サイクリックGMP依存性タンパク質リン酸化酵素、cGMP依存性タンパク質リン酸化酵素

関: cyclic GMP-dependent protein kinase、G-kinase、protein kinase G

WordNet

relying on or requiring a person or thing for support, supply, or what is needed; "dependent children"; "dependent on moisture"
addicted to a drug (同)dependant, drug-addicted, hooked, strung-out
contingent on something else (同)dependant, qualified
(of a clause) unable to stand alone syntactically as a complete sentence; "a subordinate (or dependent) clause functions as a noun or adjective or adverb within a sentence" (同)subordinate
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
an enzyme that catalyzes the conversion of a proenzyme to an active enzyme
the basic unit of money in Papua New Guinea

PrepTutorEJDIC

『頼っている』,依存している,従属している / 扶養される人(家族)
蛋白(たんばく)質

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/11/25 12:35:57」(JST)

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cGMP-dependent protein kinase or Protein Kinase G (PKG) is a serine/threonine-specific protein kinase that is activated by cGMP. It phosphorylates a number of biologically important targets and is implicated in the regulation of smooth muscle relaxation, platelet function, sperm metabolism, cell division, and nucleic acid synthesis.

Genes and proteins[edit]

PKG are serine/threonine kinases that are present in a variety of eukaryotes ranging from the unicellular organism Paramecium to humans. Two PKG genes, coding for PKG type I (PKG-I) and type II (PKG-II), have been identified in mammals. The N-terminus of PKG-I is encoded by two alternatively spliced exons that specify for the PKG-Iα and PKG-Iβ isoforms. PKG-Iβ is activated at ~10-fold higher cGMP concentrations than PKG-Iα. The PKG-I and PKG-II are homodimers of two identical subunits (~75 kDa and ~85 kDa, respectively) and share common structural features.

Each subunit is composed of three functional domains:

(1) an N-terminal domain that mediates homodimerization, suppression of the kinase activity in the absence of cGMP, and interactions with other proteins including protein substrates
(2) a regulatory domain that contains two non-identical cGMP-binding sites
(3) a kinase domain that catalyzes the phosphate transfer from ATP to the hydroxyl group of a serine/threonine side chain of the target protein

Binding of cGMP to the regulatory domain induces a conformational change which stops the inhibition of the catalytic core by the N-terminus and allows the phosphorylation of substrate proteins. Whereas PKG-I is predominantly localized in the cytoplasm, PKG-II is anchored to the plasma membrane by N-terminal myristoylation.

Tissue distribution[edit]

In general, PKG-I and PKG-II are expressed in different cell types.

PKG-I has been detected at high concentrations (above 0.1 µmol/L) in all types of smooth muscle cells (SMCs) including vascular SMCs and in platelets. Lower levels are present in vascular endothelium and cardiomyocytes. The enzyme is also expressed in fibroblasts, certain types of renal cells and leukocytes, and in specific regions of the nervous system, for example in the hippocampus, in cerebellar Purkinje cells, and in dorsal root ganglia. Neurons express either the PKG-Iα or the PKG-Iβ isoform, platelets predominantly Iβ, and both isoforms are present in smooth muscle.
PKG-II has been detected in renal cells, zona glomerulosa cells of the adrenal cortex, Clara cells in distal airways, intestinal mucosa, pancreatic ducts, parotid and submandibular glands, chondrocytes, and several brain cell nuclei, but not in cardiac and vascular myocytes.

Specifically, in smooth muscle tissue, PKG promotes the opening of calcium-activated potassium channels, leading to cell hyperpolarization and relaxation, and blocks agonist activity of phospholipase C, reducing liberation of stored calcium ions by inositol triphosphate.

Role in cancer[edit]

Cancerous colon cells stop producing PKG, which apparently limits beta-catenin thus allowing the VEGF enzyme to solicit angiogenesis.^[2]

References[edit]

^ PDB 3NMD; Casteel DE, Smith-Nguyen EV, Sankaran B, Roh SH, Pilz RB, Kim C (October 2010). "A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring". J. Biol. Chem. 285 (43): 32684–8. doi:10.1074/jbc.C110.161430. PMID 20826808.
^ Kwon IK, Schoenlein PV, Delk J, Liu K, Thangaraju M, Dulin NO, Ganapathy V, Berger FG, Browning DD (April 2008). "Expression of cyclic guanosine monophosphate-dependent protein kinase in metastatic colon carcinoma cells blocks tumor angiogenesis". Cancer 112 (7): 1462–70. doi:10.1002/cncr.23334. PMID 18260092.

External links[edit]

EC 2.7.11.12
Cyclic GMP-Dependent Protein Kinases and the Cardiovascular System
cGMP-Dependent Protein Kinases at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

A PKG inhibitor increases Ca2+-regulated exocytosis in guinea pig antral mucous cells: cAMP accumulation via PDE2A inhibition.

Tanaka S, Tanaka R, Harada S, Kohda Y, Matsumura H, Shimamoto C, Sawabe Y, Marunaka Y, Kuwabara H, Takahashi Y, Ito S, Nakahari T.SourceDept. of Physiology, Osaka Medical College, Takatsuki 569-8686, Japan. takan@art.osaka-med.ac.jp.
American journal of physiology. Gastrointestinal and liver physiology.Am J Physiol Gastrointest Liver Physiol.2013 May;304(9):G773-80. doi: 10.1152/ajpgi.00281.2012. Epub 2013 Feb 28.
In antral mucous cells, acetylcholine (ACh, 1 μM) activates Ca(2+)-regulated exocytosis, consisting of an initial peak that declines rapidly (initial transient phase) followed by a second slower decline (late phase) lasting during ACh stimulation. The addition of 8-bromo-cGMP (8-BrcGMP) enhanced th
PMID 23449671

Inhibition of diuretic stimulation of an insect secretory epithelium by a cGMP-dependent protein kinase.

