同: PKC

WordNet

the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system
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

PrepTutorEJDIC

carbonの化学記号
蛋白(たんばく)質
cesiumの化学記号
cadmiumの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2019/05/12 02:25:49」(JST)

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Protein kinase C, commonly abbreviated to PKC (EC 2.7.11.13), is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or a member of this family. PKC enzymes in turn are activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca²⁺).^[1] Hence PKC enzymes play important roles in several signal transduction cascades.^[2]

The PKC family consists of fifteen isozymes in humans.^[3] They are divided into three subfamilies, based on their second messenger requirements: conventional (or classical), novel, and atypical.^[4] Conventional (c)PKCs contain the isoforms α, β_I, β_II, and γ. These require Ca²⁺, DAG, and a phospholipid such as phosphatidylserine for activation. Novel (n)PKCs include the δ, ε, η, and θ isoforms, and require DAG, but do not require Ca²⁺ for activation. Thus, conventional and novel PKCs are activated through the same signal transduction pathway as phospholipase C. On the other hand, atypical (a)PKCs (including protein kinase Mζ and ι / λ isoforms) require neither Ca²⁺ nor diacylglycerol for activation. The term "protein kinase C" usually refers to the entire family of isoforms.

Isozymes

conventional - require DAG, Ca²⁺, and phospholipid for activation
- PKC-α (PRKCA)
- PKC-β1 (PRKCB)
- PKC-β2 (PRKCB)
- PKC-γ (PRKCG)
novel - require DAG but not Ca²⁺ for activation
- PKC-δ (PRKCD)
- PKC-ε (PRKCE)
- PKC-η (PRKCH)
- PKC-θ (PRKCQ)
atypical - require neither Ca²⁺ nor DAG for activation (require phosphatidyl serine)
- PKC-ι (PRKCI)
- PKC-ζ (PRKCZ)
related PKD
- PKD1 (PRKD1)
- PKD2 (PRKD2)
- PKD3 (PRKD3)
related PKN
- PK-N1 (PKN1)
- PK-N2 (PKN2)
- PK-N3 (PKN3)

Structure

The structure of all PKCs consists of a regulatory domain and a catalytic domain tethered together by a hinge region. The catalytic region is highly conserved among the different isoforms, as well as, to a lesser degree, among the catalytic region of other serine/threonine kinases. The second messenger requirement differences in the isoforms are a result of the regulatory region, which are similar within the classes, but differ among them. Most of the crystal structure of the catalytic region of PKC has not been determined, except for PKC theta and iota. Due to its similarity to other kinases whose crystal structure have been determined, the structure can be strongly predicted.

Regulatory

The regulatory domain or the amino-teminus of the PKCs contains several shared subregions. The C1 domain, present in all of the isoforms of PKC has a binding site for DAG as well as non-hydrolysable, non-physiological analogues called phorbol esters. This domain is functional and capable of binding DAG in both conventional and novel isoforms, however, the C1 domain in atypical PKCs is incapable of binding to DAG or phorbol esters. The C2 domain acts as a Ca²⁺ sensor and is present in both conventional and novel isoforms, but functional as a Ca²⁺ sensor only in the conventional. The pseudosubstrate region, which is present in all three classes of PKC, is a small sequence of amino acids that mimic a substrate and bind the substrate-binding cavity in the catalytic domain,lack critical serine, threonine phosphoacceptor residues, keeping the enzyme inactive. When Ca²⁺ and DAG are present in sufficient concentrations, they bind to the C2 and C1 domain, respectively, and recruit PKC to the membrane. This interaction with the membrane results in release of the pseudosubstrate from the catalytic site and activation of the enzyme. In order for these allosteric interactions to occur, however, PKC must first be properly folded and in the correct conformation permissive for catalytic action. This is contingent upon phosphorylation of the catalytic region, discussed below.

