Advertisement

Biological activity in the repopulating rat spermatocyte after the withdrawal of gossypol treatment. IV. The activity for the modification of core histones

      This paper is only available as a PDF. To read, Please Download here.

      Abstract

      Mature male rats were treated with gossypol for 8 weeks. Afterwards, treatment was halted to allow the arrested spermatogonia to revive. Fifteen days after the withdrawal of the drug treatment, the re-populating pachytene spermatocyte (RPS) had a lower level of core histone H3 and H4 acetylation (40 and 55% reduction, respectively) than that of the control pachytene spermatocyte (CPS). The reduction in core histone acetylation was found in histone H3 and H4 but not in H2A and H2B. Forty-five days after the withdrawal of the drug treatment, the inhibitory effect on core histone acetylation was recovered. Both dot-blot and standard liquid assays were used to detect the nuclear histone acetylase activity in RPS and CPS. Fifteen days after the withdrawal of gossypol treatment, the acetylase type A activity in RPS was reduced by 42% when compared to CPS. It has been concluded that after gossypol treatment, the activity for nucleosomal core histones acetylation was selectively inhibited. This effect is related to an inhibitory effect on the histone acetylase activity.

      Keywords

      To read this article in full you will need to make a payment

      Purchase one-time access:

      Academic & Personal: 24 hour online accessCorporate R&D Professionals: 24 hour online access
      One-time access price info
      • For academic or personal research use, select 'Academic and Personal'
      • For corporate R&D use, select 'Corporate R&D Professionals'

      Subscribe:

      Subscribe to Contraception
      Already a print subscriber? Claim online access
      Already an online subscriber? Sign in
      Institutional Access: Sign in to ScienceDirect

      References

        • National Coordinating Group of Male Antifertility Agents
        Gossypol: A new Antifertility Agent for Males.
        Chin Med J. 1978; 92: 417-428
        • Oian SZ
        • Wang ZG
        Gossypol: a potential antifertility agent for males.
        Ann Rev Pharmacol Toxicol. 1984; 24: 329-360
        • Wang C
        • Yeung RTT
        Gossypol and hypokalaemia.
        Contraception. 1985; 32: 237-252
        • Fei RR
        • Teng CS
        The effects of gossypol on nuclear protein in rat testes. I. Reduction in the content of basic proteins in the spermiogenic cells.
        Contraception. 1988; 37: 279-290
        • Teng CS
        • Fei RR
        The effects of gossypol on nuclear protein in rat testes. II. The synthesis of histones and testis-specific proteins after gossypol treatment.
        Contraception. 1988; 37: 291-299
        • World Health Organization Special Programme of Research
        Development and Research Training in Human Reproduction.
        in: 12th Annual Report. WHO, Geneva1983
        • Zhang SF
        • Hu Yan SL
        • Ye BK
        • Teng CS
        Biological activity in the repopulating rat spermatocyte after the withdrawal of gossypol treatment. I. The activity for DNA synthesis.
        Contraception. 1989; 40: 233-242
        • Ye BK
        • Zhang SF
        • Teng CS
        Biological activity in the repopulating rat spermatocyte after the withdrawal of gossypol treatment. II. The activity for the synthesis of cellular and nuclear basic proteins.
        Contraception. 1989; 40: 243-250
        • Teng CS
        Biological activity in the repopulating rat spermatocyte after the withdrawal of gossypol treatment. III. The activity for the transcription of messenger RNA.
        Contraception. 1992; 45: 167-176
        • Grabske RJ
        • Lake S
        • Gledhill BL
        • Meistrich ML
        Centrifugal elutriation: Separation of spermatogenic cells on the basis of sedimentation velocity.
        J Cell Physiol. 1975; 86: 177-185
        • Mezquita C
        • Teng CS
        The changes of nuclear and chromatin composition and genomic activity during spermatogenesis in the maturing rooster testis.
        Biochem J. 1977; 164: 99-111
        • Laskey RA
        • Mills AD
        Quantitative film detection of 3H and 14C in polyacryl-amide gels by fluorography.
        Eur J Biochem. 1975; 56: 335-341
        • Belikoff E
        • Wong LJ
        • Alberts BM
        Extensive purification of histone acetylase A, the major histone N-acetyl transferase activity detected in mammalian cell nuclei.
        J Biol Chem. 1980; 255: 11448-11453
        • Allis CD
        • Chicoine LG
        • Glover CVC
        • White EM
        • Gorovsky MA
        Enzyme activity dot blots: A rapid and convenient assay for acetyltransferase or protein kinase activity immobilized on nitrocellulose.
        Anal Biochem. 1986; 159: 58-66
        • Allfrey VG
        • Faulkner R
        • Mirsky AE
        Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis.
        in: Proc Natl Acad Sci USA. 51. 1964: 786-794
        • Turner BM
        Histone acetylation and control of gene expression.
        J Cell Sci. 1991; 99: 13-20
        • Csordas A
        On the biological role of histone acetylation.
        Biochem J. 1990; 265: 23-38
        • Ruiz-Carillo A
        • Wangh LJ
        • Littau VC
        • Allfrey VG
        Changes in histone acetyl content and in nuclear non-histone protein composition of avian erythroid cells at different stages of maturation.
        J Biol Chem. 1974; 249: 7358-7368
        • Allfrey VG
        Post-synthetic modifications of histone structure: a mechanism for the control of chromatin structure by the modulation of histone-DNA interactions.
        in: Li Eckhardt Chromatin and Chromosome Structure. Academic Press Inc, New York1977: 167-191
        • Garcea RL
        • Alberts BM
        Comparative studies of histone acetylation in nucleo-somes, nuclei and intact cells. Evidence for special factors which modify acetylase action.
        J Biol Chem. 1980; 255: 11454-11463
        • Sures I
        • Gallwitz D
        Histone-specific acetyltransferases from calf thymus. Isolation, properties and substrate specificity of three different enzymes.
        Biochemistry. 1980; 19: 943-951
        • Weigand RC
        • Brutlag DL
        Histone acetylase from Drosophila melanogaster specific for H4.
        J Biol Chem. 1981; 256: 4578-4583
        • Pfeffer U
        • Vidali G
        Histone acetylation: Recent approaches to a basic mechanism of genome organization.
        Int J Biochem. 1991; 23: 277-285