Mammalian fertilization involves the migration of spermatozoa through the female reproductive system.Early embryonic development is a consequence of several steps and signaling pathways being activated,as well as bioc...Mammalian fertilization involves the migration of spermatozoa through the female reproductive system.Early embryonic development is a consequence of several steps and signaling pathways being activated,as well as biochemical and morphological modifications of spermatozoa that enable them to penetrate the membrane of mature oocytes.There are some crucial steps known to clearly explain the process of fertilization,starting with hyperactivation of spermatozoa,mutual recognition,and binding of gametes mediated by receptors located on the surface membranes of both gametes.The final step is followed by oocyte activation,which is primarily triggered via sperm-derived factors,inducing a sharp increase in intracellular calcium levels,eventually leading to polyspermy block.This review integrates current knowledge of the molecular and physiological events governing fertilization,emphasizing how ion regulation and signaling pathways converge to enable sperm function and oocyte activation.Special attention is given to sperm-derived factors such as phospholipase C zeta(PLCζ)and post-acrosomal sheath WW domain-binding protein(PAWP),which play essential roles in triggering calcium release and supporting early embryonic development.展开更多
Protein kinase C (PKC) is a family of serine/threonine protein kinases, and its multiple isoforms are expressed in various mammalian tissues. The expressions of PKC α and PKC δ at protein and mRNA level in mouse tes...Protein kinase C (PKC) is a family of serine/threonine protein kinases, and its multiple isoforms are expressed in various mammalian tissues. The expressions of PKC α and PKC δ at protein and mRNA level in mouse testis were identified by Western blotting and RT\|PCR. The expression of both PKC isoenzymes in the developing mouse testis was also examined. In testes of mouse at various developmental stages, both the protein and the mRNA of PKC\|α were uniformity; but the PKC\|δ expression occurred in the testes of 3\|week old, perhaps even relatively late in spermatid development. The results suggest that each isoenzyme may have different roles in processing and modulating physiological cellular responses of spermatogenesis.展开更多
文摘Mammalian fertilization involves the migration of spermatozoa through the female reproductive system.Early embryonic development is a consequence of several steps and signaling pathways being activated,as well as biochemical and morphological modifications of spermatozoa that enable them to penetrate the membrane of mature oocytes.There are some crucial steps known to clearly explain the process of fertilization,starting with hyperactivation of spermatozoa,mutual recognition,and binding of gametes mediated by receptors located on the surface membranes of both gametes.The final step is followed by oocyte activation,which is primarily triggered via sperm-derived factors,inducing a sharp increase in intracellular calcium levels,eventually leading to polyspermy block.This review integrates current knowledge of the molecular and physiological events governing fertilization,emphasizing how ion regulation and signaling pathways converge to enable sperm function and oocyte activation.Special attention is given to sperm-derived factors such as phospholipase C zeta(PLCζ)and post-acrosomal sheath WW domain-binding protein(PAWP),which play essential roles in triggering calcium release and supporting early embryonic development.
基金supported by the National Natural Science Foundation of China(No.32371245,31972912,32371245)the Natural Science Foundation of Jiangsu Province,China(No.K20211153).
文摘Protein kinase C (PKC) is a family of serine/threonine protein kinases, and its multiple isoforms are expressed in various mammalian tissues. The expressions of PKC α and PKC δ at protein and mRNA level in mouse testis were identified by Western blotting and RT\|PCR. The expression of both PKC isoenzymes in the developing mouse testis was also examined. In testes of mouse at various developmental stages, both the protein and the mRNA of PKC\|α were uniformity; but the PKC\|δ expression occurred in the testes of 3\|week old, perhaps even relatively late in spermatid development. The results suggest that each isoenzyme may have different roles in processing and modulating physiological cellular responses of spermatogenesis.