Catalytic

The catalytic region or kinase core of the PKC allows for different functions to be processed; PKB (also known as Akt) and PKC kinases contains approximately 40% amino acid sequence similarity. This similarity increases to ~ 70% across PKCs and even higher when comparing within classes. For example, the two atypical PKC isoforms, ζ and ι/λ, are 84% identical (Selbie et al., 1993). Of the over-30 protein kinase structures whose crystal structure has been revealed, all have the same basic organization. They are a bilobal structure with a β sheet comprising the N-terminal lobe and an α helix constituting the C-terminal lobe. Both the ATP- and substrate-binding sites are located in the cleft formed by these two lobes. This is also where the pseudosubstrate domain of the regulatory region binds.^{[context needed]}

Another feature of the PKC catalytic region that is essential to the viability of the kinase is its phosphorylation. The conventional and novel PKCs have three phosphorylation sites, termed: the activation loop, the turn motif, and the hydrophobic motif. The atypical PKCs are phosphorylated only on the activation loop and the turn motif. Phosphorylation of the hydrophobic motif is rendered unnecessary by the presence of a glutamic acid in place of a serine, which, as a negative charge, acts similar in manner to a phosphorylated residue. These phosphorylation events are essential for the activity of the enzyme, and 3-phosphoinositide-dependent protein kinase-1 (PDK1) is the upstream kinase responsible for initiating the process by transphosphorylation of the activation loop.^[5]

The consensus sequence of protein kinase C enzymes is similar to that of protein kinase A, since it contains basic amino acids close to the Ser/Thr to be phosphorylated. Their substrates are, e.g., MARCKS proteins, MAP kinase, transcription factor inhibitor IκB, the vitamin D₃ receptor VDR, Raf kinase, calpain, and the epidermal growth factor receptor.

Activation

Upon activation, protein kinase C enzymes are translocated to the plasma membrane by RACK proteins (membrane-bound receptor for activated protein kinase C proteins). The protein kinase C enzymes are known for their long-term activation: They remain activated after the original activation signal or the Ca²⁺-wave is gone. It is presumed that this is achieved by the production of diacylglycerol from phosphatidylinositol by a phospholipase; fatty acids may also play a role in long-term activation.

Function

A multiplicity of functions have been ascribed to PKC. Recurring themes are that PKC is involved in receptor desensitization, in modulating membrane structure events, in regulating transcription, in mediating immune responses, in regulating cell growth, and in learning and memory. These functions are achieved by PKC-mediated phosphorylation of other proteins. However, the substrate proteins present for phosphorylation vary, since protein expression is different between different kinds of cells. Thus, effects of PKC are cell-type-specific:

Cell type	Organ/system	Activators ligands --> G_q-GPCRs	Effects
smooth muscle cell (gastrointestinal tract sphincters)	digestive system	prostaglandin F_2α^[6] --> thromboxanes^[6]	contraction
smooth muscle cells in: iris dilator muscle (sensory system) urethral sphincter (urinary system) uterus (reproductive system) arrector pili muscles (integumentary system) ureter (urinary system) urinary bladder (urinary system)^[7]^[8]	Various	adrenergic agonists --> α1 receptor	contraction
smooth muscle cells in: iris constrictor muscle ciliary muscle	sensory system	acetylcholine --> M3 receptor	contraction
smooth muscle cell (vascular)	circulatory system	5-HT --> 5-HT2A receptor adrenergic agonists --> α1 receptor	vasoconstriction^[9]^:187^[9]^:127
smooth muscle cell (seminal tract)^[9]^:163^[10]	reproductive system	adrenergic agonists --> α1 receptor	ejaculation
smooth muscle cell (GI tract)	digestive system	5-HT --> 5-HT2A or 5-HT2B receptor^[9]^:187 acetylcholine (ACh) --> M3 receptor	contraction^[11]
smooth muscle cell (bronchi)	respiratory system	5-HT --> 5-HT2A receptor adrenergic agonists --> β₂ receptor acetylcholine --> M3^[12] and M1 receptor^[13]	bronchoconstriction^[9]^:187
proximal convoluted tubule cell	kidney	angiotensin II --> AT1 receptor adrenergic agonists --> α1 receptor	stimulate NHE3 --> H⁺ secretion & Na⁺ reabsorption^[14] stimulate basolateral Na-K ATPase --> Na⁺ reabsorption^[14]
neurons in autonomic ganglia	nervous system	acetylcholine --> M1 receptor	EPSP
neurons in CNS	nervous system	5-HT --> 5-HT2A receptor glutamate --> NMDA receptor	neuronal excitation (5-HT)^[9]^[15]^:187 memory (glutamate)^[16]
platelets	circulatory system	5-HT --> 5-HT2A receptor^[9]^:187	aggregation^[9]^:187
ependymal cells (choroid plexus)	ventricular system	5-HT --> 5-HT2C receptor^[9]^:187	↑cerebrospinal fluid secretion^[9]^:187
heart muscle	circulatory system	adrenergic agonists --> β1 receptor	positive ionotropic effect^[7]
serous cells (salivary gland)	digestive system	acetylcholine --> M1 and M3 receptors adrenergic agonists --> β1 receptor	↑secretion^[7] increase salivary potassium levels.
serous cells (lacrimal gland)	digestive system	acetylcholine --> M3 receptor	↑secretion^[9]^:127
adipocyte	digestive system/endocrine system	adrenergic agonists --> β3 receptor	glycogenolysis and gluconeogenesis^[7]
hepatocyte	digestive system	adrenergic agonists --> α1 receptor	glycogenolysis and gluconeogenesis^[7]
sweat gland cells	integumentary system	adrenergic agonists --> β2 receptor	↑secretion^[7]
parietal cells	digestive system	acetylcholine --> M3 receptors^[17]	↑ gastric acid secretion

