Lymphocyte calmodulin and its participation in the stimulation of T lymphocytes by mitogenic lectins.

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Nakabayashi H, Komada H, Yoshida T, Takanari H, Izutsu K

Lymphocyte calmodulin and its participation in the stimulation of T lymphocytes by mitogenic lectins.

Biol Cell. 1992;75(1):55-9.

PubMed ID

1515867 [ View in PubMed

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Abstract

Calmodulin was purified from human tonsillar lymphocytes utilizing calcium-dependent binding of calmodulin to fluphenazine-Sepharose. The molecular weight and phosphodiesterase activation of the lymphocyte calmodulin were very similar to those of purified bovine brain calmodulin. Trifluoperazine (TFP), a calmodulin inhibitor, suppressed lymphocyte stimulation as assessed by 3H-thymidine incorporation into DNA of lectin-stimulated lymphocytes. TFP had no effect on the early 45Ca2+ uptake induced by mitogenic lectins, although this latter was inhibited by verapamil which also suppressed the 3H-thymidine incorporation. The results are in keeping with the interpretation that the inhibition of T cell stimulation by TFP was not due to suppression of Ca2+ uptake, but due to inactivation of Ca(2+)-calmodulin complex which might be formed subsequent to Ca2+ entry into the cell.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Fluphenazine	Calmodulin	Protein	Humans	Unknown	Inhibitor	Details