Regulation of protein kinases in exocrine secretory cells during agonist-induced exocytosis

Söling, Hans‐Dieter; Padel, Ulrike; Jahn, Reinhard; Thiel, Gerald; Kricke, P.; Fest, Werner

doi:10.1016/0065-2571(85)90044-5

Cited by 10 publications

(2 citation statements)

References 29 publications

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“…The increased phosphorylation of these two proteinswas not observed during the early phase after a single injection of isoprenaline, which is characterized by maximal stimulation of exocytosis [28]. A selective increase in 32p incorporation into proteins with the apparent Mr values of histones HI and H3 at this time, on the other hand, is in accordance with previous results on mouse parotid glands stimulated in vitro with isoprenaline [32].…”

Section: Discussionsupporting

confidence: 91%

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

Hoffmann

Schwoch²

1989

Biochemical Journal

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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.

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Section: Discussionsupporting

confidence: 91%

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

Hoffmann

Schwoch²

1989

Biochemical Journal

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“…Pilot experiments checked that the state of S6 phosphorylation was not altered during the preparation of the ribosomes. 37 'C as given above and then homogenized with 10 vol. (v/w) of 50 mM sodium phosphate pH 7.0, 2 mM EDTA, 0.2 mM EGTA, 0.1 mM phenylinethylsulfonyl fluoride, 0.01 YO leupeptin, and 0.3 mM sucrose in a glass-teflon Potter homogenizer.…”

Section: Piiosphorylation Of Proteins In Intact Guinea Pig Parotid MImentioning

confidence: 99%

Phosphorylation of the ribosomal protein S6 during agonist‐induced exocytosis in exocrine glands is catalyzed by calcium‐phospholipid‐dependent protein kinase (protein kinase C)

Padel¹,

Söling²

1985

European Journal of Biochemistry

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The ribosomal protein S6 in exocrine cells is phosphorylated during stimulated during stimulation of exocytosis by cAMP‐dependent or calcium‐dependent agonists. Under both conditions the same tryptic S6 phosphopeptides (termed A, B, and C) were found [Padel, Kruppa, Jahn & Söling (1983) FEBS Lett. 159, 112–118]. Studies have now been made of the phosphorylation pattern of protein S6 from purified guinea pig parotid ribosomes following in vitro phosphorylation with calmodulin‐dependent, phospholipid‐dependent, and cAMP‐dependent protein kinases. Only the phospholipid‐dependent enzyme led to the phosphorylation of peptides A, B, and C, while the cAMP‐dependent enzyme phosphorylated only peptides A and C, and the calmodulin‐dependent enzyme did not phosphorylate any of the phosphopeptides found in S6 from unstimulated or stimulated intact cells. Guinea pig parotid microsomes contain substantial phospholipid‐dependent protein kinase activity. Stimulation of intact parotid glands with tetradecanolyphorbol acetate led to a significant phosphorylation of S6 and a similar tryptic S6 phosphopeptide pattern as seen with carbamoylcholine. It is concluded that activation of phospholipid‐dependent protein kinase is responsible for the phosphorylation of protein S6 during stimulation with calcium‐dependent and cAMP‐dependent secretagogues.

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Sialagogue-stimulated protein phosphorylation related to ornithine decarboxylase induction in cultured rat parotid explants

Ueno

Kikuchi

Nishino

et al. 1991

Archives of Oral Biology

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Regulation of protein kinases in exocrine secretory cells during agonist-induced exocytosis

Cited by 10 publications

References 29 publications

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

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

Phosphorylation of the ribosomal protein S6 during agonist‐induced exocytosis in exocrine glands is catalyzed by calcium‐phospholipid‐dependent protein kinase (protein kinase C)

Sialagogue-stimulated protein phosphorylation related to ornithine decarboxylase induction in cultured rat parotid explants

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