Pathology

Protein kinase C, activated by tumor promoter phorbol ester, may phosphorylate potent activators of transcription, and thus lead to increased expression of oncogenes, promoting cancer progression,^[18] or interfere with other phenomena. Prolonged exposure to phobol ester, however, promotes the down-regulation of Protein kinase C. Loss-of-function mutations ^[19] and low PKC protein levels^[20] are prevalent in cancer, supporting a general tumor-suppressive role for Protein kinase C.

Protein kinase C enzymes are important mediators of vascular permeability and have been implicated in various vascular diseases including disorders associated with hyperglycemia in diabetes mellitus, as well as endothelial injury and tissue damage related to cigarette smoke. Low-level PKC activation is sufficient to reverse cell chirality through phosphatidylinositol 3-kinase/AKT signaling and alters junctional protein organization between cells with opposite chirality, leading to an unexpected substantial change in endothelial permeability, which often leads to inflammation and disease.^[21]

Inhibitors

Protein kinase C inhibitors, such as ruboxistaurin, may potentially be beneficial in peripheral diabetic nephropathy.^[22]

Chelerythrine is a natural selective PKC inhibitor. Other naturally occurring PKCIs are miyabenol C, myricitrin, gossypol.

Other PKCIs : Verbascoside, BIM-1.

Bryostatin 1 can act as a PKC inhibitor; It was investigated for cancer.

Activators

The Protein kinase C activator ingenol mebutate, derived from the plant Euphorbia peplus, is FDA-approved for the treatment of actinic keratosis.^[23]^[24]

Bryostatin 1 can act as a PKCe activator and as of 2016 is being investigated for Alzheimer's disease.^[25]

