The mode of action of certain 3- and 5-nitropyridines and pyrimidines. III. Biochemical lesions in Trichomonas vaginalis

Michaels, Rhoda M.; Treick, Ronald W.

doi:10.1016/0014-4894(62)90076-0

Cited by 10 publications

(2 citation statements)

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“…Although the glycogen content of T. vaginalis has previously been investigated (Mack and Mu¨ller 1980;Michaels and Treick 1962;Wellerson and Kupferberg 1962), we are not aware of any reports in the literature of phosphorylase measurements being made with this organism. Similarly, we are not aware of any reports where either glycogen phosphorylase activity or glycogen content has been measured in T. tenax.…”

Section: Discussionmentioning

confidence: 99%

“…However, the enzymology of glycogen storage in trichomonads remains ill defined. Glycogen synthesis and/or utilization by T. vaginalis, Trichomonas gallinae, and Trichomonas foetus have (has) been described (Feinberg and Morgan 1953;Manners and Ryley 1955;Michaels and Treick 1962;Wellerson and Kupferberg 1962). In both T. vaginalis and T. foetus, synthesis of glycogen in response to abundant extracel-lular carbohydrate and utilization of this glycogen upon carbohydrate depletion has been reported (Mack and Mu¨ller 1980;Ryley 1955).…”

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confidence: 99%

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Glycogen Accumulation and Degradation by the Trichomonads Trichomonas vaginalis and Trichomonas tenax

Nielsen

Pradhan

Brittingham

et al. 2012

J Eukaryotic Microbiology

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Several species of trichomonad have been shown to accumulate significant quantities of glycogen during growth, suggesting an important role for this compound in cell physiology. We provide the first analysis of the changes in glycogen content and glycogen phosphorylase activity that occur during in vitro growth of two trichomonad species: Trichomonas vaginalis and Trichomonas tenax. Both species accumulated glycogen following inoculation into fresh medium and utilized this compound during logarithmic growth. Glycogen phosphorylase activity also varied during growth in a species-specific manner. The expression of phosphorylase genes in T. vaginalis remained constant during growth and thus transcriptional control did not explain the observed fluctuations in phosphorylase activity. After cloning, expression, and purification, two recombinant glycogen phosphorylases from T. vaginalis and one recombinant glycogen phosphorylase from T. tenax had robust activity and, in contrast to many other eukaryotic glycogen phosphorylases, did not appear to be regulated by reversible protein phosphorylation. Furthermore, allosteric regulation, if present, was not mediated by compounds known to impact the activity of better characterized phosphorylases.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%