کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1927453 1536517 2006 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Ganglioside GM2 modulates the erythrocyte Ca2+-ATPase through its binding to the calmodulin-binding domain and its 'receptor'
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Ganglioside GM2 modulates the erythrocyte Ca2+-ATPase through its binding to the calmodulin-binding domain and its 'receptor'
چکیده انگلیسی
We have previously demonstrated that gangliosides were able to modulate the plasma membrane Ca2+-ATPase (PMCA) from porcine brain synaptosomes and porcine erythrocytes [Y. Zhao, X. Fan, F. Yang, X. Zhang, Arch. Biochem. Biophys. 427 (2004) 204-212 and J. Zhang, Y. Zhao, J. Duan, F. Yang, X. Zhang, Arch. Biochem. Biophys. 444 (2005) 1-6]. The results indicated that the PMCA from porcine erythrocytes responded to gangliosides was different from that from synaptosomes, suggesting that the effects of gangliosides on the PMCA are isoform specific. Most interestingly, GM2 activated the PMCA from porcine erythrocytes at lower concentrations, but inhibited it at higher concentrations. In the present study, we found that GD1b, GM1 and GM3 did not affect the calpain digested PMCA from porcine erythrocytes or the intact enzyme in the presence of calmodulin, while GM2 inhibited it. Moreover, a synthetic peptide of 17 amino acid residues corresponding to the 'receptor' of the calmodulin-binding domain of the enzyme interfered with the inhibition of the enzyme by GM2 in competition assays. Taken together, our results suggested that gangliosides GD1b, GM1, GM2 (lower concentrations) and GM3 stimulated the PMCA by the interaction with calmodulin-binding domain, while the interaction of GM2 with the 'receptor' of the calmodulin-binding domain of the enzyme led to the inhibition of the enzyme.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 454, Issue 2, 15 October 2006, Pages 155-159
نویسندگان
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