Adenosine triphosphate catabolism in bovine spermatozoa

A. Minelli, P. Miscetti, A. Proietti, L. Luzi, I. Mezzasoma

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Adenosine triphosphate metabolism in caudal epididymis bovine spermatozoa was studied. Measurements by HPLC at appropriate time intervals of the spermatozoa content of ATP and its derivatives were carried out under different experimental conditions. In the presence of 2-D-glucose, cellular ATP was transformed almost quantitatively into ADP and AMP at a rate of 2.3 nmol/min per 108 cells. At the same time, ADP and AMP accumulated at a rate of 1.52 and 0.58 nmol/min per 108 cells, respectively. In the first 4 min, about 50% of total ATP was degraded, the AEC of the cells dropped to non-physiological values while the content of other nucleosides did not vary significantly. Inorganic Pi content also remained unchanged. Under non-induced conditions up to 240 min, no variations of the adenylic content and of the EC value was observed. Under induced and non-induced conditions, IMP and adenosine were not detected within the spermatozoa. The lack of IMP might be ascribed either to the absence of AMP deaminase, whose activity has never been found in the spermatozoa or to the intracellular environment which down regulates the activity of the enzyme. In order to explain low levels and absence of variations of adenosine, several enzymic investigations were carried out. Adenosine kinase activity was not determined, therefore the transformation of adenosine into AMP had to be excluded. Nevertheless, enzymic activities potentially able to dephosphorylate the formed AMP are present in the spermatozoa. Our findings are indicative of the existence in the spermatozoa of acid and alkaline phosphatase and of 5′-nucleotidase membrane-derived. The effects of some intracellular conditions on both AMP and PNPP hydrolysing activities were examined. This paper indicates that the intracellular pH and the content of the adenylic nucleotides and Pi of the cell exert a negative control of the rate of hydrolysis of AMP, which might explain the lack of production and variations in the spermatozoa adenosine level.

Original languageEnglish
Pages (from-to)605-611
Number of pages7
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume110
Issue number3
DOIs
Publication statusPublished - 1995

Fingerprint

Adenosine Monophosphate
Spermatozoa
Adenosine Triphosphate
Adenosine
Inosine Monophosphate
Adenosine Diphosphate
AMP Deaminase
Adenosine Kinase
5'-Nucleotidase
Acid Phosphatase
Nucleosides
Epididymis
Metabolism
Alkaline Phosphatase
Hydrolysis
Nucleotides
Down-Regulation
Derivatives
Membranes
Glucose

Keywords

  • 5′-Nucleotidase
  • Adenylic metabolism
  • Bovine spermatozoa
  • Energy charge
  • Enzymes adenylic metabolism
  • Phosphate content
  • PNPPases

ASJC Scopus subject areas

  • Biochemistry
  • Physiology

Cite this

Adenosine triphosphate catabolism in bovine spermatozoa. / Minelli, A.; Miscetti, P.; Proietti, A.; Luzi, L.; Mezzasoma, I.

In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 110, No. 3, 1995, p. 605-611.

Research output: Contribution to journalArticle

Minelli, A. ; Miscetti, P. ; Proietti, A. ; Luzi, L. ; Mezzasoma, I. / Adenosine triphosphate catabolism in bovine spermatozoa. In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. 1995 ; Vol. 110, No. 3. pp. 605-611.
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