Evidence for ryanodine receptors in Schistosoma mansoni.

Abstract:

:The present study investigated the presence of ryanodine receptors in the trematode Schistosoma mansoni. [3H]Ryanodine specific binding sites were found in the four subcellular fractions of S. mansoni; however, more binding sites were recovered in the heterogeneous fraction P1 and the microsomal fraction P4, as was thapsigargin-sensitive (Ca2+-Mg2+)ATPase activity, marking the sarco/endoplasmic reticulum calcium ATPase (SERCA) pumps. This binding had an equilibrium dissociation constant (Kd) in the nanomolar range, an apparent maximal number of receptors (Bmax) of about 80 fmol/mg of protein, and was modulated by ions (Ca2+, Mg2+) and some pharmacological tools such as caffeine. Ryanodine was able to accelerate the rate of 45Ca2+ release from actively loaded vesicles, and also to induce a transient contraction of the whole worm. We conclude that ryanodine-sensitive Ca2+ release channels are present in S. mansoni, with properties very similar to the ones present in higher animals.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Silva CL,Cunha VM,Mendonça-Silva DL,Noël F

doi

10.1016/s0006-2952(98)00219-6

subject

Has Abstract

pub_date

1998-10-15 00:00:00

pages

997-1003

issue

8

eissn

0006-2952

issn

1873-2968

pii

S0006-2952(98)00219-6

journal_volume

56

pub_type

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