BIOMAT Database Logo BIOMAT Database Logo

Phosphorylative neuromodulation of the regulatory subunit of cyclic AMP-dependent protein kinase type II in skeletal muscle. 1985

J A McLane, and S P Squinto, and H C Yeoh, and I R Held

The phosphorylative neuromodulation of the regulatory subunit of protein kinase type II (R-II) in cytosolic fractions from denervated and sham-operated, contralateral soleus muscles of the rat was evaluated. The denervation-induced increase in the 32P-phosphorylation of R-II is not related to an increased dephosphorylation by cation-dependent or cation-independent protein phosphatases in the cytosolic fractions. The level of 32P-phosphorylation of an exogenous heptapeptide substrate (Kemptide) by dissociated catalytic subunits of cyclic AMP-dependent protein kinase in cytosolic fractions from denervated and sham-operated solei did not differ. Also, no change in the concentration of cytosolic R-II assessed by competitive enzyme-linked immunosorbent assays (ELISA) was found after denervation. However, the in vitro 32P-phosphorylation of R-II in these samples was increased. Taken together, our results suggest that the increased availability of autophosphorylatable sites reflects an in vivo modulation of R-II phosphorylation rather than a significant change in total R-II content.

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009474 Neurons The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM. Nerve Cells,Cell, Nerve,Cells, Nerve,Nerve Cell,Neuron
D010085 Oxidative Phosphorylation Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds. Phosphorylation, Oxidative,Oxidative Phosphorylations,Phosphorylations, Oxidative
D010749 Phosphoprotein Phosphatases A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) Phosphoprotein Phosphatase,Phosphoprotein Phosphohydrolase,Protein Phosphatase,Protein Phosphatases,Casein Phosphatase,Ecto-Phosphoprotein Phosphatase,Nuclear Protein Phosphatase,Phosphohistone Phosphatase,Phosphoprotein Phosphatase-2C,Phosphoseryl-Protein Phosphatase,Protein Phosphatase C,Protein Phosphatase C-I,Protein Phosphatase C-II,Protein Phosphatase H-II,Protein-Serine-Threonine Phosphatase,Protein-Threonine Phosphatase,Serine-Threonine Phosphatase,Threonine Phosphatase,Ecto Phosphoprotein Phosphatase,Phosphatase C, Protein,Phosphatase C-I, Protein,Phosphatase C-II, Protein,Phosphatase H-II, Protein,Phosphatase, Casein,Phosphatase, Ecto-Phosphoprotein,Phosphatase, Nuclear Protein,Phosphatase, Phosphohistone,Phosphatase, Phosphoprotein,Phosphatase, Phosphoseryl-Protein,Phosphatase, Protein,Phosphatase, Protein-Serine-Threonine,Phosphatase, Protein-Threonine,Phosphatase, Serine-Threonine,Phosphatase, Threonine,Phosphatase-2C, Phosphoprotein,Phosphatases, Phosphoprotein,Phosphatases, Protein,Phosphohydrolase, Phosphoprotein,Phosphoprotein Phosphatase 2C,Phosphoseryl Protein Phosphatase,Protein Phosphatase C I,Protein Phosphatase C II,Protein Phosphatase H II,Protein Phosphatase, Nuclear,Protein Serine Threonine Phosphatase,Protein Threonine Phosphatase,Serine Threonine Phosphatase
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D003714 Denervation The resection or removal of the nerve to an organ or part. Laser Neurectomy,Neurectomy,Peripheral Neurectomy,Radiofrequency Neurotomy,Denervations,Laser Neurectomies,Neurectomies,Neurectomies, Laser,Neurectomies, Peripheral,Neurectomy, Laser,Neurectomy, Peripheral,Neurotomies, Radiofrequency,Neurotomy, Radiofrequency,Peripheral Neurectomies,Radiofrequency Neurotomies

Related Publications

J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Regulatory subunit of cyclic AMP-dependent protein kinase I from porcine skeletal muscle: purification and proteolysis.
September 1978, Archives of biochemistry and biophysics,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
A cyclic AMP-medicated intersubunit disulfide crosslinking reaction of the regulatory subunit of type II cyclic AMP-dependent protein kinase.
July 1982, FEBS letters,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Autophosphorylation of rabbit skeletal muscle cyclic AMP-dependent protein kinase I catalytic subunit.
October 1978, The Journal of biological chemistry,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
MTG8 proto-oncoprotein interacts with the regulatory subunit of type II cyclic AMP-dependent protein kinase in lymphocytes.
September 2001, Oncogene,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Production and characterization of monoclonal antibodies to type II regulatory subunit of cyclic AMP dependent protein kinase.
January 1980, Proceedings of the Western Pharmacology Society,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Phosphorylation of the regulatory subunit of type I cyclic AMP-dependent protein kinase by its catalytic subunit.
January 1985, Journal of cyclic nucleotide and protein phosphorylation research,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Kinetic mechanism of skeletal muscle cyclic AMP-dependent protein kinase.
March 1978, FEBS letters,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Role of cholinergic neuromuscular transmission in the neuroregulation of the autophosphorylatable regulatory subunit of cyclic AMP-dependent protein kinase type II and the acetylcholine receptor content in skeletal muscle.
March 1987, Brain research,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Phosphorylation of the type-II regulatory subunit of cyclic-AMP-dependent protein kinase by glycogen synthase kinase 3 and glycogen synthase kinase 5.
October 1982, European journal of biochemistry,
J A McLane, and S P Squinto, and H C Yeoh, and I R Held
Localization of the regulatory subunit of type II cyclic AMP-dependent protein kinase on the cytoplasmic microtubule network of cultured cells.
January 1982, Cell biology international reports,
Copied contents to your clipboard!