Protein-Tyrosine Kinase Signaling in the Biological Functions Associated with Sperm

Ijiri, Takashi W.; Hasan, A. K. M. Mahbub; Sato, Kenichi

doi:10.1155/2012/181560

Cited by 29 publications

(22 citation statements)

References 210 publications

(189 reference statements)

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“…The increase in cAMP stimulates protein kinase A (PKA), which activates a series of pathways and coincides with increased protein tyrosine phosphorylation (Harrison, 2004). Since our first reports in 1995 (Visconti et al, 1995a,b), the increase in tyrosine phosphorylation has been used as an endpoint of capacitation in sperm from many species (Baldi et al, 2002;Ficarro et al, 2003;Ijiri et al, 2012;Jagan Mohanarao and Atreja, 2011;Roy and Atreja, 2008;Signorelli et al, 2012). However, the identity of the protein tyrosine kinase(s) responsible for this signaling event has remained elusive.…”

Section: Introductionmentioning

confidence: 99%

The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm

et al. 2016

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Sperm capacitation is required for fertilization. At the molecular level, this process is associated with fast activation of protein kinase A. Downstream of this event, capacitating conditions lead to an increase in tyrosine phosphorylation. The identity of the tyrosine kinase(s) mediating this process has not been conclusively demonstrated. Recent experiments using stallion and human sperm have suggested a role for PYK2 based on the use of small molecule inhibitors directed against this kinase. However, crucially, loss-of-function experiments have not been reported. Here, we used both pharmacological inhibitors and genetically modified mice models to investigate the identity of the tyrosine kinase(s) mediating the increase in tyrosine phosphorylation in mouse sperm. Similar to stallion and human, PF431396 blocks the capacitation-associated increase in tyrosine phosphorylation. Yet, sperm from Pyk2 −/− mice displayed a normal increase in tyrosine phosphorylation, implying that PYK2 is not responsible for this phosphorylation process. Here, we show that PF431396 can also inhibit FER, a tyrosine kinase known to be present in sperm. Sperm from mice targeted with a kinase-inactivating mutation in Fer failed to undergo capacitation-associated increases in tyrosine phosphorylation. Although these mice are fertile, their sperm displayed a reduced ability to fertilize metaphase II-arrested eggs in vitro.

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Section: Introductionmentioning

confidence: 99%

The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm

et al. 2016

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“…Sperm proteins must go through a series of changes and modifications before fertilization. The changes and modifications include glycosylation of proacrosin, alterations in lipids, and increases in cAMP and surface negative charge (Ijiri et al, 2012). Despite the fact that the mechanism underlying capacitation is not entirely clear, there are numerous studies implicating the involvement of cAMP-dependent tyrosine phosphorylation in capacitation (Ficarro et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Expression and tyrosine phosphorylation of sp32 regulate the activation of the boar proacrosin/acrosin system

et al. 2015

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ABSTRACT. The current study investigated the relationship between the level of expression and tyrosine phosphorylation of the sperm protein 32 (sp32) and the activation of the boar proacrosin/acrosin system. The acrosomal membrane proteins of boar sperm for use in different treatment experiments (i.e., fresh sperm, freezing and thawing, capacitation, and acrosome reaction) were separated, stained by Coomassie brilliant blue, and analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and western blot. The results showed that there were differences in the expression level of sp32 among capacitated, frozen-thawed, and post acrosomal reaction sperms. sp32 expression was higher and significantly higher in capacitated and post-acrosomal reaction sperms than in frozen-thawed sperms and fresh semen, respectively. The level of sp32 tyrosine phosphorylation was significantly different between the frozen-thawed sperms and sperms in the other experimental groups. However, bands with molecular masses of 38 to 170 ku in the fresh semen group were more noticeable, indicating that large acrosomal membrane proteins underwent modification and degradation during capacitation and the acrosomal reaction. As a proacrosin binding protein, sp32 shows 2375 sp32 participates in proacrosin activation ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (1): 2374-2383 (2015) upregulated expression and increase in tyrosine phosphorylation levels during the activation of the boar proacrosin/acrosin system.

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“…Here, the male gametes pass a window of time, ranging from hours to days, waiting for the oocyte and interaction with the oviductal epithelial cells. In this context, the spermatozoa are exposed to different gradients of either activating (i.e., bicarbonate, pH, calcium concentration, progesterone, serum proteins) or inhibiting (i.e., endocannabinoids) factors, which influence their metabolic activity and reactivity (Alasmari et al, 2013;Barboni et al, 2011;Ijiri et al, 2012;Wertheimer et al, 2013). Here, the spermatozoa undergo the process of capacitation, acquiring the full ability to fertilize.…”

Section: Introductionmentioning

confidence: 99%

Network Analyses of Sperm–Egg Recognition and Binding: Ready to Rethink Fertility Mechanisms?

Bernabò

Ordinelli

Agostino

et al. 2014

OMICS: A Journal of Integrative Biology

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The rapid growth of published literature makes biomedical text mining increasingly invaluable for unpacking implicit knowledge hidden in unstructured text. We employed biomedical text mining and biological networks analyses to research the process of sperm egg recognition and binding (SERB). We selected from the literature the molecules expressed either on spermatozoa or on oocytes thought to be involved in SERB and, using an automated literature search software (Agilent Literature Search), we realized a network, SERBN, characterized by a hierarchical scale free and a small world topology. We used an integrated approach, either based on selection of hubs or by a cluster analysis, to discern the key molecules of SERB. We found that in most cases some of them are not directly situated on spermatozoa and oocyte, but are dispersed in oviductal fluid or embedded in exosomes present in the perivitelline space. To confirm and validate our results, we performed further analyses using STRING and Reactome FI software. Our findings underscore that the fertility is not a property of gametes in isolation, but rather depends on the functional integrity of the entire reproductive system. These observations collectively underscore the importance of integrative biology in exploring biological systems and in rethinking of fertility mechanisms in the light of this innovative approach.

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Protein-Tyrosine Kinase Signaling in the Biological Functions Associated with Sperm

Cited by 29 publications

References 210 publications

The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm

The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm

Expression and tyrosine phosphorylation of sp32 regulate the activation of the boar proacrosin/acrosin system

Network Analyses of Sperm–Egg Recognition and Binding: Ready to Rethink Fertility Mechanisms?

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