scholarly journals On the mechanism whereby ACTH and cyclic AMP increase adrenal polyphosphoinositides. Rapid stimulation of the synthesis of phosphatidic acid and derivatives of CDP - diacylglycerol.

1980 ◽  
Vol 255 (15) ◽  
pp. 7232-7237 ◽  
Author(s):  
R.V. Farese ◽  
M.A. Sabir ◽  
R.E. Larson
1986 ◽  
Vol 110 (3) ◽  
pp. 405-416 ◽  
Author(s):  
P. J. Hyatt ◽  
J. B. G. Bell ◽  
K. Bhatt ◽  
F. W. Chu ◽  
J. F. Tait ◽  
...  

ABSTRACT Results on the effects of peptides on the phospholipid metabolism and steroid and cyclic AMP (cAMP) outputs of rat adrenal capsular cells (96% zona glomerulosa, 4% zona fasciculata) were obtained in a series of three batch experiments. Their significance was examined by analysis of variance. Incorporation of [32P] into phosphatidylcholine, phosphatidic acid and phosphatidylinositol was measured. Production of [3H]inositol-1 monophosphate, inositol-1,4 bis-phosphate and inositol-1,4,5 tris-phosphate was estimated after prelabelling with [3H]inositol followed by 1 min incubation with a steroidogenic stimulus. Angiotensin II (0·25 nmol/l to 0·25 μmol/l) highly significantly (P < 0·01) stimulated aldosterone and corticosterone outputs, [32P] incorporation into phosphatidic acid and phosphatidylinositol (but not into phosphatidylcholine) and the production of the three [3H]inositol phosphates. Aldosterone and corticosterone outputs were stimulated by α-MSH (above 0·1 nmol/l). However, incorporation of [32P] was not significantly increased until 10 μmol α-MSH/l but, unlike with angiotensin II, incorporation into phosphatidylcholine was also then stimulated. Also, the production of the inositol phosphates was not increased significantly (P > 0·05) by any dose of α-MSH (10 nmol/l, 1 μmol/l and 0·1 mmol/l) used. Therefore, it can be concluded that α-MSH does not stimulate phospholipase C in rat zona glomerulosa cells. In further experiments, it was also found that there were significant increases in cAMP as well as in steroid outputs above 1 nmol α-MSH/l (highly significant above 10 nmol α-MSH/l). There were plateaux of the outputs of both steroids and cAMP from 0·1 to 1 μmol α-MSH/l. However, there were further increases in steroid and cAMP outputs of the capsular cells at higher doses. Concomitant results on the stimulation of corticosterone output by zona fasciculata–reticularis cells indicate that this additional increase was mostly due to the stimulation of the contaminating zona fasciculata cells. It was also confirmed that α-MSH preferentially stimulates steroidogenesis by the zona glomerulosa. However, under our conditions, α-MSH highly significantly increased the output of cAMP by both zona fasciculata and glomerulosa cells. J. Endocr. (1986) 110, 405–416


1972 ◽  
Vol 50 (8) ◽  
pp. 840-844 ◽  
Author(s):  
John H. McNeill ◽  
Cheng-Yi Lee ◽  
Lawrence D. Muschek

A number of derivatives of imidazole, and the imidazoline derivatives phentolamine and tolazoline, were tested for their effect on cyclic AMP phosphodiesterase obtained from rat brain. Phentolamine and tolazoline inhibited the enzyme with phentolamine being the most potent. Histamine and a derivative of triazole (3-β-aminoethyl-1,2,4-triazole) increased enzyme activity about 10%. It is suggested that enzyme inhibition by phentolamine in addition to an α-adrenergic blockade may explain the reported enhancement of certain catecholamine responses. The stimulation of the enzyme by histamine also may exlpain some of the pharmacological actions of histamine.


1986 ◽  
Vol 56 (03) ◽  
pp. 260-262 ◽  
Author(s):  
Isabella Roos ◽  
Fabrizia Ferracin ◽  
Alfred Pletscher

SummaryArginine-vasopressin (AVP) in the presence of Mg2+ but not in the absence of bivalent cations led to accumulation of [32P]-phosphatidic acid ([32P]-PA) in human blood platelets. Mg2+ also enhanced the specific binding of [3H]-AVP to intact platelets. The concentrations of the cation which enabled AVP to cause half maximal rise of [32P]-PA and those inducing half maximal [3H]-AVP-binding were of the same order. It is concluded that the stimulation of phosphatidyl inositide breakdown by AVP in presence of Mg2+ is at least partially due to a Mg2+-induced enhancement of specific AVP-binding to the platelet membranes.


2006 ◽  
Vol 1071 (1) ◽  
pp. 63-74 ◽  
Author(s):  
Maria C. Olianas ◽  
Paolo Solari ◽  
Luciana Garau ◽  
Anna Liscia ◽  
Roberto Crnjar ◽  
...  

1991 ◽  
Vol 11 (9) ◽  
pp. 4591-4598 ◽  
Author(s):  
M R Mitts ◽  
J Bradshaw-Rouse ◽  
W Heideman

The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B.


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