Cyclic adenosine 3':5'-monophosphate-dependent protein kinase. Comparison of type II enzymes from bovine brain, skeletal muscle, and cardiac muscle.

Hartl, Fabian; Roskoski, Robert

doi:10.1016/s0021-9258(18)32759-5

Cited by 30 publications

(2 citation statements)

References 26 publications

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“…Moreover, the two types of regulatory subunit can have different subcellular localizations (30). There also are tissue-specific forms: for example, the R, subunits of vertebrate heart, liver, brain, and adipose tissue differ in structure (22,30,41,45) and in antigenicity (18,44).…”

Section: Ofaplysia Californica By Photoaffinity Labeling Withmentioning

confidence: 99%

Structural studies on a family of cAMP-binding proteins in the nervous system of Aplysia.

Eppler¹,

Bayley²,

Greenberg³

et al. 1986

The Journal of Cell Biology

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Abstract. Five major cAMP-binding proteins that differ in size and charge have been identified in neurons ofAplysia californica by photoaffinity labeling with[32p]8-N3cAMP. These proteins, which we believe are regulatory subunits of cAMP-dependent protein kinase, all differ from the major cAMP-binding protein of buccal muscle. We have compared the structures of these proteins by peptide mapping after chemical and proteolytic cleavage. These analyses indicate that the five binding proteins from nervous tissue and the major muscle protein are closely related to each other. For example, the three neuronal proteins that are most alike and the cAMP-binding protein from muscle have a similar, if not identical, Mr 20,000 domain that contains the 8-N3cAMP-binding site; beyond this domain they diverge. All six proteins appear to belong to a family in which homologous regions have been conserved to maintain common functions. We suggest that the regions of the molecules that differ mediate special functions such as ticketing to particular compartments of the cell. Evidence for regional assortment of the cAMP-dependent protein kinases according to structural type was afforded by subceUular fractionation of Aplysia nervous tissue; photoaffinity labeling of cytoplasm, cytoskeleton, and membrane fractions demonstrated a differential distribution of the five neuronal cAMP-binding proteins. Selective phosphorylation of specific substrates could be a consequence of the compartmentation of diverse cAMPdependent kinases.

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Section: Ofaplysia Californica By Photoaffinity Labeling Withmentioning

confidence: 99%

Structural studies on a family of cAMP-binding proteins in the nervous system of Aplysia.

Eppler¹,

Bayley²,

Greenberg³

et al. 1986

The Journal of Cell Biology

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show abstract

“…Corrected mobilities of protein bands were calculated according to the procedure of Weber & Osborn (1969). The molar concentration of the C subunit was calculated by assuming a Mr of 40 000 (Hartl & Roskoski, 1983).…”

Section: Methodsmentioning

confidence: 99%

Adenosine cyclic 3',5'-monophosphate dependent protein kinase: fluorescent affinity labeling of the catalytic subunit from bovine skeletal muscle with o-phthalaldehyde

Puri¹,

Bhatnagar²,

Roskoski³

1985

Biochemistry

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The catalytic subunit of adenosine cyclic 3',5'-monophosphate dependent protein kinase from bovine skeletal muscle was rapidly inactivated by o-phthalaldehyde at 25 degrees C (pH 7.3). The reaction followed pseudo-first-order kinetics, and the second-order rate constant was 1.1 X 10(2) M-1 s-1. Absorbance and fluorescence spectroscopic data were consistent with the formation of an isoindole derivative (1 mol/mol of enzyme). The reaction between the catalytic subunit and o-phthalaldehyde was not reversed by the addition of reagents containing free primary amino and sulfhydryl functions following inactivation. The reaction, however, could be arrested at any stage during its progress by the addition of an excess of cysteine or less efficiently by homocysteine or glutathione. The catalytic subunit was protected from inactivation by the presence of the substrates magnesium adenosine triphosphate and an acceptor serine peptide substrate. The decrease in fluorescence emission intensity of incubation mixtures containing iodoacetamide- or 5'-[p-(fluorosulfonyl)benzoyl]adenosine-modified catalytic subunit and o-phthalaldehyde paralleled the loss of phosphotransferase activity. Catalytic subunit denatured with urea failed to react with o-phthalaldehyde. Inactivation of the catalytic subunit by o-phthalaldehyde is probably due to the concomitant modification of lysine-72 and cysteine-199. The proximal distance between the epsilon-amino function of the lysine and the sulfhydryl group of the cysteine residues involved in isoindole formation in the native enzyme is estimated to be approximately 3 A. The molar transition energy of the catalytic subunit-o-phthalaldehyde adduct was 121 kJ/mol and compares favorably with a value of 127 kJ/mol for the 1-[(beta-hydroxyethyl)thio]-2-(beta-hydroxyethyl)isoindole in hexane, indicating that the active site lysine and cysteine residues involved in formation of the isoindole derivative of the catalytic subunit are located in a hydrophobic environment. o-Phthalaldehyde probably acts as an active site specific reagent for the catalytic subunit.

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Protein phosphorylation in cultured endothelial cells

Mackie

Lai

Nairn

et al. 1986

Journal Cellular Physiology

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We have investigated the protein phosphorylation systems present in cultured bovine aortic and pulmonary artery endothelial cells. The cells contain cyclic AMP-dependent protein kinase, three calcium/calmodulin-dependent protein kinases, protein kinase C, and at least one tyrosine kinase. No cyclic GMP-dependent protein kinase activity was found. The cells also contained numerous substrates for cyclic AMP-dependent protein kinase and protein kinase C. Fewer substrates were found for the calcium/calmodulin-dependent protein kinases. There was little difference between either protein kinase activities or substrates when pulmonary artery endothelium was compared to aortic endothelium grown under similar culture conditions. It is likely that these various protein kinases and their respective substrate proteins are involved in mediating several of the actions of the hormones and drugs which affect the vascular endothelium.

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Cyclic adenosine 3':5'-monophosphate-dependent protein kinase. Comparison of type II enzymes from bovine brain, skeletal muscle, and cardiac muscle.

Cited by 30 publications

References 26 publications

Structural studies on a family of cAMP-binding proteins in the nervous system of Aplysia.

Structural studies on a family of cAMP-binding proteins in the nervous system of Aplysia.

Adenosine cyclic 3',5'-monophosphate dependent protein kinase: fluorescent affinity labeling of the catalytic subunit from bovine skeletal muscle with o-phthalaldehyde

Protein phosphorylation in cultured endothelial cells

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