Protein kinase C activity and isoform expression during early postnatal development of rat myocardium.

作者: B. Hamplova , O. Novakova , E. Tvrzicka , F. Kolar , F. Novak

DOI: 10.1385/CBB:43:1:105

关键词:

摘要: Total protein kinase C (PKC) activity, its isoform expression, and concentration fatty acid (FA) composition of diacylglycerol (DAG) were determined in the left ventricular myocardium rat during early postnatal development (d 2, 3, 5, 7, 10). PKC activity measured by incorporation 32P into histone IIIS decreased between d 2 10 homogenate as well cytosolic, membrane (100,000g), nuclear-cytoskeletal-myofilament fractions (1000g). Likewise, expression isoforms (α, δ, e) immunoblotting generally declined period analyzed, although with a variable pattern. In nuclear cytoskeletal myofilament fractions, PKCδ PKCe markedly returning to or close level immediately on 5. PKCα fraction remained almost unchanged declining thereafter. associated predominantly particulate whereas was more abundant cytosolic fraction. DAG exhibited significant decline consistent decrease maximal activity. The unsaturation index FA tended 3 owing lowered proportion all polyunsaturated n−6 n−3 series. These results demonstrate that developmental is not linear subcellular localization enzyme exhibits isoform-specific day-by-day changes period. are compatible view signaling may be involved control rapid switch myocardial growth pattern first week life.

参考文章(41)
Kathy L Schreiber, Louise Paquet, Bruce G Allen, Hansjörg Rindt, None, Protein kinase C isoform expression and activity in the mouse heart. American Journal of Physiology-heart and Circulatory Physiology. ,vol. 281, ,(2001) , 10.1152/AJPHEART.2001.281.5.H2062
Ashwani Malhotra, Barinder Pal Singh Kang, David Opawumi, Waindel Belizaire, Leonard G. Meggs, Molecular biology of protein kinase C signaling in cardiac myocytes. Molecular and Cellular Biochemistry. ,vol. 225, pp. 97- 107 ,(2001) , 10.1023/A:1012261903611
A. Kishimoto, Y. Takai, T. Mori, U. Kikkawa, Y. Nishizuka, Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover. Journal of Biological Chemistry. ,vol. 255, pp. 2273- 2276 ,(1980) , 10.1016/S0021-9258(19)85886-6
Abdelkarim Sabri, Susan F. Steinberg, Protein kinase C isoform-selective signals that lead to cardiac hypertrophy and the progression of heart failure Molecular and Cellular Biochemistry. ,vol. 251, pp. 97- 101 ,(2003) , 10.1007/978-1-4419-9238-3_14
Yasutomi Nishizuka, Protein kinase C and lipid signaling for sustained cellular responses. The FASEB Journal. ,vol. 9, pp. 484- 496 ,(1995) , 10.1096/FASEBJ.9.7.7737456
Daria Mochly-Rosen, Adrienne S. Gordon, Anchoring proteins for protein kinase C: a means for isozyme selectivity The FASEB Journal. ,vol. 12, pp. 35- 42 ,(1998) , 10.1096/FASEBJ.12.1.35
Marian Mosior, Alexandra C. Newton, Mechanism of Interaction of Protein Kinase C with Phorbol Esters REVERSIBILITY AND NATURE OF MEMBRANE ASSOCIATION Journal of Biological Chemistry. ,vol. 270, pp. 25526- 25533 ,(1995) , 10.1074/JBC.270.43.25526
Y Nishizuka, Studies and perspectives of protein kinase C Science. ,vol. 233, pp. 305- 312 ,(1986) , 10.1126/SCIENCE.3014651
Nicole R. Murray, Alan P. Fields, Phosphatidylglycerol Is a Physiologic Activator of Nuclear Protein Kinase C Journal of Biological Chemistry. ,vol. 273, pp. 11514- 11520 ,(1998) , 10.1074/JBC.273.19.11514