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3 edition of Studies of the regulation of the bovine heart type II cAMP-dependent protein kinase found in the catalog.

Studies of the regulation of the bovine heart type II cAMP-dependent protein kinase

Catherine A. O"Brian

Studies of the regulation of the bovine heart type II cAMP-dependent protein kinase

by Catherine A. O"Brian

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Published .
Written in English


Edition Notes

Statementby Catherine A. O"Brian.
Classifications
LC ClassificationsMicrofilm 84/2644 (Q)
The Physical Object
FormatMicroform
Paginationvii, 169 leaves
Number of Pages169
ID Numbers
Open LibraryOL2562072M
LC Control Number85101416

Abstract. Genetic alterations in the PRKACA gene coding for the catalytic α subunit of the cAMP-dependent protein kinase A (PKA-C) are linked to cortisol-secreting adrenocortical adenomas, resulting in Cushing’s those, a single mutation (LR) has been found in up to 67% of patients. Because the x-ray structures of the wild-type and mutant kinases are essentially identical. Sisson JH, JR Spurzem, K. May, TA Wyatt Ethanol down-regulates cAMP-dependent protein kinase activation in bovine airway cells Am J Respir Crit Care Med ; (3)A Wyatt TA, Wish T, Sisson JH, Romberge DJ Extracellular cAMP-dependent protein kinase activity in alveolar proteinosis lavage fluid Am J Respir Crit Care Med ; (3)A.

Hypertension is asymptomatic and a well-known “silent killer”, which can cause various concomitant diseases in human population after years of adherence. Although there are varieties of synthetic antihypertensive drugs available in current market, their relatively low efficacies and major application in only single drug therapy, as well as the undesired chronic adverse effects associated Cited by: 8. The importance of Ca2+ signalling in key events of cancer cell function and tumour progression, such as proliferation, migration, invasion and survival, has recently begun to be appreciated. Many cellular Ca2+-stimulated signalling cascades utilise the intermediate, calmodulin (CaM). The Ca2+/CaM complex binds and activates a variety of enzymes, including members of the multifunctional Ca2 Cited by: 5.

Protein kinases are used to add phosphate groups to proteins. The one shown here is cAMP-dependent protein kinase, also known as protein kinase A or PKA (PDB entries 3tnp, 1j3h and 2h9r). It is composed of two types of subunits. The catalytic subunit, shown here in . The function of free sulfhydryl groups in the catalytic subunit of phosphorylase kinase Yuan, Chiun-Jye, "The function of free sulfhydryl groups in the catalytic subunit of phosphorylase kinase " ().Retrospective Theses with a homology of around 40% with that of cAMP-dependent protein kinase and other kinases. The homology of conserved.


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Studies of the regulation of the bovine heart type II cAMP-dependent protein kinase by Catherine A. O"Brian Download PDF EPUB FB2

Abstract. The C-subunit of type II cyclic AMP-dependent protein kinase from bovine heart was labelled with the fluorophore fluorescamine (FAM). The association of the dye-labelled subunit (CFAM) with the R-subunit isolated from the same source Cited by: 3. Immunization of guinea pigs with bovine cardiac cAMP-dependent protein kinase (ATP:protein phosphotransferase, EC ) resulted in the development of precipitating antibodies to the cAMP-binding subunit of the enzyme.

Both the phosphorylated and nonphosphorylated cAMP-binding protein of the protein kinase reacted with the by: STUDIES ON THE ACTIVATION MECHANISM OF CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASES F.

Hofmann, V. Flockerzi, K. Schwechheimer and N. Speichermann Pharmakologisches Institut der Universitat, Im Neuenheimer FeldD Heidelberg, Germany ABSTRACT Regulatory subunit free of cAMP and catalytic subunit has been prepared from type I and type II cAMP-dependent protein Author: F.

Hofmann, V. Flockerzi, K. Schwechheimer, N. Speichermann. MECHANISM OF REGULATION OF cAMP-DEPENDENT PROTEIN KINASE I, A N W TYPE OF ALLOSTERIC ENZYME CONTROL E Karl G. Wagner, Erwin Rieke, Rudiger Lawaczeck and Jlirgen Hoppe Abteilung Molekularbiologie, Gesellschaft flir Biotechnologische Forschung, Braunschweig The number of allosteric enzymes that are thoroughly understood regarding the interdependence of ligand Author: Karl G.

Wagner, Erwin Rieke, Rüdiger Lawaczeck, Jürgen Hoppe. In cell biology, protein kinase A (PKA) is a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP).

PKA is also known as cAMP-dependent protein kinase (EC ).Protein kinase A has several functions in the cell, including regulation of BRENDA: BRENDA entry.

In teraction the regulatory subunit of a type II cAMP-dependent protein kinase with mammalian sperm flagellum Article (PDF Available) in Journal of Biological Chemistry (4) March. Corbin JD, Sugden PH, West L, Flockhart DA, Lincoln TM, McCarthy D.

