Effects of tyrosine kinase inhibitor on the motility and ATP concentrations of fowl spermatozoa

Ashizawa, Koji; Higashio, Mari; Tsuzuki, Yasuhiro

doi:10.1002/(sici)1098-2795(199802)49:2<196::aid-mrd10>3.0.co;2-x

Cited by 12 publications

(7 citation statements)

References 44 publications

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“…(1998) had observed that PTK inhibitors 2,5‐MeC and poly glu‐tyr (4:1) had no effect on the motility of demembranated fowl spermatozoa but 2,5‐MeC inhibited motility of intact spermatozoa. Based on this observation Ashizawa et al . (1998) suggested that the tyrosine kinase activity which is associated with sustenance of sperm motility in fowl spermatozoa is not retained in the axoneme and/or accessory cytoskeletal components but may be present in the plasma membrane of spermatozoa.…”

Section: Discussionmentioning

confidence: 88%

“…In fact, if permeability was responsible then piceatannol which inhibited motility of intact spermatozoa should have also inhibited the motility of demembranated spermatozoa. In an earlier study Ashizawa et al . (1998) had observed that PTK inhibitors 2,5‐MeC and poly glu‐tyr (4:1) had no effect on the motility of demembranated fowl spermatozoa but 2,5‐MeC inhibited motility of intact spermatozoa.…”

Section: Discussionmentioning

confidence: 93%

“…Earlier studies have indicated that protein tyrosine kinase are involved in the initiation and activation of motility of trout and Ciona spermatozoa (Morisawa & Hayashi, 1985; Hayashi et al ., 1987; Dey & Brokaw, 1991) and in the maintainance of flagellar movement in fowl spermatozoa (Ashizawa et al ., 1998). Further, recent studies have also suggested that regulation of motility in bovine spermatozoa may involve cross‐talk between cAMP‐dependent protein kinase, Ca 2+ and tyrosine kinase pathways (Vijayaraghavan et al ., 1997).…”

Section: Introductionmentioning

confidence: 99%

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Inhibition of motility of hamster spermatozoa by protein tyrosine kinase inhibitors

et al. 2000

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Genistein, tyrphostin and piceatannol, which are specific inhibitors of protein tyrosine kinase, were screened for their effects on the motility of intact and demembranated hamster spermatozoa. Of the three inhibitors only piceatannol inhibited the motility of intact spermatozoa. None of the inhibitors had any inhibitory effect on the reactivation of motility of demembranated hamster spermatozoa. Taken together these results indicated that a protein tyrosine kinase associated with the membrane of hamster spermatozoa was probably involved in sustenance of hamster sperm motility. Therefore in the present study a membrane-associated protein tyrosine kinase was purified from a detergent-soluble extract of plasma membranes of mature hamster spermatozoa. The purification involved cation exchange chromatography on fast protein liquid chromatography (FPLC) followed by affinity chromatography either on an antiphosphotyrosine antibody agarose or poly glu-tyr agarose column. The pure protein tyrosine kinase had an apparent molecular mass of 45 kDa. The enzyme was not inhibited by genistein or herbimycin but was inhibited by piceatannol. This is the first report on the purification of a sperm plasma membrane-associated protein tyrosine kinase, an enzyme which has also been implicated in hamster sperm motility.

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Section: Discussionmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

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Inhibition of motility of hamster spermatozoa by protein tyrosine kinase inhibitors

et al. 2000

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“…However, it may be that PKC involvement in sperm motility expression is species related, reflecting the ability of Ca 2ϩ to stimulate motility: the ion has no effect in boar sperm (Tajima et al, 1987; see also ''Materials and Methods''). There have also been reports that tyrosine phosphorylation plays a role in the control of motility (Vijayaraghavan et al, 1997;Ashizawa et al, 1998;Si and Okuno, 1999), although Ain et al (1999) found no effect of the PTK inhibitor tyrphostin A-47 on hamster sperm motility. In our experiments, sperm preincubated with the general PTK inhibitor lavendustin A (Onoda et al, 1989;O'Dell et al, 1991) showed no changes either in basal motility or in the initial degree to which bicarbonate was able to stimulate motility.…”

Section: Discussionmentioning

confidence: 99%

Bicarbonate Stimulation of Boar Sperm Motility via a Protein Kinase A—Dependent Pathway: Between‐Cell and Between‐Ejaculate Differences Are Not Due to Deficiencies in Protein Kinase A Activation

