Regulation of the intracellular calcium level in human blood platelets: Cyclic adenosine 3′,5′-monophosphate dependent phosphorylation of a 22 000 dalton component in isolated Ca2+-accumulating vesicles

Käser-Glanzmann, R.; Gerber, Esther; Lüscher, E. F.

doi:10.1016/0005-2736(79)90271-2

Cited by 134 publications

(36 citation statements)

References 16 publications

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“…1, lane e). The same results were obtained with platelet membrane vesicles prepared according to [37] (results not shown here). eluted much earlier from the column than phosphorylated protein 111 (retention time 22 min versus 45 min for protein 111).…”

Section: Phosphorylation Of a 22-kda Membrune Protein In Plateletssupporting

confidence: 85%

“…One of these proteins is a 22-kDa membrane protein which is claimed to play a role in the CAMP-stimulated active transport of Ca2+ out of the platelet cytosol . This protein was found in Ca'+-accumulating vesicles, which led to the assumption of an analogy to phospholamban ('thrombolamban' [36]), although experimental data supporting this assumption have not been presented [37,381. The 22-kDa protein which became phosphorylated by an endogenous protein kinase following application of cAMP to platelet membranes is presumably the same protein [39].…”

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confidence: 99%

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cAMP‐dependent protein phosphorylation of membrane proteins in the parotid gland, platelets and liver

Thiel

Söling

1988

European Journal of Biochemistry

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Stimulation of secretion in exocrine secretory glands leads to the phosphorylation of a 22-kDa membrane protein (protein 111) whose function is still unknown [Jahn et al. (1980) Eur. J. Biochem. 112, 345-352;Jahn & Soling (1980) Proc. Nut1 Acad. Sci. USA 78, 6903 -69061. This report describes the comparison of this protein with phosphorylated membrane proteins of similar molecular mass in platelets and liver. Incubation of platelets with agents which raise the intracellular cAMP concentration results in the phosphorylation of a 22-kDa protein which is also phosphorylated in membrane preparations by endogenous kinases or by exogenous CAMP-dependent protein kinase. It is shown that this protein is distinct from protein I11 although both proteins have the same molecular mass and are substrates of CAMP-dependent protein kinase. In contrast to platelets, protein I11 could be demonstrated in liver microsomes. This indicates that the function of protein 111 is not exclusively linked to the stimulus-secretion coupling in exocrine cells.Stimulation of secretion in exocrine glands by agonists involving cAMP as second messenger leads to the phosphorylation of the ribosomal protein S6 (protein I) and two other particulate proteins with apparent molecular masses of 24 kDa (protein 11) and 22 kDa (protein 111) [I -91. Recently, we published the purification and characterization of protein 111 [lo] showing that this protein belongs to a group of very hydrophobic membrane proteins whose functions are still unknown. Spearman et al. [Ill and Quissel[9] questioned the idea of a direct relationship between an increased phosphorylation state of protein I11 and the secretory process in exocrine secretory glands because the protein is located in the endoplasmic reticulum [9, 11, 121 and shows a slow rate of phosphate turnover. Plewe et al. [12], who found protein 111 in a microsomal subfraction that exhibits the highest ATPdependent calcium transport activity, discussed a possible role of protein 111 for the regulation of calcium sequestration by the endoplasmic reticulum. This hypothesis was adopted in analogy to the function of phospholamban, the putative regulator of the cardiac Ca2+ pump, which was described previously as a 22-kDa phosphoprotein In contrast to the parotid gland, where a rise in intracelluIar cAMP concentration induces exocytosis, cAMP inhibits aggregation and secretion in platelets. This effect of cAMP in platelets is associated with the phosphorylation of various proteins suggesting a coupling between the inhibitory role of cAMP on exocytosis and protein phosphorylation. One of these proteins is a 22-kDa membrane protein which is claimed to play a role in the CAMP-stimulated active transport of Ca2+ out of the platelet cytosol [26-361. This protein was found in Ca'+-accumulating vesicles, which led to the assumption of an analogy to phospholamban ('thrombolamban' [36]), although experimental data supporting this assumption have not been presented [37, 381. The 22-kDa protein which became phosphorylated by an en...

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Section: Phosphorylation Of a 22-kda Membrune Protein In Plateletssupporting

confidence: 85%

mentioning

confidence: 99%

cAMP‐dependent protein phosphorylation of membrane proteins in the parotid gland, platelets and liver

Thiel

Söling

1988

European Journal of Biochemistry

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“…2A, B and 3A, MTP activity is increased in GR having low levels of cAMP and high levels of Ca 2+ . Therefore, one could speculate that MTP activity can be reduced by converting the level of cAMP from low to high, which is known to reduce intracellular Ca 2+ in various cells (10)(11)(12). Therefore, a cAMP analogue, db-cAMP, was used to http://bmbreports.org Effect of thapsigargin on MTP activity.…”

Section: Effect Of Db-camp On Mtp Activitymentioning

confidence: 99%

The opposite correlation between calcium ion and cyclic-AMP regarding the activation of microsomal triglyceride transfer protein in rat liver

Cho

Kim²,

Yu³

et al. 2009

BMB Reports

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“…Our results demonstrate the importance of preventing endogenous proteolysis in studies on the phosphorylation of platelet membrane proteins and suggest that membrane-bound type I enzyme may normally mediate the CAMP-dependent phosphorylation of the membrane polypeptides thought to be important in the inhibition of platelet function by CAMP [2,3,7].…”

Section: Discussionmentioning

confidence: 94%

“…The presence of both soluble [4-71 and membrane-bound [8] CAMP-dependent protein kinases has been reported in platelets. In one study, addition of soluble protein kinase with the ion-exchange characteristics of the type 1 enzyme was required for the CAMP-dependent phosphorylation of the Mr 22 000 membrane polypeptide [7], but preliminary experiments in this laboratory have indicated that a membrane-bound CAMP-dependent protein kinase can phosphorylate this polypeptide [3]. We have, therefore, investigated the distribution of CAMPdependent protein kinase activity and of photoaffinitylabelled CAMP-binding proteins between the particulate and supernatant fractions of platelets sonicated under various conditions.…”

Section: Introductionmentioning

confidence: 99%

Subcellular distribution of cyclic AMP‐dependent protein kinase activity and of cyclic AMP‐binding proteins in human platelets

Salama

Haslam

1981

FEBS Letters

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Regulation of the intracellular calcium level in human blood platelets: Cyclic adenosine 3′,5′-monophosphate dependent phosphorylation of a 22 000 dalton component in isolated Ca2+-accumulating vesicles

Cited by 134 publications

References 16 publications

cAMP‐dependent protein phosphorylation of membrane proteins in the parotid gland, platelets and liver

cAMP‐dependent protein phosphorylation of membrane proteins in the parotid gland, platelets and liver

The opposite correlation between calcium ion and cyclic-AMP regarding the activation of microsomal triglyceride transfer protein in rat liver

Subcellular distribution of cyclic AMP‐dependent protein kinase activity and of cyclic AMP‐binding proteins in human platelets

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