References

^ Wilson CH, Ali ES, Scrimgeour N, Martin AM, Hua J, Tallis GA, Rychkov GY, Barritt GJ (2015). "Steatosis inhibits liver cell store-operated Ca²⁺ entry and reduces ER Ca²⁺ through a protein kinase C-dependent mechanism". The Biochemical Journal. 466 (2): 379–90. doi:10.1042/BJ20140881. PMID 25422863.
^ Ali ES, Hua J, Wilson CH, Tallis GA, Zhou FH, Rychkov GY, Barritt GJ (2016). "The glucagon-like peptide-1 analogue exendin-4 reverses impaired intracellular Ca2+ signalling in steatotic hepatocytes". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1863 (9): 2135–46. doi:10.1016/j.bbamcr.2016.05.006. PMID 27178543.
^ Mellor H, Parker PJ (Jun 1998). "The extended protein kinase C superfamily". The Biochemical Journal. 332. 332 (Pt 2): 281–92. doi:10.1042/bj3320281. PMC 1219479. PMID 9601053.
^ Nishizuka Y (Apr 1995). "Protein kinase C and lipid signaling for sustained cellular responses" (abstract). FASEB Journal. 9 (7): 484–96. doi:10.1096/fasebj.9.7.7737456. PMID 7737456.
^ Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR (Jul 2000). "A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1". The Journal of Biological Chemistry. 275 (27): 20806–13. doi:10.1074/jbc.M000421200. PMID 10764742.
^ ^a ^b Biancani P, Harnett KM (2006). "Signal transduction in lower esophageal sphincter circular muscle, PART 1: Oral cavity, pharynx and esophagus". GI Motility Online. doi:10.1038/gimo24 (inactive 2019-04-28).
^ ^a ^b ^c ^d ^e ^f Fitzpatrick D, Purves D, Augustine G (2004). "Table 20:2". Neuroscience (Third ed.). Sunderland, Mass: Sinauer. ISBN 978-0-87893-725-7.
^ Chou EC, Capello SA, Levin RM, Longhurst PA (Dec 2003). "Excitatory alpha1-adrenergic receptors predominate over inhibitory beta-receptors in rabbit dorsal detrusor". The Journal of Urology. 170 (6 Pt 1): 2503–7. doi:10.1097/01.ju.0000094184.97133.69. PMID 14634460.
^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k Rang HP, Dale MM, Ritter JM, Moore PK (2003). "Ch. 10". Pharmacology (5th ed.). Elsevier Churchill Livingstone. ISBN 978-0-443-07145-4.
^ Koslov DS, Andersson K (2013-01-01). "Physiological and pharmacological aspects of the vas deferens—an update". Integrative and Regenerative Pharmacology. 4: 101. doi:10.3389/fphar.2013.00101. PMID 23986701.
^ Sanders KM (Jul 1998). "G protein-coupled receptors in gastrointestinal physiology. IV. Neural regulation of gastrointestinal smooth muscle". The American Journal of Physiology. 275 (1 Pt 1): G1–7. doi:10.1152/ajpgi.1998.275.1.G1. PMID 9655677.
^ Parker K, Brunton L, Goodman LS, Lazo JS, Gilman A (2006). Goodman & Gilman's the pharmacological basis of therapeutics (11th ed.). New York: McGraw-Hill. p. 185. ISBN 978-0-07-142280-2.
^ "Entrez Gene: CHRM1 cholinergic receptor, muscarinic 1".
^ ^a ^b Walter F. Boron (2005). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. ISBN 978-1-4160-2328-9. Page 787
^ Barre A, Berthoux C, De Bundel D, Valjent E, Bockaert J, Marin P, Bécamel C (2016). "Presynaptic serotonin 2A receptors modulate thalamocortical plasticity and associative learning". Proceedings of the National Academy of Sciences of the United States of America. 113 (10): E1382–91. Bibcode:2016PNAS..113E1382B. doi:10.1073/pnas.1525586113. PMC 4791007. PMID 26903620.
^ Jalil SJ, Sacktor TC, Shouval HZ (2015). "Atypical PKCs in memory maintenance: the roles of feedback and redundancy". Learning & Memory. 22 (7): 344–53. doi:10.1101/lm.038844.115. PMC 4478332. PMID 26077687.
^ Boron, Walter F. Medical Physiology.
^ Yamasaki T, Takahashi A, Pan J, Yamaguchi N, Yokoyama KK (March 2009). "Phosphorylation of Activation Transcription Factor-2 at Serine 121 by Protein Kinase C Controls c-Jun-mediated Activation of Transcription". The Journal of Biological Chemistry. 284 (13): 8567–81. doi:10.1074/jbc.M808719200. PMC 2659215. PMID 19176525.
^ Antal CE, Hudson AM, Kang E, Zanca C, Wirth C, Stephenson NL, Trotter EW, Gallegos LL, Miller CJ, Furnari FB, Hunter T, Brognard J, Newton AC (January 2015). "Cancer-associated protein kinase C mutations reveal kinase's role as tumor suppressor". Cell. 160 (3): 489–502. doi:10.1016/j.cell.2015.01.001. PMC 4313737. PMID 25619690.
^ Baffi TR, Van AN, Zhao W, Mills GB, Newton AC (March 2019). "Protein Kinase C Quality Control by Phosphatase PHLPP1 Unveils Loss-of-Function Mechanism in Cancer". Molecular Cell. 74 (2): 378–392.e5. doi:10.1016/j.molcel.2019.02.018. PMID 30904392.
^ Fan J, Ray P, Lu Y, Kaur G, Schwarz J, Wan L (24 October 2018). "Cell chirality regulates intercellular junctions and endothelial permeability". Science Advances. 4 (10): eaat2111. Bibcode:2018SciA....4.2111F. doi:10.1126/sciadv.aat2111. PMC 6200360. PMID 30397640.
^ Anderson PW, McGill JB, Tuttle KR (Sep 2007). "Protein kinase C beta inhibition: the promise for treatment of diabetic nephropathy". Current Opinion in Nephrology and Hypertension. 16 (5): 397–402. doi:10.1097/MNH.0b013e3281ead025. PMID 17693752.
^ Siller G, Gebauer K, Welburn P, Katsamas J, Ogbourne SM (Feb 2009). "PEP005 (ingenol mebutate) gel, a novel agent for the treatment of actinic keratosis: results of a randomized, double-blind, vehicle-controlled, multicentre, phase IIa study". The Australasian Journal of Dermatology. 50 (1): 16–22. doi:10.1111/j.1440-0960.2008.00497.x. PMID 19178487.
^ "FDA Approves Picato® (ingenol mebutate) Gel, the First and Only Topical Actinic Keratosis (AK) Therapy With 2 or 3 Consecutive Days of Once-Daily Dosing". eMedicine. Yahoo! Finance. January 25, 2012. Archived from the original on February 10, 2012. Retrieved 2012-02-14.
^ Amended FDA Protocol Submitted for Phase 2b Trial of Advanced Alzheimer’s Therapy. Aug 2016

