Protein Kinase C

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(Added the references correctly, that is, I added them as explained in the lecture. Cleaned up the text. Not one link!!! So, I added some.)
 
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Protein kinase C, commonly abbreviated to PKC, is a family of [[protein kinase|protein kinase]] [[enzyme|enzymes]] that are involved in controlling the function of other [[proteins|proteins]] through the [[phosphorylation|phosphorylation]] of [[hydroxyl groups|hydroxyl groups]] of [[serine|serine]] and [[threonine|threonine]] [[amino acid|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|diacylglycerol]] (DAG) or [[calcium ions|calcium ions]] (Ca<sup>2+</sup>)<ref>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.</ref>. Hence PKC enzymes play important roles in several [[Signal_transduction|signal transduction cascades]]<ref>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". BBA − Molecular Cell Research. 1863: 2135–46.</ref><br>  
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Protein kinase C, commonly abbreviated to PKC, is a family of [[Protein kinase|protein kinase]] [[Enzyme|enzymes]] that are involved in controlling the function of other [[Proteins|proteins]] through the [[Phosphorylation|phosphorylation]] of [[Hydroxyl groups|hydroxyl groups]] of [[Serine|serine]] and [[Threonine|threonine]] [[Amino acid|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|diacylglycerol]] (DAG) or [[Calcium ions|calcium ions]] (Ca<sup>2+</sup>)<ref>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.</ref>. Hence PKC enzymes play important roles in several [[Signal transduction|signal transduction cascades]]<ref>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". BBA − Molecular Cell Research. 1863: 2135–46.</ref>.<br>  
  
 
=== References  ===
 
=== References  ===
  
 
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Latest revision as of 20:34, 6 December 2017

Protein kinase C, commonly abbreviated to PKC, 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].

References

  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.
  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". BBA − Molecular Cell Research. 1863: 2135–46.

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