Phosphoinositide breakdown in isolated myelin is stimulated by GTP analogues and calcium | Zendy

Golly F. | Zendy; Larocca J. N. | Zendy; Ledeen R. W. | Zendy

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Phosphoinositide breakdown in isolated myelin is stimulated by GTP analogues and calcium

Author(s) -

Golly F.,

Larocca J. N.,

Ledeen R. W.

Publication year - 1990

Publication title -

journal of neuroscience research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.72

H-Index - 160

eISSN - 1097-4547

pISSN - 0360-4012

DOI - 10.1002/jnr.490270313

Subject(s) - inositol , inositol phosphate , gtp' , chemistry , carbachol , calcium , incubation , phosphatase , biophysics , in vivo , endocrinology , medicine , biochemistry , biology , receptor , enzyme , organic chemistry , microbiology and biotechnology

Purified myelin from rat brainstem, prelabeled in vivo by intracerebral injection of [ 3 H]myoinositol, showed enhanced breakdown of phosphoinositides on treatment with 5'‐guanylylimidodiphosphate [Gpp‐(NH)p] and Ca 2+ . Concentration variation of the former in the presence of Ca 2+ snowed a dose‐dependent release of inositol 1,4‐bisphosphate (IP 2 ) and inositol 1,4,5‐trisphosphate (IP 3 ), while inositol 1‐phosphate (IP) release was erratic. Concentration‐dependent release of IP 2 and IP 3 was also observed with Ca 2+ as the variable in the presence of Gpp(NH)p. Carbachol, when present, did not enhance the stimulatory effect of Gpp(NH)p alone. Addition of diphosphoglycerate during incubation enhanced IP 3 at the expense of IP 2 , suggesting the presence of IP 3 phosphatase in mylein.

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