pH regulation of an egg cortex tyrosine kinase

Jiang, Wanping; Veno, Patricia A.; Wood, Boy W.; Peaucellier, Gérard; Kinsey, William H.

doi:10.1016/0012-1606(91)90448-c

Cited by 25 publications

(10 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, it is unclear whether tyrosyl phosphorylation preceded or was a consequence of early ionic events. For example, tyrosyl phosphorylation of a 350 kDa membrane protein was dependent on cytoplasmic alkalinization (Jiang et al 1990(Jiang et al , 1991 that occurs subsequent to the rise in [Ca 2+ ]i. Also antiphosphotyrosine antibody was used to detect phosphorylation of 91 and 138 kDa proteins within 20 s after insemination or after ionophorestimulated intracellular Ca 2+ release (Ciapa & Epel 1991).…”

Section: Introductionmentioning

confidence: 99%

Protein tyrosine kinase‐dependent release of intracellular calcium in the sea urchin egg

1999

Self Cite

View full text Add to dashboard Cite

The aminoguanide, methylglyoxal bis(guanylhydrazone) (MGBG), was shown to stimulate phosphorylation of RR-SRC, a synthetic protein tyrosine kinase (PTK) substrate, and different levels of tyrosyl phosphorylation of endogenous proteins in a sea urchin egg membrane-cortex preparation. Stimulating protein tyrosine kinase activity in the sea urchin egg stimulated intracellular Ca 2+ release, because microinjection of 1-5 mM of MGBG into unfertilized eggs triggered a transient rise in intracellular Ca 2+ activity ([Ca 2+ ]i) after a brief latent period. Pretreating eggs with PTK-specific inhibitors, genistein or tyrphostin B42, significantly inhibited the MGBG-induced rise in [Ca 2+ ]i. Methylglyoxal bis(guanylhydrazone) stimulation of PTK activities in the unfertilized sea urchin egg appeared to trigger Ca 2+ release through phospholipase C (PLC)-dependent inositol 1,4,5-trisphosphate (InsP3) production. The MGBG-induced Ca 2+ response could be suppressed in eggs preloaded with the InsP3 receptor antagonist, heparin, and was reduced in eggs pretreated with U73122, a PLC inhibitor. However, the response was unchanged in eggs treated with nicotinamide, an inhibitor of ADP-ribosyl cyclase, or nifedipine, an inhibitor of nicotinic acid adenine dinucleotide phosphate activity. These results suggest that MGBG may be useful as a chemical agonist of PTK in sea urchin eggs and allow direct testing of the PTK requirement for the transient rise in [Ca 2+ ]i in sea urchin eggs during fertilization. Although genistein was observed to significantly delay the onset, the sperm-induced Ca 2+ response in PTK inhibitor-loaded eggs otherwise appeared normal. Therefore, it was concluded that sea urchin eggs contain a PTK-dependent pathway that can mediate intracellular Ca 2+ release, but PTK activity does not appear to be required for the fertilization response.

show abstract

Section: Introductionmentioning

confidence: 99%

Protein tyrosine kinase‐dependent release of intracellular calcium in the sea urchin egg

1999

Self Cite

View full text Add to dashboard Cite

show abstract

“…Further study, including immuno-electron microscopy, is needed to clarify this issue. It is important to note that Kinsey and his colleagues (Jiang et al ., 1989(Jiang et al ., , 1990(Jiang et al ., , 1991 have reported the transient phosphorylation of a high relative molecular mass protein (-350 kD) at fertilization . We are investigating the possibility that the -350-kD polypeptide detected by anti-70KL IgG is phosphorylated .…”

Section: Discussionmentioning

confidence: 99%

Identification of the sea urchin egg receptor for sperm using an antiserum raised against a fragment of its extracellular domain.

Foltz

Lennarz

1992

The Journal of Cell Biology

View full text Add to dashboard Cite

Abstract. Sea urchin egg fertilization requires the species-specific interaction of molecules on the sperm and egg surfaces. Previously, we isolated an extracellular, 70-kD glycosylated fragment of the S. purpuratus egg receptor for sperm by treating the eggs with lysylendoproteinase C (Foltz, K. R., and W J. . J. Cell Biol. 111:2951-2959 . To characterize the receptor further, we have generated a polyclonal antiserum (anti-70KL) against the purified 70-kD fragment. Anti-70KL was found to react with a single polypeptide of -350 kD on Western blots, presumed to be the intact receptor, in an egg cell surface preparation . This polypeptide appeared to be tightly associated with the plasma membrane/vitelline layer complex, as it was released from these preparations only by detergent treatment . Immunofluorescence microscopy revealed Aey step in fertilization is gamete binding mediated by surface molecules of the sperm and the egg . As reviewed elsewhere, this interaction generally is spe cies specific and involves several recognition steps (see Vacquier and

show abstract

“…Also, antibodies specific for the phosphorylated and non-phosphorylated regulatory tyrosine located in the catalytic domain (Y 416 ) of SFKs can differentiate between active and inactive forms but cannot distinguish among the different family members due to the highly conserved sequence of the phosphorylation site. Early subcellular fractionation studies demonstrated that Fyn and possibly other SFKs were concentrated in the plasma membrane and cortex of sea urchin and zebrafish oocytes [61;68;69]. Confocal immunofluorescence analysis has been used to examine the subcellular localization of SFKs in oocytes from sea urchins, zebrafish, and mice.…”

Section: Subcellular Localizationmentioning

confidence: 99%

Src-Family Tyrosine Kinases in Oogenesis, Oocyte Maturation and Fertilization: An Evolutionary Perspective

Kinsey

2014

Advances in Experimental Medicine and Biology

Self Cite

View full text Add to dashboard Cite

The oocyte is a highly specialized cell poised to respond to fertilization with a unique set of actions needed to recognize and incorporate a single sperm, complete meiosis, reprogram maternal and paternal genomes and assemble them into a unique zygotic genome, and finally initiate the mitotic cell cycle. Oocytes accomplish this diverse series of events through an array of signal transduction pathway components that include a characteristic collection of protein tyrosine kinases. The src-family protein kinases figure importantly in this signaling array and oocytes characteristically express certain SFKs at high levels to provide for the unique actions that the oocyte must perform. The SFKs typically exhibit a distinct pattern of subcellular localization in oocytes and perform critical functions in different subcellular compartments at different steps during oocyte maturation and fertilization. While many aspects of SFK signaling are conserved among oocytes from different species, significant differences exist in the extent to which src-family -mediated pathways are used by oocytes from species that fertilize externally vs those which are fertilized internally. The observation that several oocyte functions which require SFK signaling appear to represent common points of failure during assisted reproductive techniques in humans, highlights the importance of these signaling pathways for human reproductive health.

show abstract

pH regulation of an egg cortex tyrosine kinase

Cited by 25 publications

References 34 publications

Protein tyrosine kinase‐dependent release of intracellular calcium in the sea urchin egg

Protein tyrosine kinase‐dependent release of intracellular calcium in the sea urchin egg

Identification of the sea urchin egg receptor for sperm using an antiserum raised against a fragment of its extracellular domain.

Src-Family Tyrosine Kinases in Oogenesis, Oocyte Maturation and Fertilization: An Evolutionary Perspective

Contact Info

Product

Resources

About