scholarly journals Stimulation of cyclic AMP-dependent protein kinase by catecholamines and its relationship to .ALPHA.-amylase release in rat parotid gland.

1982 ◽  
Vol 32 (5) ◽  
pp. 699-716 ◽  
Author(s):  
Keiichi YOSHIMURA ◽  
Eriko NEZU ◽  
Toshie YONEYAMA
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Parotid Gland ◽  
Alpha Amylase ◽  
Dependent Protein Kinase ◽  
Amylase Release ◽  
Rat Parotid Gland ◽  
Dependent Protein ◽  
Rat Parotid ◽  
Stimulation Of

scholarly journals Co-ordinated changes in the cyclic AMP signalling system and the phosphorylation of two nuclear proteins of Mr 130,000 and 110,000 during proliferative stimulation of the rat parotid gland by isoprenaline. Possible identity of the two proteins with pp135 and nucleolin

1989 ◽  
Vol 263 (3) ◽  
pp. 785-793 ◽  
Author(s):  
J Hoffmann ◽  
G Schwoch
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Parotid Gland ◽  
Dna Synthesis ◽  
Beta Agonist ◽  
Nuclear Proteins ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
32P Incorporation ◽  
Stimulation Of

Parotid glands were stimulated to growth by repeated injection of the beta-agonist isoprenaline into rats. Incubation of intact parotid-gland lobules with [32P]Pi and subsequent analysis of nuclear proteins revealed in the stimulated glands an increased 32P incorporation into two acid-soluble non-histone proteins with apparent Mr values of 110,000 and 130,000 (p110 and p130). After a single injection of isoprenaline, leading to a biphasic increase in DNA synthesis (maximum at 24 h), the same two proteins showed a transiently increased 32P incorporation at 17 h after injection. At this time point at the onset of DNA synthesis the total activity of soluble cyclic AMP-dependent protein kinase decreased. No change in p110/p130 phosphorylation was observed at 0.3 h after stimulation, a time of maximal stimulation of secretion. Administration of the beta-antagonist propranolol 8 h after the injection of isoprenaline suppressed the increase in DNA synthesis, the preceding changes in the concentration of cyclic AMP and in the activity of cyclic AMP-dependent protein kinase, as well as the increased phosphorylation of p110 and p130. Cross-reactivity of p110 and p130 with specific antisera against two nucleolar phosphoproteins of similar molecular mass (nucleolin and pp135), as well as their localization in a nucleolar cell fraction, indicated a possible identity of p110 and p130 with these two proteins. Our results suggest that nucleolin and pp135 are nuclear target proteins of cyclic AMP in the cyclic AMP-influenced regulation of the transition of cells from the G1 to the S phase.

Stimulation of chick adrenal steroidogenesis by avian parathyroid hormone

1988 ◽  
Vol 116 (1) ◽  
pp. 91-95 ◽  
Author(s):  
J. Rosenberg ◽  
M. Pines ◽  
S. Hurwitz
Keyword(s):  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Steroid Hormone ◽  
Hormone Secretion ◽  
Peptide Hormone ◽  
Adrenocortical Cells ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Stimulation Of

ABSTRACT Dispersed chick adrenocortical cells were incubated with avian parathyroid hormone (aPTH) or ACTH. Accumulation of cyclic AMP (cAMP), activity of cAMP-dependent protein kinase and the secretion of corticosterone and aldosterone, in response to these hormones, were measured. Accumulation of cAMP and activity of cAMP-dependent protein kinase were stimulated by both aPTH and ACTH as well as by cholera toxin. Cyclic AMP production followed a similar time-course when stimulated by either peptide hormone. Stimulation of steroid hormone secretion was detectable after 20 min of incubation with ACTH, but only after 40 min with aPTH. The maximal steroid hormone secretion by adrenocortical cells was similar when induced by either peptide hormone. The aPTH concentrations needed for half-maximal response of corticosterone and aldosterone secretion were higher than those for ACTH (2·5- and 2-fold respectively), but still within the physiological range. The 11β-hydroxylase inhibitor metyrapone inhibited the secretion of both corticosterone and aldosterone when induced by either aPTH or ACTH. The results suggest that aPTH is almost as potent as ACTH in stimulating the secretion of corticosterone and aldosterone from chick adrenocortical cells and utilizes a cAMP-dependent pathway similar to that of ACTH. J. Endocr. (1988) 116, 91–95

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