Presence of Hormonally-Sensitive Adenylate Cyclase Receptors in Capillary-Enriched Fractions from Rat Cerebral Cortex

1978 ◽  
Vol 15 (5) ◽  
pp. 286-298 ◽  
Author(s):  
George M. Baca ◽  
Gene C. Palmer
Keyword(s):  
Cerebral Cortex ◽  
Adenylate Cyclase ◽  
Rat Cerebral Cortex

scholarly journals Effects of desipramine administration on receptor-adenylate cyclase coupling in rat cerebral cortex

1988 ◽  
Vol 46 ◽  
pp. 168
Author(s):  
Fumiaki Tsuchiya ◽  
Toshikazu Saito ◽  
Yuko Hatta ◽  
Hiroshi Ikeda ◽  
Masayuki Watanabe ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Adenylate Cyclase ◽  
Rat Cerebral Cortex

EGTA-sensitive and -insensitive forms of particulate adenylate cyclase in rat cerebral cortex: regulation by divalent cations and GTP

1985 ◽  
Vol 63 (8) ◽  
pp. 1007-1016 ◽  
Author(s):  
P. V. Sulakhe
Keyword(s):  
Enzyme Activity ◽  
Cerebral Cortex ◽  
Adenylate Cyclase ◽  
Gray Matter ◽  
Rank Order ◽  
Divalent Cations ◽  
Rat Cerebral Cortex ◽  
Chloride Salt ◽  
Low Concentrations ◽  
Stimulation Of

Interactions of several divalent cations (Mn2+, Ca2+, Co2+, Sr2+, and Zn2+) with EGTA-inhibitable adenylate cyclase were investigated in washed membranes (particles) isolated from the gray matter of rat cerebral cortex. The EGTA-inhibitable (called sensitive) enzyme activity was assayed in the presence of Triton X-100 since this detergent caused a marked increase (up to 20-fold) in the enzyme activity. The effects of various divalent metals (all added as chloride salt) indicated the presence of two distinct sites called site I and site II. At low concentrations (less than micromolar) Mn2+, Co2+, and Ca2+ increased (up to 10-fold) the enzyme activity to the same extent and appeared to act via binding to site I (high affinity site). The rank order of affinity was Mn2+ ≥ Co2+ > Ca2+. Zn2+ showed the highest affinity and Sr2+ the lowest towards binding to site I; both these metals increased the enzyme activity to lesser extents than Mn2+, Co2+, or Ca2+. GTP was not required for the stimulation of this enzyme by low concentrations of Ca2+. The interaction of Mn2+ with site II (low affinity site) caused further increase in the enzyme activity, whereas Co2+, Ca2+, and Sr2+ were inhibitory at concentrations >10 μM. Isolated fraction contained loosely and tightly associated pools of calmodulin. Myelin basic protein, but not calcineurin, inhibited the EGTA-sensitive adenylate cyclase activity. The EGTA-insensitive enzyme activity was increased by norepinephrine by mechanisms that depended on GTP and was inhibited by Ca2+. The stimulation of the EGTA-insensitive enzyme modulated the Mg2+ requirement such that Mg2+ binding to the low affinity site (site II) apparently occurred with higher affinity. The likely significance of these results is discussed with regard to (i) the presence of two classes of adenylate cyclase in rat cerebral cortex gray matter and (ii) the regulation of their activities by calmodulin-requiring and GTP-requiring mechanisms.

Effect of thuringiensin on adenylate cyclase in rat cerebral cortex

2004 ◽  
Vol 194 (1) ◽  
pp. 34-40 ◽  
Author(s):  
San-Fu Tsai ◽  
Chi Yang ◽  
Shun-Cheng Wang ◽  
Jiunn-Shiow Wang ◽  
Jenn-Sheng Hwang ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Adenylate Cyclase ◽  
Rat Cerebral Cortex

Heterologous sensitization of adenylate cyclase activity by serotonin in the rat cerebral cortex

1993 ◽  
Vol 3 (4) ◽  
pp. 463-475 ◽  
Author(s):  
Alessandra C. Rovescalli ◽  
Nicoletta Brunello ◽  
Jorge Perez ◽  
Silvia Vitali ◽  
Luca Steardo ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Rat Cerebral Cortex ◽  
Heterologous Sensitization
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