External links

protein+kinase+c at the US National Library of Medicine Medical Subject Headings (MeSH)
Eukaryotic Linear Motif resource motif class MOD_LATS_1

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. プロテインキナーゼCと糖尿病の血管合併症 protein kinase c and the vascular complications of diabetes mellitus
2. 虚血プレコンディショニングの定義および病因 definition and pathogenesis of ischemic preconditioning
3. 血小板生物学 platelet biology
4. 心臓の虚血性再潅流障害 ischemic reperfusion injury of the heart
5. T細胞受容体シグナル伝達 t cell receptor signaling

English Journal

Analysis of the cell wall integrity pathway of Ashbya gossypii.

Lengeler KB, Wasserstrom L, Walther A, Wendland J.SourceCarlsberg Laboratory, Yeast Genetics, Gamle Carlsberg Vej 10, DK-1799 Copenhagen V, Denmark.
Microbiological research.Microbiol Res.2013 Dec 14;168(10):607-14. doi: 10.1016/j.micres.2013.06.008. Epub 2013 Jul 10.
Fungal cells are exposed to rapidly changing environmental conditions, in particular with regard to the osmotic potential. This requires constant remodeling of the cell wall and, therefore, the cell wall integrity (CWI) MAP-kinase pathway plays a major role in shaping the fungal cell wall to protect
PMID 23850207

Regulation of the MIR155 host gene in physiological and pathological processes.

