[Alteration of phospholamban phosphatase activity associated with cardiac sarcoplasmic reticulum during sepsis in rats].

Abstract

In the present study, rat cardiac sarcoplasmic reticulum (SR) phospholamban (PLB) phosphatase was partially purified by chromatography on DEAE-Sephacel. This PLB phosphatase was indentical to phosphatase-1. It was shown on electrophoresis of SDS-PAGE autoradiography that the PLB phosphatase in rats during early sepsis (ES) depressed dephosphorylation of substrates (32P-phosphorylase a and 32P-SR). However, dephosphorylation of the substrates by the partially purified phosphatase during late sepsis (LS) was same as that in control rats. The partially purified PLB phosphatase activity in ES rats was significantly decreased, but showed no change in LS rats. The results above were confirmed by a studing of the substrate concentration (enzyme concentration, time)--enzyme reaction velocity curve in showing that both affinity and maximum initial velocity (Vmax) of the phosphatase in the ES rats were decreased, but had no change in those in the LS rats.

• Authors: Q Yang, L L Wu, X Tang, C S Tang
• Journal: Sheng li xue bao : [Acta physiologica Sinica] (Sheng Li Xue Bao) Vol. 47 Issue 4 Pg. 357-65 (Aug 1995) ISSN: 0371-0874 [Print] China
• PMID: 7481877 (Publication Type: English Abstract, Journal Article)

Chemical References

• phospholamban phosphatase
• Phosphoprotein Phosphatases
• Protein Phosphatase 1
• Adenosine Triphosphatases

Topics

• Adenosine Triphosphatases (metabolism)
• Animals
• Male
• Myocardium (enzymology)
• Phosphoprotein Phosphatases (metabolism)
• Protein Phosphatase 1
• Rats
• Rats, Sprague-Dawley
• Sarcoplasmic Reticulum (enzymology)
• Shock, Septic (enzymology)