Alpha-Melanocyte-Stimulating Hormone Inhibits Corticotropin Releasing Factor Release by Blocking Protein Kinase C

1994 ◽  
Vol 1 (3) ◽  
pp. 153-158 ◽  
Author(s):  
Krzysztof Lyson ◽  
Samuel M. McCann
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Corticotropin Releasing Factor ◽  
Melanocyte Stimulating Hormone ◽  
Kinase C ◽  
Factor Release ◽  
Stimulating Hormone

scholarly journals Role of tyrosine kinase and protein kinase C in the steroidogenic actions of angiotensin II, α-melanocyte-stimulating hormone and corticotropin in the rat adrenal cortex

1995 ◽  
Vol 305 (2) ◽  
pp. 433-438 ◽  
Author(s):  
S Kapas ◽  
A Purbrick ◽  
J P Hinson
Keyword(s):  
Protein Kinase C ◽  
Angiotensin Ii ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Zona Glomerulosa ◽  
Aldosterone Secretion ◽  
Melanocyte Stimulating Hormone ◽  
Kinase C ◽  
Stimulating Hormone

The role of protein kinases in the steroidogenic actions of alpha-melanocyte-stimulating hormone (alpha-MSH), angiotensin II (AngII) and corticotropin (ACTH) in the rat adrenal zona glomerulosa was examined. Ro31-8220, a potent selective inhibitor of protein kinase C (PKC), inhibited both AngII- and alpha-MSH-stimulated aldosterone secretion but had no effect on aldosterone secretion in response to ACTH. The effect of Ro31-8220 on PKC activity was measured in subcellular fractions. Basal PKC activity was higher in cytosol than in membrane or nuclear fractions. Incubation of the zona glomerulosa with either alpha-MSH or AngII resulted in significant increases in PKC activity in the nuclear and cytosolic fractions and decreases in the membrane fraction. These effects were all inhibited by Ro31-8220. ACTH caused a significant increase in nuclear PKC activity only, and this was inhibited by Ro31-8220 without any significant effect on the steroidogenic response to ACTH, suggesting that PKC translocation in response to ACTH may be involved in another aspect of adrenal cellular function. Tyrosine phosphorylation has not previously been considered to be an important component of the response of adrenocortical cells to peptide hormones. Both AngII and alpha-MSH were found to activate tyrosine kinase, but ACTH had no effect, observations that have not been previously reported. Tyrphostin 23, a specific antagonist of tyrosine kinases, inhibited aldosterone secretion in response to AngII and alpha-MSH, but not ACTH. These data confirm the importance of PKC in the adrenocortical response to AngII and alpha-MSH, and, furthermore, indicate that tyrosine kinase may play a critical role in the steroidogenic actions of AngII and alpha-MSH in the rat adrenal zona glomerulosa.

α-Melanocyte Stimulating Hormone-Induced Pigmentation Is Blocked by Depletion of Protein Kinase C

1996 ◽  
Vol 227 (1) ◽  
pp. 70-79 ◽  
Author(s):  
Hee-Young Park ◽  
Vladimir Russakovsky ◽  
Yi Ao ◽  
Esther Fernandez ◽  
Barbara A. Gilchrest
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Melanocyte Stimulating Hormone ◽  
Kinase C ◽  
Stimulating Hormone

α-Melanocyte-stimulating hormone stimulates protein kinase C activity in murine B16 melanoma

1992 ◽  
Vol 133 (3) ◽  
pp. 333-340 ◽  
Author(s):  
J. Buffey ◽  
A. J. Thody ◽  
S. S. Bleehen ◽  
S. Mac Neil
Keyword(s):  
Enzyme Activity ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Soluble Fraction ◽  
Fold Increase ◽  
Total Activity ◽  
Melanocyte Stimulating Hormone ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Stimulating Hormone

ABSTRACT The effect of α-melanocyte-stimulating hormone (α-MSH) on protein kinase C activity and distribution was investigated in murine B16 F1 melanoma cells, α-MSH was found to induce an increased association of protein kinase C (PKC) activity with the particulate fraction of the cells, with an associated loss of enzyme activity from the soluble fraction. The peak response to α-MSH occurred between 20 and 60 min of incubation time, and enzyme activities redistributed to those seen in the control cells over the following 12 to 24 h. The average response to α-MSH (1 nmol/l) was an approximate 2·5-fold increase in the percentage of enzyme activity associated with the membrane within 1 h of exposure to α-MSH; the particulate enzyme activity represented 19·2 ± 4·4% of total activity in the absence of α-MSH and 50·7 ± 4·7% (means ± s.e.m., n = 9, P < 0·005) in the presence of α-MSH (1 nmol/l). Cells which had a relatively small percentage of their PKC activity on the membrane initially were significantly (P < 0·01) more responsive to α-MSH stimulation than cells which initially had a relatively large percentage of PKC activity on the membrane. The association of PKC activity with the membrane showed some evidence of being dose-related to α-MSH. This is the first report, to the best of our knowledge, of α-MSH activating PKC. Journal of Endocrinology (1992) 133, 333–340

Thyroid-stimulating hormone activates phospholipase D in FRTL-5 thyroid cells via stimulation of protein kinase C.

Endocrinology ◽  
1995 ◽  
Vol 136 (9) ◽  
pp. 3794-3799 ◽  
Author(s):  
S Gupta ◽  
A Gomez-Muñoz ◽  
W C Matowe ◽  
D N Brindley ◽  
J Ginsberg
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Thyroid Stimulating Hormone ◽  
Thyroid Cells ◽  
Kinase C ◽  
Stimulation Of ◽  
Stimulating Hormone

scholarly journals Amygdala protein kinase C epsilon regulates corticotropin-releasing factor and anxiety-like behavior

2008 ◽  
Vol 7 (3) ◽  
pp. 323-333 ◽  
Author(s):  
H. M. B. Lesscher ◽  
T. McMahon ◽  
A. W. Lasek ◽  
W.-H. Chou ◽  
J. Connolly ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Corticotropin Releasing Factor ◽  
Kinase C ◽  
Protein Kinase C Epsilon
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