Elton TS, Selemon H, Elton SM, Parinandi NL.SourceDavis Heart and Lung Research Institute, The Ohio State University, Columbus, OH, USA; College of Pharmacy, Division of Pharmacology, The Ohio State University, Columbus, OH, USA; Department of Medicine, Division of Cardiology, The Ohio State University, Columbus, OH, USA. Electronic address: terry.elton@osumc.edu.
Gene.Gene.2013 Dec 10;532(1):1-12. doi: 10.1016/j.gene.2012.12.009. Epub 2012 Dec 14.
MicroRNAs (miRNAs), a family of small nonprotein-coding RNAs, play a critical role in posttranscriptional gene regulation by acting as adaptors for the miRNA-induced silencing complex to inhibit gene expression by targeting mRNAs for translational repression and/or cleavage. miR-155-5p and miR-155-3
PMID 23246696

Spinal cord maturation and locomotion in mice with an isolated cortex.

Han Q, Feng J, Qu Y, Ding Y, Wang M, So KF, Wu W, Zhou L.SourceGuangdong-Hongkong-Macau Institute of CNS Regeneration, Jinan University, Guangzhou 510632, PR China.
Neuroscience.Neuroscience.2013 Dec 3;253:235-44. doi: 10.1016/j.neuroscience.2013.08.057. Epub 2013 Sep 4.
The spinal cord plays a key role in motor behavior. It relays major sensory information, receives afferents from supraspinal centers and integrates movement in the central pattern generators. Spinal motor output is controlled via corticofugal pathways including corticospinal and cortico-subcortical
PMID 24012835

Japanese Journal

Involvement of autophagy in the pharmacological effects of the mTOR inhibitor everolimus in acute kidney injury.

Nakagawa Shunsaku,Nishihara Kumiko,Inui Ken-Ichi,Masuda Satohiro
European journal of pharmacology 696(1-3), 143-154, 2012-12-05
… Using cells from normal kidney epithelial cell lines, we found that the antiproliferative effects of mTOR inhibitor everolimus accompanied the accumulation of a marker for cellular autophagic activity, the phosphatidylethanolamine-conjugated form of microtubule-associated protein 1 light chain 3 (LC3-II) in cells. … We also showed that the primary autophagy factor UNC-51-like kinase 1 was involved in the antiproliferative effects of everolimus. …
NAID 120004996384

A Tobacco CBL-Interacting Protein Kinase Homolog Is Involved in Phosphorylation of the N-Terminal Domain of the Cucumber Mosaic Virus Polymerase 2a Protein

KANG Hyun Ku,YANG Seung Hwan,LEE Young Pyo [他]
Bioscience, Biotechnology, and Biochemistry 76(11), 2101-2106, 2012-11
NAID 40019498943

Related Pictures

Protein Kinase C as a Therapeutic Target | Clinical Cancer Research プロテインキナーゼC - JapaneseClass.jp Frontiers | Protein Kinase C: Targets to Regenerate Brain Injuries? | Cell and Protein kinase C (PK-C) ̌ ڎw diacylglycerol (DAG) ̊ U ̂̍ Protein Kinase C-delta; PKC-delta Serine-Threonine Kinase PKCδ - Briacell

★リンクテーブル★

リンク元	「プロテインキナーゼC」「PKC」「リン脂質依存性タンパク質リン酸化酵素」「C-kinase」「リン脂質依存性タンパク質キナーゼ」
拡張検索	「protein kinase C-θ」「protein kinase C-activating factor」「protein kinase C-alpha」「protein kinase C-epsilon」
関連記事	「C」「kinase」「protein kinase」「Cs」「Cd」

「プロテインキナーゼC」

Protein kinase C terminal domain
Identifiers
Symbol	Pkinase_C
Pfam	PF00433
InterPro	IPR017892
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

Protein kinase C
Identifiers
EC number	2.7.11.13
CAS number	141436-78-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: protein kinase C PKC
同: Cキナーゼ C kinase、リン脂質依存性プロテインキナーゼ phospholipid-dependent protein kinase
関: カルシウム依存性プロテインキナーゼ、プロテインキナーゼ

「PKC」

　　[★]

同: protein kinase C

「リン脂質依存性タンパク質リン酸化酵素」

　　[★]

英: protein kinase C、C-kinase
関: Cキナーゼ、プロテインキナーゼC、リン脂質依存性タンパク質キナーゼ

「C-kinase」

　　[★]

