Rationally designed peptide regulators of protein kinase C.

Abstract

Protein-protein interactions sequester enzymes close to their substrates. Protein kinase C (PKC) is one example of a ubiquitous signaling molecule with effects that are dependent upon localization. Short peptides derived from interaction sites between each PKC isozyme and its receptor for activated C kinase act as highly specific inhibitors and have become available as selective drugs in basic research and animal models of human diseases, such as myocardial infarction and hyperglycemia. Whereas the earlier inhibitory peptides are highly specific, we believe that peptides targeting additional interactions between PKC and selective substrates will generate even more selective tools that regulate different functions of individual isozymes. Here, we discuss the methodologies and applications for identifying selective regulators of PKC.

• Authors: Eric N Churchill, Nir Qvit, Daria Mochly-Rosen
• Journal: Trends in endocrinology and metabolism: TEM (Trends Endocrinol Metab) Vol. 20 Issue 1 Pg. 25-33 (Jan 2009) ISSN: 1043-2760 [Print] United States
• PMID: 19056296 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)

Chemical References

• Enzyme Activators
• Enzyme Inhibitors
• Peptide Fragments
• Protein Kinase C

Topics

• Amino Acid Sequence
• Animals
• Drug Design
• Enzyme Activation (drug effects)
• Enzyme Activators (chemical synthesis, chemistry, pharmacology)
• Enzyme Inhibitors (chemical synthesis, chemistry, pharmacology)
• Humans
• Models, Biological
• Models, Molecular
• Molecular Sequence Data
• Peptide Fragments (chemical synthesis, chemistry, pharmacology)
• Protein Binding (drug effects)
• Protein Kinase C (metabolism, physiology)