Autophosphorylation of adenosine 3′,5′-monophosphate-dependent protein kinase from bovine brain

Maeno, Hiroo; Reyes, Procerfina L.; Ueda, Tetsufumi; Rudolph, Stephen A.; Greengard, Paul

doi:10.1016/0003-9861(74)90066-6

Cited by 87 publications

(27 citation statements)

References 17 publications

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“…Using exogenous ( Y~~P ) A T P as substrate it was apparent that the reaction took place at the outer surface of intact Ehrlich cells and resulted in phosphorylation of the protein-bound seryl-and threonyl-residues of the phosphate acceptor protein(s) (3,4,35,36). Endogenous protein kinases effecting phosphorylation of endogenous membrane proteins have since then been found in several tissues including brain membrane fragments and synaptic preparations (22,29,45,47,49), human red cell membranes (6,20,39,40,41), rat liver plasma membranes (3 1, 44) and mitochondria1 membranes (32), bovine anterior pituitary particulate fractions including plasma membranes (26,27,43), membrane preparations from bovine corpus luteum (7, 8) and hamster ovary cells (9), mouse mammary gland (30), renal medulla (15), cortex (17) and brush border (l), toad bladder (13, 14), canine heart (51), adrenal gland (48), myelin basic protein (lo), HeLa cells (24,' 33), muscle cells (5) and fat cells (11,21).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of Endogenous Membrane Proteins by Endogenous Protein Kinase at the Outer Surface of Ehrlich Cells

Ågren¹,

Ronquist²

1976

Upsala Journal of Medical Sciences

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An endogenous protein kinase at the surface of Ehrlich cells has been studied. Using exogenous (Y~~P)ATP as a phosphoryl group donator, a transfer was demonstrated into endogenous acceptor protein(s) as well as to exogenous phosvitin. Seryl-and threonyl-residues isolated from the endogenous and exogenous acceptor protein were found to be labeled. The ratio between the labeled phosphorylserine and phosphorylthreonine was about 3.5 : 1 for both the endogenous acceptor of the intact cells and the exogenous acceptor. In similar experiments with a membrane preparation from Ehrlich cells, this ratio increased to about 7 : 1 provided the exogenous acceptor protein was absent. The results were independent of whether l~l O -~ M dibutyryl cyclic AMP was used or not with intact cells and a membrane fraction mainly consisting of vesicles. Whether the regulatory subunit of the membrane-associated protein kinase was in cis-or trans-disposition to the catalytic subunit no binding and dependence of the cyclic nucleotide was observed. Since the purified membrane fraction was considered free from endogenous cyclic AMP, it was concluded that the membrane-associated protein kinase of Ehrlich cells is not dependent on cyclic AMP. The critical role of arginine for: the cyclic AMP dependence of the serinecontaining residue in the catalytic subunit is discussed.

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Section: Introductionmentioning

confidence: 99%

Phosphorylation of Endogenous Membrane Proteins by Endogenous Protein Kinase at the Outer Surface of Ehrlich Cells

Ågren¹,

Ronquist²

1976

Upsala Journal of Medical Sciences

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“…Protein kinase activities in the microsomal fractions were determined by measuring the incorporation of 32Pi from [y-32P]ATP into histones by the method of Maeno et al (17) and into a endogenous membrane-bound protein, Protein A as described previously (5).…”

Section: Methodsmentioning

confidence: 99%

A possible mechanism for relaxation of rat uterine smooth muscle by nicardipine hydrochloride (YC-93), a new potent vasodilator.

Nishikori¹,

Takenaka²,

Maeno³

1981

Jpn.J.Pharmacol

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“…While the phosphoprotein D phosphatase from toad bladder [72,73] and the synaptic membrane protein II phosphatase from rat brain [178] are activated by cAMP. The former two enzymes are soluable and the latter ones are mem brane bound.…”

Section: Phosphoprotein Phosphatasementioning

confidence: 99%

“…At least four phosphoprotein phosphatases have tentatively been identified which respond to cAMP [49,50,72,73,178,193].…”

Section: Phosphoprotein Phosphatasementioning

confidence: 99%

Second Messenger System in Neoplasia

Criss¹

1974

Oncology

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Hormones have been observed to initiate tumors in animals and are thought to be involved in cellular selection and/or progression of neoplastic lesions in humans. Hormones are the ‘First messengers’ in mammalian systems as they allow cell to cell and organ to organ communication A ‘second messenger’ system is currently being elucidated. This second messenger system involves several cellular membraneous and intracellular components which act to relay extracellular messages to intracellular targets including the genomic machinery within the nucleus. The current manuscript reviews and discusses the following components of the second messenger system in normal versus neoplastic tissues: hormone binding, message transduction, adenylate cyclases, guanylate cyclases, cyclic AMP, cyclic GMP, cyclic nucleotide phosphodiesterases, cyclic nucleotide binding proteins, protein kinases (protein phosphorylation), and phosphoprotein dephosphatases (phosphoprotein de-phosphorylation).

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Autophosphorylation of adenosine 3′,5′-monophosphate-dependent protein kinase from bovine brain

Cited by 87 publications

References 17 publications

Phosphorylation of Endogenous Membrane Proteins by Endogenous Protein Kinase at the Outer Surface of Ehrlich Cells

Phosphorylation of Endogenous Membrane Proteins by Endogenous Protein Kinase at the Outer Surface of Ehrlich Cells

A possible mechanism for relaxation of rat uterine smooth muscle by nicardipine hydrochloride (YC-93), a new potent vasodilator.

Second Messenger System in Neoplasia

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