Molecular and Cellular Biochemistry

, Volume 270, Issue 1, pp 215–221

Alternative splicing generates a CaM kinase IIβ isoform in myocardium that targets the sarcoplasmic reticulum through a putative αKAP and regulates GAPDH

  • Puneet Singh
  • John J. Leddy
  • George J. Chatzis
  • Maysoon Salih
  • Balwant S. Tuana
Article

DOI: 10.1007/s11010-005-5234-y

Cite this article as:
Singh, P., Leddy, J.J., Chatzis, G.J. et al. Mol Cell Biochem (2005) 270: 215. doi:10.1007/s11010-005-5234-y

Abstract

We report the isolation of a full length cDNA from cardiac muscle that encodes a ∼73 kDa calcium/calmodulin (CaM) dependent kinase IIβ isoform (CaMKIIβC) that was generated by alternative splicing of the CaMKIIβ gene. Antipeptide antibodies raised to specific regions of the kinase identified a 73 kDa kinase polypeptide in cardiac SR. Anti-alpha kinase anchoring protein (αKAP) antibodies identified a 25 kDa polypeptide in cardiac SR and RT-PCR followed by sequence analysis confirmed the presence of a full length αKAP encoding transcript in myocardium. Protein interaction assays revealed that the 73 kDa CaMKIIβC binds GAPDH to modulate the production of NADH in a Ca2+/CaM dependent reaction. The presence of a CaMKIIβ isoform that can target the SR presumably via its membrane anchor αKAP defines a previously unrecognized Ca2+/CaM regulatory system in myocardium. (Mol Cell Biochem 270: 215–221, 2005)

Key words

CaM kinase II GAPDH α-KAP myocardium NADH 

Copyright information

© Springer Science + Business Media, Inc. 2005

Authors and Affiliations

  • Puneet Singh
    • 1
  • John J. Leddy
    • 1
  • George J. Chatzis
    • 1
  • Maysoon Salih
    • 1
  • Balwant S. Tuana
    • 1
  1. 1.Department of Cellular and Molecular MedicineUniversity of OttawaOttawaCanada

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