Studies on the properties and mode of action of the purified regulatory subunit of bovine heart adenosine 3’:5’-monophosphate-dependent protein by: 1. Get this from a library. Cellular regulation by protein phosphorylation: [proceedings of the NATO Advanced Study Institute on Cellular Regulation by Protein Phosphorylation held at Château LaLonde-les-Maures (France), September].

[Ludwig M G Heilmeyer; Advanced Study Institute on Cellular Regulation by Protein Phosphorylation (, La Londe-les-Maures);]. Bramson HN, Thomas N, Matsueda R, Nelson NC, Taylor SS and Kaiser ET () Modification of the Catalytic Subunit of Bovine Heart cAMP-Dependent Protein Kinase with Affinity Labels Related to Peptide Substrates.

Biol. Chem. – PubMed Google ScholarAuthor: S. Taylor, W. Yonemoto, W. Dostmann, D. Knighton, J. Sowadski, F. Herberg, J. Autonomic control of ventricular function occurs through regulation of cAMP-dependent protein kinase (PKA). The diabetic heart has suppressed β-adrenergic responsiveness, partly attributable to receptor changes, yet little is known about how PKA signaling is directly by: Protein phosphorylation in intact bovine epididymal spermatozoa: identification of the type II regulatory subunit of cyclic adenosine 3',5'-monophosphate-dependent protein kinase as an endogenous.

What I'd like to do here is to delve more deeply into the protein kinase structure and function. And if we look at PKA, PKA is, again, a prototype kinase we understand best.

And it is activated by hormone neurotransmitter binding to the outside of a cell. Expression of the -Subunit of Phosphorylase b Kinase in E. Coli.- Conformational and Shape Changes Associated with cAMP-Dependent Protein Kinase.- Crystallographic Studies of the Catalytic Subunit of cAMP-Dependent Protein Kinase.- 6-Phosphofructo 2-Kinase/Fructose 2,6-Bisphosphatase: Kinetic Changes Induced by Phosphorylation Protein kinases and phosphatases play pivotal roles in regulating and coordinating aspects of metabolism, gene expression, cell growth, cell motility, cell differentiation, and cell division.

As a result, if cellular life is to function in an orderly manner, the switching on and off of protein kinases and phosphatases is as crucial for their function as their catalytic by:   PKA and PKC Regulation of A-MuLV Envelope Protein-induced Syncytium Formation with NMU34m Cells—To determine if PKA and PKC demonstrate similar regulation of PiT2- and A-MuLV envelope-induced syncytium formation in a cell type other than NIH3T3 cells, kinase activator and inhibitor studies also were carried out with NMU34m cells.

Pyruvate dehydrogenase kinase (also pyruvate dehydrogenase complex kinase, PDC kinase, or PDK; EC ) is a kinase enzyme which acts to inactivate the enzyme pyruvate dehydrogenase by phosphorylating it using ATP. PDK thus participates in the regulation of the pyruvate dehydrogenase complex of which pyruvate dehydrogenase is the first component.

Both PDK and the pyruvate BRENDA: BRENDA entry. Activation of cAMP‐dependent protein kinase is necessary for actin rearrangements in human neutrophils during phagocytosis. Liselotte Ydrenius. Corresponding Author. E-mail address: [email protected] Department of Cell Biology, University of Linköping, by: Multiple forms of protein kinase inhibitor exist in mammalian testis.

Specific antibodies to testicular protein kinase inhibitor (PKI) have been raised in sheep. The antibody to the smallest of the inhibitors ( daltons) has been purified by antigen-affinity chromatography and shown to give a precipitin band with the inhibitor by double by: These hormones strongly activate cAMP-dependent protein kinases both in the cytosol and in humour cell nuclei by causing the elevation of PK-1 and PK-2 activities.

Ovarian hormone action on the proliferation is similar to that of growth factors, i.e., the hormones significantly stimulate the calcium-activated, phospholipid-dependent protein. There was good correlation between protein kinase activation and the increase in force. Epinephrine and the phosphodiesterase inhibitor 1-methylisobutylxanthine were synergistic in their stimulatory effects on cAMP, protein kinase activity, active phosphorylase, and contractile by:.

cAMP-dependent protein kinase (PKA) is the structural (Belham et al. ; Peterson and Schreiber ; prototype for members of the kinase family (Taylor et Toker and Newton ; Alessi ). The AGC fam-al. ). The PKA catalytic subunit is an active enzyme ily includes all isoforms of protein kinase C (PKC), pro-Cited by: cAMP-dependent activation of protein kinase A as a therapeutic target of skin hyperpigmentation by diphenylmethylene hydrazinecarbothioamide Hyoeun Shin1, Seung Deok Hong1, Eunmiri Roh1, Sang-Hun Jung2, Won-Jea Cho3, Sun Hong Park1, Da Young Yoon1, Seon Mi Ko1, Bang Yeon Hwang1, Jin Tae Hong1, Tae-Young Heo4, Sang-Bae Han1 and Youngsoo Kim1Cited by: This gene encodes a member of the cAMP-dependent protein kinase inhibitor family.

The encoded protein may play a role in the protein kinase A (PKA) pathway by interacting with the catalytic subunit of PKA, and overexpression of this gene may play a role in prostate cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.