Protein kinase C as a stress sensor

@article{citeulike:2221503, abstract = {While there are many reviews which examine the group of proteins known as protein kinase C (PKC), the focus of this article is to examine the cellular roles of two PKCs that are important for stress responses in neurological tissues (PKC[gamma] and [epsilon]) and in cardiac tissues (PKC[epsilon]). These two kinases, in particular, seem to have overlapping functions and interact with an identical target, connexin 43 (Cx43), a gap junction protein which is central to proper control of signals in both tissues. While PKC[gamma] and PKC[epsilon] both help protect neural tissue from ischemia, PKC[epsilon] is the primary PKC isoform responsible for responding to decreased oxygen, or ischemia, in the heart. Both do this through Cx43. It is clear that both PKC[gamma] and PKC[epsilon] are necessary for protection from ischemia. However, the importance of these kinases has been inferred from preconditioning experiments which demonstrate that brief periods of hypoxia protect neurological and cardiac tissues from future insults, and that this depends on the activation, translocation, or ability for PKC[gamma] and/or PKC[epsilon] to interact with distinct cellular targets, especially Cx43. This review summarizes the recent findings which define the roles of PKC[gamma] and PKC[epsilon] in cardiac and neurological functions and their relationships to ischemia/reperfusion injury. In addition, a biochemical comparison of PKC [gamma] and PKC [epsilon] and a proposed argument for why both forms are present in neurological tissue while only PKC [epsilon] is present in heart, are discussed. Finally, the biochemistry of PKCs and future directions for the field are discussed, in light of this new information.}, author = {Barnett, Micheal E. and Madgwick, Daniel K. and Takemoto, Dolores J. }, citeulike-article-id = {2221503}, doi = {http://dx.doi.org/10.1016/j.cellsig.2007.05.014}, journal = {Cellular Signalling}, month = {September}, number = {9}, pages = {1820--1829}, posted-at = {2008-01-12 03:09:20}, priority = {2}, title = {Protein kinase C as a stress sensor}, url = {http://dx.doi.org/10.1016/j.cellsig.2007.05.014}, volume = {19}, year = {2007} }

TY - JOUR ID - citeulike:2221503 L3 - citeulike-article-id:2221503 TI - Protein kinase C as a stress sensor JF - Cellular Signalling VL - 19 IS - 9 SP - 1820 EP - 1829 N2 - While there are many reviews which examine the group of proteins known as protein kinase C (PKC), the focus of this article is to examine the cellular roles of two PKCs that are important for stress responses in neurological tissues (PKC[gamma] and [epsilon]) and in cardiac tissues (PKC[epsilon]). These two kinases, in particular, seem to have overlapping functions and interact with an identical target, connexin 43 (Cx43), a gap junction protein which is central to proper control of signals in both tissues. While PKC[gamma] and PKC[epsilon] both help protect neural tissue from ischemia, PKC[epsilon] is the primary PKC isoform responsible for responding to decreased oxygen, or ischemia, in the heart. Both do this through Cx43. It is clear that both PKC[gamma] and PKC[epsilon] are necessary for protection from ischemia. However, the importance of these kinases has been inferred from preconditioning experiments which demonstrate that brief periods of hypoxia protect neurological and cardiac tissues from future insults, and that this depends on the activation, translocation, or ability for PKC[gamma] and/or PKC[epsilon] to interact with distinct cellular targets, especially Cx43. This review summarizes the recent findings which define the roles of PKC[gamma] and PKC[epsilon] in cardiac and neurological functions and their relationships to ischemia/reperfusion injury. In addition, a biochemical comparison of PKC [gamma] and PKC [epsilon] and a proposed argument for why both forms are present in neurological tissue while only PKC [epsilon] is present in heart, are discussed. Finally, the biochemistry of PKCs and future directions for the field are discussed, in light of this new information. AU - Barnett, Micheal AU - Madgwick, Daniel AU - Takemoto, Dolores PY - 2007/09// UR - http://dx.doi.org/10.1016/j.cellsig.2007.05.014 ER -