Compartmentation of Second Messenger Action: Immunocytochemical and Biochemical Evidence - ScienceDirect

Vitamins & Hormones

Volume 42, 1985, Pages 197-252

Vitamins & Hormones

https://doi.org/10.1016/S0083-6729(08)60063-1 Get rights and content

Publisher Summary

This chapter discusses the compartmentation of second-messenger action. Extensive work has been reported by a number of investigators approaching the problems of compartmentalized second-messenger action. They have produced a body of evidence strongly suggesting that compartmentalization plays a vital role in cellular regulation. Immunocytochemical localization of second messengers and the proteins controlled by cyclic AMP (cAMP), cGMP, and Ca²⁺ often show distinct subcellular patterns best explained by compartmentation. cAMP serves as the second messenger for numerous hormones, including many catecholamines, prostaglandins, and peptide hormones. cAMP is synthesized intracellularly from ATP by the membrane-associated enzyme complex adenylate cyclase. Hormone binding to a receptor signals the catalytic unit of adenylate cyclase to increase cAMP synthesis rate via an intermediate protein G₈. The only known mechanism by which cAMP regulates eukaryotic cellular function is through the activation of cAMP-dependent protein kinases (cA-PKs), of which two general isozymic types exist. The holoenzyme is a tetramer consisting of two catalytic and two regulatory subunits. Kinase activity is regulated by cAMP binding to two sites on each of the regulatory (R) subunits of the cA-PK holoenzyme.

References (166)

F.A. Anderer
Preparation and properties of an artificial antigen immunologically related to tobacco mosaic virus
Biochim. Biophys. Acta
(1963)
H.-A. Arfmann et al.
High mobility group proteins from CHO cells and their modifications during cell cycle
Biochem. Biophys. Res. Commun.
(1981)
M.A. Ariano
Distribution of components of the guanosine 3′,5′-phosphate system in rat caudate-putamen
Neuroscience
(1983)
T. Asano et al.
Activation of the inhibitory GTP-binding protein of adenylate cyclase, Gi, by β-adrenergic receptors in reconstituted phospholipid vesicles
J. Biol. Chem.
(1984)
E.G. Beale et al.
N6, O2′-Dibutyryl-cyclic AMP and glucose regulate the amount of messenger RNA coding for hepatic phosphoenolpyruvate carboxykinase (GTP)
J. Biol. Chem.
(1982)
J.A. Beavo et al.
Identification and properties of cyclic nucleotide phosphodiesterases
Mol. Cell. Endocrinol.
(1982)
C. Boney et al.
Direct evidence that the protein kinase catalytic subunit mediates the effects of cAMP on tyrosine aminotransferase synthesis
J. Biol. Chem.
(1983)
C.L. Browne et al.
Localization of the regulatory subunit of type II cAMP-dependent protein kinase on the cytoplasmic microtubule network of cultured cells
Cell Biol. Int. Rep.
(1982)
I.L.O. Buxton et al.
Compartments of cyclic AMP and protein kinase in mammalian cardiomyocytes
J. Biol. Chem.
(1983)
M.A. Cimbala et al.
Rapid changes in the concentration of phosphoenolpyruvate carboxykinase mRNA in rat liver and kidney. Effects of insulin and cyclic AMP
J. Biol. Chem.
(1982)

P. Cohen et al.

The role of inhibitor-1 in the cyclic AMP-mediated control of glycogen metabolism in skeletal muscle

J.D. Corbin et al.

The distribution and dissociation of cyclic adenosine 3′,5′-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues

J. Biol. Chem.

(1975)

J.I. Davies et al.

Quantitative aspects of the regulation of cellular cyclic AMP levels. I. Structure and kinetics of a model system

J. Theor. Biol.

(1975)

E. DeRobertis

Nucleocytoplasmic segregation of proteins and RNAs

Cell

(1983)

C. Dingwall et al.

A polypeptide domain that specifies migration of nucleoplasmin into the nucleus

Cell

(1982)

F. Dopere et al.

Release and activation of phosphorylase phosphatase upon rupture of organelles from rat liver

Biochem. Biophys. Res. Commun.

(1982)

S.O. Doskeland et al.

Binding proteins for cyclic AMP in mammalian tissues

Int. J. Biochem.

(1981)

J.-G. Falbriard et al.

Preparation of derivatives of adenosine 3′,5′-phosphate

Biochim. Biophys. Acta

(1967)

D.A. Fell

Theoretical analyses of the functioning of high- and low-K m cyclic nucleotide phosphodiesterases in the regulation of the concentration of adenosine 3′,5′-cyclic monophosphate in animal cells

J. Theor. Biol.

(1980)

J.G. Foulkes et al.

Antagonistic effects of insulin and β-adrenergic agonists on the activity of protein phosphatase inhibitor-1 in skeletal muscle of the perfused rat hemicorpus

J. Biol. Chem.

(1982)

A.G. Gilman

G proteins and dual control of adenylate cyclase

Cell

(1984)

L. Goldstein

Localization of nucleus specific protein as shown by transplantation experiments in amoeba proteus

Exp. Cell Res.

