteases whose members are expressed widely in a variety of cells. We investigated the expression and possible role of the calpain isoforms m and m throughout egg activation. Both calpains were expressed in the rat egg and localized at the egg cortex as well as in the meiotic spindle. m Calpain translocated to the membrane and to the spindle area during parthenogenetic egg activation and during in vivo fertilization, upon sperm binding to the egg. The cytoskeletal protein a-spectrin (fodrin) was proteolysed by calpain during the egg-activation process, as demonstrated by specific calpain-breakdown products. Following parthenogenetic activation by ionomycin or puromycin, the calpain-selective permeable inhibitor, calpeptin, inhibited the resumption of meiosis and cortical reaction in a dosedependent manner. Calpeptin was also effective in inhibiting in vitro fertilization. These results may imply a correlation between calpain activation and mammalian egg activation at fertilization and a possible role for calpain in the cascade of cellular events leading to resumption of meiosis.

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Quantitative studies of changes in cortical granule number and distribution in the mouse oocyte during meiotic maturation

Cited by 181 publications

References 43 publications

Mammalian cortical granules: Contents, fate, and function

Mammalian cortical granules: Contents, fate, and function

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

Expression and possible involvement of calpain isoforms in mammalian egg activation

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