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| [1.] Dsa/Fragment 019 01 - Diskussion Zuletzt bearbeitet: 2016-08-02 19:07:34 WiseWoman | Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Wikipedia Protein kinase A 2007 |
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| Untersuchte Arbeit: Seite: 19, Zeilen: 1-10 |
Quelle: Wikipedia Protein kinase A 2007 Seite(n): 1 (online source), Zeilen: - |
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| Regulation
Protein kinase A has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It is controlled by cAMP: in the absence of cAMP, the kinase is a tetramer of two regulatory and two catalytic subunits (R2C2), with the regulatory subunits blocking the catalytic center of the catalytic subunits. Binding of cAMP to the regulatory subunit leads to dissociation of active RC dimers. Also, the catalytic subunit itself can be regulated by phosphorylation. Downregulation of protein kinase A occurs by a feedback mechanism: one of the substrates that are activated by the kinase is a phosphodiesterase, which converts cAMP to AMP, thus reducing the amount of cAMP that can activate protein kinase A. |
Regulation
Protein kinase A has several functions in the cell, including regulation of glycogen, sugar, and lipid metabolism. It is controlled by cAMP: in the absence of cAMP, the kinase is a tetramer of two regulatory and two catalytic subunits (R2C2), with the regulatory subunits blocking the catalytic center of the catalytic subunits. Binding of cAMP to the regulatory subunit leads to dissociation of active RC dimers. Also, the catalytic subunit itself can be regulated by phosphorylation. Downregulation of protein kinase A occurs by a feedback mechanism: one of the substrates that is activated by the kinase is a phosphodiesterase, which converts cAMP to AMP, thus reducing the amount of cAMP that can activate protein kinase A. |
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| [2.] Dsa/Fragment 019 11 - Diskussion Zuletzt bearbeitet: 2016-08-02 19:19:59 WiseWoman | Dsa, Fragment, Gesichtet, KidsNet Protein kinase 2007, KomplettPlagiat, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 19, Zeilen: 11-23 |
Quelle: KidsNet Protein kinase 2007 Seite(n): 1 (online source), Zeilen: - |
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| - Protein kinase C: protein kinase C is actually a family of protein kinases that require Ca2+, diacylglycerol, and a phospholipid such as phosphatidylcholine for activation. Thus, protein kinase C is activated through the same signal transduction pathway as phospholipase C. At least twelve members of the protein kinase C family have been identified in mammals, due to their high sequence homology. The protein kinase C usually means the protein kinase Cα enzyme.
Structure and regulation Protein kinase C enzymes consist of an N-terminal regulatory domain and a C-terminal catalytic domain. The kinases are inactive in the absence of activating agents, due to autoinhibition of the regulatory domain. They can be activated tumor promoters such as tetradecanoyl-phorbol-acetate (TPA) or by the cofactors Ca2+, diacylglycerol and a phospholipid. The common linear structure of protein kinase C enzymes is: N-pseudosubstrate - TPA-binding - (Ca2+-binding) - ATP-binding - substrate-binding- C. |
Protein kinase C
Protein kinase C is actually a family of protein kinases that require Ca2+, diacylglycerol, and a phospholipid such as phosphatidylcholine[?] for activation. Thus, protein kinase C is activated through the same signal transduction pathway as phospholipase C. At least twelve members of the proteine kinase C family have been identified in mammals, due to their high sequence homology[?]. The protein kinase C usually means the protein kinase Cα enzyme. Structure and regulation Protein kinase C enzymes consist of an N-terminal regulatory domain and a C-terminal catalytic domain. The kinases are inactive in the absence of activating agents, due to autoinhibition of the regulatory domain. They can be activated tumor promotors such as tetradecanoyl-phorbol-acetate[?] (TPA) or by the cofactors Ca2+, diacylglycerol, and a phospholipid. The common linear structure of protein kinase C enzymes is: N - pseudosubstrate - TPA-binding - (Ca2+-binding) - ATP-binding - substrate-binding - C |
The source is not given. Note: the text before and after the documented passage can also be found in this source, but other, more likely sources have been used for the documentation of those fragments. |
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| [3.] Dsa/Fragment 019 24 - Diskussion Zuletzt bearbeitet: 2016-08-02 19:03:47 WiseWoman | Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Wikipedia Protein kinase C 2007 |
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| Untersuchte Arbeit: Seite: 19, Zeilen: 24-34 |
Quelle: Wikipedia Protein kinase C 2007 Seite(n): 1 (online source), Zeilen: - |
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| 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. This is presumably achieved by the production of diacylglycerol from phosphatidylcholine by a phospholipase; fatty acids may also play a role in long-term activation.
Function 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 MARCKS proteins, MAP kinase, transcription factor inhibitor IκB, the vitamin D3 receptor VDR, Raf kinase, calpain, and the EGF receptor. |
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. This is presumably achieved by the production of diacylglycerol from phosphatidylcholine by a phospholipase; fatty acids may also play a role in long-term activation.
Function 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 MARCKS proteins, MAP kinase, transcription factor inhibitor IκB, the vitamin D3 receptor VDR, Raf kinase, calpain, and the epidermal growth factor receptor. |
No source is given. |
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| [4.] Dsa/Fragment 019 35 - Diskussion Zuletzt bearbeitet: 2016-08-02 19:12:17 WiseWoman | Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Wikipedia Serine-threonine-specific protein kinase 2006 |
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| Untersuchte Arbeit: Seite: 19, Zeilen: 35-42 |
Quelle: Wikipedia Serine-threonine-specific protein kinase 2006 Seite(n): 1 (online source), Zeilen: - |
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| Ca2+/calmodulin-dependent protein kinases:
Also called CaM kinases, these kinases are primarily regulated by the Ca2+/calmodulin complex. These kinases show a memory effect on activation. Two types of CaM kinases are: • Specialized CaM kinases. An example is the myosin light chain kinase (MLCK) that phosphorylates myosin, causing muscles to contract. • Multifunctional CaM kinases. Also collectively called CaM kinase II, which play a role in many processes, such as neurotransmitter secretion, transcription factor regulation, and glycogen metabolism. |
Ca2+/calmodulin-dependent protein kinases
Also called CaM kinases (EC 2.7.11.17), these kinases are primarily regulated by the Ca2+/calmodulin complex. These kinases show a memory effect on activation. Two types of CaM kinases are: • Specialized CaM kinases. An example is the myosin light chain kinase (MLCK) that phosphorylates myosin, causing muscles to contract. • Multifunctional CaM kinases. Also collectively called CaM kinase II, which play a role in many processes, such as neurotransmitter secretion, transcription factor regulation, and glycogen metabolism. |
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