HOLT,

HARRISON

2002

Journal of Andrology

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Because poorly motile sperm samples can often be stimulated by treatments that increase intracellular levels of cyclic adenosine monophosphate (cAMP), it has been supposed that such samples are unable to maintain an adequate supply of the cyclic nucleotide with which to activate protein kinase A (PKA). To investigate this hypothesis, we incubated boar sperm samples with bicarbonate (a stimulator of adenylyl cyclase) and compared its effect with that of 5,6‐dichloro‐1‐beta‐D‐ribofuranosyl‐benzimidazole 3‘,5’‐cyclic monophosphothioate (cBIMPS, a highly permeable and stable cAMP analog). Videomicroscopy assessment of motility was followed by computer analysis of the sperm tracks to produce motility descriptor values for many individual cells in each sample, whence “cluster” analysis of these data identified groups of spermatozoa that differed in motility characteristics. Bicarbonate stimulation of motility was characterized by an increase in the linearity (LIN) and progressive velocity of part of the sperm population only. The size of this “fast linear” subpopulation varied considerably between ejaculates. However, treatment with cBIMPS did not induce significantly more “fast linear” sperm than treatment with bicarbonate. In further experiments investigating the role of protein kinases in motility control, bicarbonate stimulation was greatly inhibited by H89 (a specific inhibitor of PKA), whereas GF109203X and lavendustin A (inhibitors of protein kinase C [PKC] and protein tyrosine kinase [PTK], respectively) had essentially no effect. While inclusion of the protein phosphatase inhibitor calyculin stimulated motility, it failed to increase the overall percentage of “fast linear sperm” induced by bicarbonate. We conclude that intersperm and interejaculate differences in boar sperm motility are not due to inadequacy in cAMP supply or to ineffective PKA activity.

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“…Taken together, these events lead to an increase in the tyrosine phosphorylation of specific sperm proteins (Leclerc et al, 1996(Leclerc et al, , 1998Ficarro et al, 2003). An elevation in protein phosphotyrosine content has also been shown to be important in other sperm functions such as the acrosome reaction (Naz and Rajesh, 2004) and the hyperactivation, which is a motility pattern generally associated with sperm capacitation (Carrera et al, 1996;Leclerc et al, 1996;Ashizawa et al, 1998;Mahony and Gwathmey, 1999;Si and Okuno, 1999). Phosphorylation of the fibrous sheath components would cause a decrease in the stiffness of this flagellar sub-fraction, rendering it able to generate greater bends causing sperm hyperactivation (Si and Okuno, 1999).…”

Section: Introductionmentioning

confidence: 99%

Expression of hck‐tr, a truncated form of the src‐related tyrosine kinase hck, in bovine spermatozoa and testis

Bordeleau

Leclerc

2007

Molecular Reproduction Devel

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In bull testicular haploid germ cells, an mRNA encoding for hck was detected in addition to another one encoding for hck-tr, a truncated form of the tyrosine kinase hck. As the transcripts were expressed in spermatids, we tried to determine whether hck-tr is present in mature bovine spermatozoa. Two polyclonal antibodies were produced against peptides specific to the N- and C-terminal portions of the truncated protein. Western blot analyses confirmed the presence of hck-tr in total protein extracts of ejaculated bull spermatozoa, and sub-cellular fractionation experiments suggest its presence in both head and flagellum. The truncated protein appears tightly associated with cytoskeletal elements as it could be extracted only with SDS under reducing conditions. When assessed by indirect immunofluorescence, hck-tr was mostly localized at the acrosomal area of the sperm cell and a similar localization was observed on demembranated spermatozoa. Immunohistochemical studies on testis sections revealed protein expression in spermatocytes as well as in round and elongating spermatids. The results presented in this study clearly show the presence of mRNAs encoding for hck and hck-tr in testicular germ cells; hck-tr being translated during spermatogenesis and expressed on mature ejaculated bull spermatozoa.

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Effects of tyrosine kinase inhibitor on the motility and ATP concentrations of fowl spermatozoa

Cited by 12 publications

References 44 publications

Inhibition of motility of hamster spermatozoa by protein tyrosine kinase inhibitors

Inhibition of motility of hamster spermatozoa by protein tyrosine kinase inhibitors

Bicarbonate Stimulation of Boar Sperm Motility via a Protein Kinase A—Dependent Pathway: Between‐Cell and Between‐Ejaculate Differences Are Not Due to Deficiencies in Protein Kinase A Activation

Expression of hck‐tr, a truncated form of the src‐related tyrosine kinase hck, in bovine spermatozoa and testis

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