Interferon-mediated protein kinase and low-molecular-weight inhibitor of protein synthesis

Nature ◽  
1976 ◽  
Vol 264 (5585) ◽  
pp. 477-480 ◽  
Author(s):  
WALDEN K. ROBERTS ◽  
ARA HOVANESSIAN ◽  
RONALD E. BROWN ◽  
MICHAEL J. CLEMENS ◽  
IAN M. KERR
Keyword(s):  
Molecular Weight ◽  
Protein Synthesis ◽  
Protein Kinase ◽  
Low Molecular Weight ◽  
Inhibitor Of Protein Synthesis

Synthesis of low molecular weight inhibitor of protein synthesis with enzyme from interferon-treated cells

Nature ◽  
1977 ◽  
Vol 268 (5620) ◽  
pp. 537-540 ◽  
Author(s):  
ARA G. HOVANESSIAN ◽  
RONALD E. BROWN ◽  
IAN M. KERR
Keyword(s):  
Molecular Weight ◽  
Protein Synthesis ◽  
Low Molecular Weight ◽  
Inhibitor Of Protein Synthesis

Small GTPase-regulated phospholipase D in granulocytes

1996 ◽  
Vol 74 (4) ◽  
pp. 459-467 ◽  
Author(s):  
Martin G. Houle ◽  
Sylvain Bourgoin
Keyword(s):  
Molecular Weight ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Tyrosine Kinases ◽  
Binding Proteins ◽  
Active Role ◽  
Small Gtpase ◽  
Low Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding

This review examines the functional role of phospholipase D in the neutrophil. Phospholipase D is emerging as an important component in the signal transduction pathways leading to granulocyte activation. Through the second messenger it produces, phosphatidic acid, phospholipase D plays an active role in the regulation of granulocyte NADPH oxidase activation and granular secretion. Many factors from both the cytosol and the membrane are necessary for maximal phospholipase D activation. This paper will focus on the regulation of phospholipase D by low molecular weight GTP-binding proteins, tyrosine kinases, and protein kinase C.Key words: phospholipase D, low molecular weight GTP-binding proteins, tyrosine kinases, protein kinase C, granulocytes.

scholarly journals Low molecular weight fibroblast growth factor-2 signals via protein kinase C and myofibrillar proteins to protect against postischemic cardiac dysfunction

2013 ◽  
Vol 304 (10) ◽  
pp. H1382-H1396 ◽  
Author(s):  
Janet R. Manning ◽  
Sarah O. Perkins ◽  
Elizabeth A. Sinclair ◽  
Xiaoqian Gao ◽  
Yu Zhang ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Fibroblast Growth Factor ◽  
Cardiac Dysfunction ◽  
Fibroblast Growth Factor 2 ◽  
Low Molecular Weight ◽  
Fibroblast Growth ◽  
Kinase C

Among its many biological roles, fibroblast growth factor-2 (FGF2) acutely protects the heart from dysfunction associated with ischemia/reperfusion (I/R) injury. Our laboratory has demonstrated that this is due to the activity of the low molecular weight (LMW) isoform of FGF2 and that FGF2-mediated cardioprotection relies on the activity of protein kinase C (PKC); however, which PKC isoforms are responsible for LMW FGF2-mediated cardioprotection, and their downstream targets, remain to be elucidated. To identify the PKC pathway(s) that contributes to postischemic cardiac recovery by LMW FGF2, mouse hearts expressing only LMW FGF2 (HMWKO) were bred to mouse hearts not expressing PKCα (PKCαKO) or subjected to a selective PKCε inhibitor (εV1–2) before and during I/R. Hearts only expressing LMW FGF2 showed significantly improved postischemic recovery of cardiac function following I/R ( P < 0.05), which was significantly abrogated in the absence of PKCα ( P < 0.05) or presence of PKCε inhibition ( P < 0.05). Hearts only expressing LMW FGF2 demonstrated differences in actomyosin ATPase activity as well as increases in the phosphorylation of troponin I and T during I/R compared with wild-type hearts; several of these effects were dependent on PKCα activity. This evidence indicates that both PKCα and PKCε play a role in LMW FGF2-mediated protection from cardiac dysfunction and that PKCα signaling to the contractile apparatus is a key step in the mechanism of LMW FGF2-mediated protection against myocardial dysfunction.

Sign in / Sign up

Export Citation Format

Share Document