Functional proteomic analysis of protein kinase C ε signaling complexes in the normal heart and during cardioprotection

Peipei Ping, Jun Zhang, William M. Pierce, Roberto Bolli

Research output: Contribution to journalArticle

Abstract

Using two-dimensional electrophoresis, mass spectrometry, immunoblotting, and affinity pull-down assays, we found that myocardial protein kinase C ε (PKCε) is physically associated with at least 36 known proteins that are organized into structural proteins, signaling molecules, and stress-responsive proteins. Furthermore, we found that the cardioprotection induced by activation of PKCε is coupled with dynamic modulation and recruitment of PKCε-associated proteins. The results suggest heretofore-unrecognized functions of PKCε and provide an integrated framework for the understanding of PKCε-dependent signaling architecture and cardioprotection.

Original languageEnglish (US)
Pages (from-to)59-62
Number of pages4
JournalCirculation Research
Volume88
Issue number1
StatePublished - Jan 19 2001
Externally publishedYes

Fingerprint

Proteomics
Protein Kinase C
Proteins
Heat-Shock Proteins
Immunoblotting
Electrophoresis
Mass Spectrometry

Keywords

  • Protein kinase C ε
  • Stress-activated kinases
  • Stress-activated proteins

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine

Cite this

Functional proteomic analysis of protein kinase C ε signaling complexes in the normal heart and during cardioprotection. / Ping, Peipei; Zhang, Jun; Pierce, William M.; Bolli, Roberto.

In: Circulation Research, Vol. 88, No. 1, 19.01.2001, p. 59-62.

Research output: Contribution to journalArticle

Ping, Peipei ; Zhang, Jun ; Pierce, William M. ; Bolli, Roberto. / Functional proteomic analysis of protein kinase C ε signaling complexes in the normal heart and during cardioprotection. In: Circulation Research. 2001 ; Vol. 88, No. 1. pp. 59-62.
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