(1958)

J.F. Harper et al.

Immunofluorescence localization of calmodulin in unfixed frozed tissue sections

D.R. Hathaway et al.

Interaction of calmodulin with myosin light-chain kinase and cAMP-dependent protein kinase in bovine brain

J. Biol. Chem.

(1981)

J.S. Hayes et al.

Selective activation of particulate cAMP-dependent protein kinase by isoproterenol and prostaglandin E1

J. Biol. Chem.

(1980)

J.S. Hayes et al.

Evidence for selective regulation of the phosphorylation of myocyte proteins by isoproterenol and prostaglandin E1

Biochim. Biophys. Acta

(1982)

C.M. Heyworth et al.

The phorbol ester, TPA inhibits glucagon-stimulated adenylate cyclase activity

FEBS Lett.

(1984)

F. Hofmann et al.

Concentrations of cyclic AMP-dependent protein kinase subunits in various tissues

J. Biol. Chem.

(1977)

P.B. Iynedjian et al.

Increase in level of functional messenger RNA coding for phosphoenolpyruvate carboxykinase (GTP) during induction by cyclic adenosine 3′,5′-monophosphate

J. Biol. Chem.

(1977)

E.M. Johnson et al.

Differential effects of cyclic adenosine-3′,5′-monophosphate on phosphorylation of rat liver nuclear acidic proteins

Arch. Biochem. Biophys.

(1972)

R.A. Jungmann et al.

Cyclic AMP regulation of lactate dehydrogenase. Isoproterenol and N 6, O 2′-dibutyryl-cyclic AMP increase the rate of transcription and change the stability of lactate dehydrogenase A subunit messenger RNA in rat C6 glioma cells

J. Biol. Chem.

(1983)

C.L. Kapoor et al.

Radioimmunoassay for the regulatory subunit of type I cAMP-dependent protein kinase

J. Biol. Chem.

(1979)

C.L. Kapoor et al.

Appearance of 50,000- and 52,000-dalton cAMP receptor proteins in the nucleoli of regressing MCF-7 human breast cancer upon estrogen withdrawal

Cell Biol. Int. Rep.

(1983)

E.S. Kempner et al.

The molecular biology of Euglena gracilis. IV. Cellular stratification by centrifuging

Exp. Cell Res.

(1968)

E.S. Kempner et al.

The molecular biology of Euglena gracilis. V. Enzyme localization

Exp. Cell Res.

(1968)

C.B. Klee et al.

Isolation and characterization of bovine brain calcineurin: A calmodulin-stimulated protein phosphatase

U. Klockmann et al.

Acylation: A new posttranslational modification specific for plasma membrane associated simian virus 40 large T antigen

FEBS Lett.

(1983)

Y. Koide et al.

Alterations in the intracellular distribution of cGMP and guanylate cyclase activity during rat liver regeneration

J. Biol. Chem.

(1978)

M.S. Laks et al.

Modulation of nuclear protein kinase activity and phosphorylation of histone H1 subspecies during the prereplicative phase of rat liver regeneration

J. Biol. Chem.

(1981)

R.E. Lanford et al.

Biochemical characterization of nuclear and cytoplasmic forms of SV40 tumor antigens encoded by parental and transport-defective mutant SV40-adenovirus 7 hybrid viruses

Virology

(1980)

J.C. Lawrence et al.

Hormonal control of glycogen synthase in rat hemidiaphragms: Effects of insulin and epinephrine on the distribution of phosphate between two cyanogen bromide fragment

J. Biol. Chem.

(1983)

S.A. Livesey et al.

Selective hormonal activation of cyclic AMP-dependent protein kinase isoenzymes in normal and malignant osteoblasts

J. Biol. Chem.

(1982)

M.S. Livingstone et al.

Loss of calcium/calmodulin responsiveness in adenylate cyclase of rutabaga, a Drosophila learning mutant

Cell

(1984)

F. Meyer et al.

Control of phosphorylase activity in a muscle glycogen particle

J. Biol. Chem.

(1970)

P.B. Moore et al.

Calcium binding proteins and cellular regulation

Life Sci.

(1982)

G.H. Murdoch et al.

Polypeptide hormone regulation of gene expression. Thyrotropin-releasing hormone rapidly stimulates both transcription of the prolactin gene and the phosphorylation of a specific nuclear protein

J. Biol. Chem.

(1983)

R.S. Adelstein et al.

Phosphorylation of smooth muscle myosin light chain kinase by the catalytic subunit of adenosine 3′:5′-monophosphate-dependent protein kinase

J. Biol. Chem.

(1978)

S. Alemany et al.

Antibody to protein phosphatase 2A as a probe of phosphatase structure and function

Eur. J. Biochem.

(1984)

R. Barber et al.

The egress of cyclic AMP from metazoan cells

Adv. Cyclic Nucleotide Res.

(1983)

F.E. Bloom et al.

Adenosine 3′,5′-monophosphate is localized in cerebellar neurons: Immunofluorescence evidence

Science

(1972)

Cited by (0)

Copyright © 1985 Academic Press Inc. Published by Elsevier Inc. All rights reserved.