Cキナーゼ、プロテインキナーゼC、リン脂質依存性タンパク質リン酸化酵素

関: PKC、protein kinase C

「リン脂質依存性タンパク質キナーゼ」

　　[★]

英: protein kinase C
関: プロテインキナーゼC、リン脂質依存性タンパク質リン酸化酵素

「protein kinase C-θ」

　　[★]

英: [[]]
同: PKC-θ
関: [[]]

同: PKC-θ

「protein kinase C-activating factor」

　　[★] プロテインキナーゼC活性化因子

「protein kinase C-alpha」

　　[★]

プロテインキナーゼCα

「protein kinase C-epsilon」

　　[★]

プロテインキナーゼCε

「C」

　　[★]

炭素 carbon
シトシン cytosine
システイン cysteine
シチジン
セルシウス度摂氏 degrees Celsius degree C
産婦人科領域で「子宮外頚子宮外頚部 exocervix」を表現するための略語

「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

「Cs」

　　[★] セシウム, caesium, cesium 　

「Cd」

　　[★] カドミウム

関: cadmium

[1] Wilson CH, Ali ES, Scrimgeour N, Martin AM, Hua J, Tallis GA, Rychkov GY, Barritt GJ (2015). "Steatosis inhibits liver cell store-operated Ca²⁺ entry and reduces ER Ca²⁺ through a protein kinase C-dependent mechanism". The Biochemical Journal. 466 (2): 379–90. doi:10.1042/BJ20140881. PMID 25422863.

[2] Ali ES, Hua J, Wilson CH, Tallis GA, Zhou FH, Rychkov GY, Barritt GJ (2016). "The glucagon-like peptide-1 analogue exendin-4 reverses impaired intracellular Ca2+ signalling in steatotic hepatocytes". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1863 (9): 2135–46. doi:10.1016/j.bbamcr.2016.05.006. PMID 27178543.

[pmid9601053-3] Mellor H, Parker PJ (Jun 1998). "The extended protein kinase C superfamily". The Biochemical Journal. 332. 332 (Pt 2): 281–92. doi:10.1042/bj3320281. PMC 1219479. PMID 9601053.

[pmid7737456-4] Nishizuka Y (Apr 1995). "Protein kinase C and lipid signaling for sustained cellular responses" (abstract). FASEB Journal. 9 (7): 484–96. doi:10.1096/fasebj.9.7.7737456. PMID 7737456.

[pmid10764742-5] Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR (Jul 2000). "A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1". The Journal of Biological Chemistry. 275 (27): 20806–13. doi:10.1074/jbc.M000421200. PMID 10764742.

[Biancani-6] Biancani P, Harnett KM (2006). "Signal transduction in lower esophageal sphincter circular muscle, PART 1: Oral cavity, pharynx and esophagus". GI Motility Online. doi:10.1038/gimo24 (inactive 2019-04-28).

[purves-7] ^ ^a ^b ^c ^d ^e ^f Fitzpatrick D, Purves D, Augustine G (2004). "Table 20:2". Neuroscience (Third ed.). Sunderland, Mass: Sinauer. ISBN 978-0-87893-725-7.

[pmid14634460-8] Chou EC, Capello SA, Levin RM, Longhurst PA (Dec 2003). "Excitatory alpha1-adrenergic receptors predominate over inhibitory beta-receptors in rabbit dorsal detrusor". The Journal of Urology. 170 (6 Pt 1): 2503–7. doi:10.1097/01.ju.0000094184.97133.69. PMID 14634460.

[Rang-9] ^ ^a ^b ^c ^d ^e ^f ^g ^h ⁱ ^j ^k Rang HP, Dale MM, Ritter JM, Moore PK (2003). "Ch. 10". Pharmacology (5th ed.). Elsevier Churchill Livingstone. ISBN 978-0-443-07145-4.

[10] Koslov DS, Andersson K (2013-01-01). "Physiological and pharmacological aspects of the vas deferens—an update". Integrative and Regenerative Pharmacology. 4: 101. doi:10.3389/fphar.2013.00101. PMID 23986701.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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protein kinase C