Ruka KA, Miller AP, Blumenthal EM.SourceDept. of Biological Sciences, Marquette Univ., P.O. Box 1881, Milwaukee, WI 53201-1881. edward.blumenthal@marquette.edu.
American journal of physiology. Renal physiology.Am J Physiol Renal Physiol.2013 May;304(9):F1210-6. doi: 10.1152/ajprenal.00231.2012. Epub 2013 Feb 27.
The rate of urine secretion by insect Malpighian tubules (MTs) is regulated by multiple diuretic and antidiuretic hormones, often working either synergistically or antagonistically. In the Drosophila melanogaster MT, only diuretic factors have been reported. Two such agents are the biogenic amine ty
PMID 23445619

Japanese Journal

Cyclic GMP-Dependent Signaling in Cardiac Myocytes

TAKIMOTO Eiki
Circulation journal : official journal of the Japanese Circulation Society 76(8), 1819-1825, 2012-07-25
… Cyclic GMP (cGMP) and its effector kinase PKG regulate diverse cellular functions. … In cardiac myocytes, cGMP is produced by soluble and particulate guanylyl cyclases (GCs), the former stimulated by nitric oxide and the latter by natriuretic peptides, and is hydrolyzed to inactive 5′-GMP by cGMP-phosphodiesterases (PDEs). … cGMP-PKG modulates cardiac contractility, hypertrophy and remodeling, and exerts cardioprotection. …
NAID 10030504080

Hydrogen Peroxide Enhances Vasodilatation by Increasing Dimerization of cGMP-Dependent Protein Kinase Type Iα

DOU Dou,ZHENG Xiaoxu,LIU Juan,XU Xiaojian,YE Liping,GAO Yuansheng
Circulation journal : official journal of the Japanese Circulation Society 76(7), 1792-1798, 2012-06-25
… Background: cGMP-dependent protein kinase type I (PKG I) plays a key role in vasodilatation caused by cGMP-elevating agents. … In isolated porcine coronary arteries, H2O2 increased the dimers of total PKG I in a concentration-dependent manner, but had no effect on dimerization of PKG Iβ. …
NAID 10030503931

Stabilization of cGMP-dependent protein kinase G (PKG) expression in vascular smooth muscle cells : contribution of 3'UTR of its mRNA

Sellak Hassan,Lincoln Thomas M.,Choi Chung-Sik
The journal of biochemistry 149(4), 433-441, 2011-04-01
NAID 10030584717

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★リンクテーブル★

リンク元	「サイクリックGMP依存性タンパク質リン酸化酵素」「cGMP依存性タンパク質リン酸化酵素」「G-kinase」「cyclic GMP-dependent protein kinase」
関連記事	「dependent」「kinase」「protein kinase」

「サイクリックGMP依存性タンパク質リン酸化酵素」

protein kinase, cGMP-dependent, type II
Identifiers
Symbol	PRKG2
Entrez	5593
HUGO	9416
OMIM	601591
RefSeq	NM_006259
UniProt	Q13237
Other data
Locus	Chr. 4 q13.1-21.1

protein kinase, cGMP-dependent, type I
	; Crystallographic structure of the leucine zipper domain of human cGMP dependent protein kinase I beta.
Identifiers
Symbol	PRKG1
Alt. symbols	PRKGR1B, PRKG1B
Entrez	5592
HUGO	9414
OMIM	176894
RefSeq	NM_006258
UniProt	Q13976
Other data
Locus	Chr. 10 q11.2

　　[★]

英: cGMP-dependent protein kinase、protein kinase G、G-kinase
関: プロテインキナーゼG、cGMP依存性タンパク質リン酸化酵素、サイクリックGMP依存性タンパク質キナーゼ、Gキナーゼ

「cGMP依存性タンパク質リン酸化酵素」

　　[★]

英: cGMP-dependent protein kinase
関: プロテインキナーゼG、サイクリックGMP依存性タンパク質リン酸化酵素、サイクリックGMP依存性プロテインキナーゼ

「G-kinase」

　　[★]

Gキナーゼ、プロテインキナーゼG、サイクリックGMP依存性タンパク質リン酸化酵素

関: cGMP-dependent protein kinase、protein kinase G

「cyclic GMP-dependent protein kinase」

　　[★]

サイクリックGMP依存性プロテインキナーゼ

関: cGMP-dependent protein kinase、protein kinase G

「dependent」

　　[★]

adj.

依存性の、依存的な、依存型の、依存の

関: depend、dependence、dependency、dependently

「kinase」

　　[★] キナーゼカイネースリン酸化酵素 phosphoenzyme phosphotransferase 　

「protein kinase」

　　[★] プロテインキナーゼ

同: protein kinases

[pmid20826808-1] PDB 3NMD; Casteel DE, Smith-Nguyen EV, Sankaran B, Roh SH, Pilz RB, Kim C (October 2010). "A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring". J. Biol. Chem. 285 (43): 32684–8. doi:10.1074/jbc.C110.161430. PMID 20826808.

[pmid18260092-2] Kwon IK, Schoenlein PV, Delk J, Liu K, Thangaraju M, Dulin NO, Ganapathy V, Berger FG, Browning DD (April 2008). "Expression of cyclic guanosine monophosphate-dependent protein kinase in metastatic colon carcinoma cells blocks tumor angiogenesis". Cancer 112 (7): 1462–70. doi:10.1002/cncr.23334. PMID 18260092.

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案内

cGMP-dependent protein kinase