Regulatory elements and functional implication for the formation of dimeric visinin-like protein-1

Ku Chung Chen, Li Kuan Wang, Long Sen Chang

研究成果: 雜誌貢獻文章同行評審

15 引文 斯高帕斯(Scopus)

摘要

Size exclusion chromatographic analyses showed that Ca 2+-free VILIP-1 contained both monomeric and dimeric forms, while no appreciable dimerization was noted with Ca 2+-free VILIP-3. Swapping of EF-hands 3 and 4 of VILIP-1 with those of VILIP-3 caused the inability of the resulting chimeric protein to form dimeric protein. Nonreducing SDS-PAGE analyses revealed that most of the dimeric VILIP-1 was noncovalently bound together. Reduced glutathione (GSH)/oxidized glutathione (GSSG) treatment notably enhanced the formation of disulfide-linked VILIP-1 dimer, while Ca 2+ and Mg 2+ enhanced disulfide dimerization of VILIP-1 marginally in the presence of thiol compounds. Cys-187 at the C-terminus of VILIP-1 contributed greatly to form S-S-crosslinked dimer as revealed by mutagenesis studies. The ability of GSH/GSSG-treated VILIP-1 to activate guanylyl cyclase B was reduced by substituting Cys-187 with Ala. Together with disulfide dimer of VILIP-1 detected in rat brain extracts, our data may imply the functional contribution of disulfide dimer to the interaction of VILIP-1 with its physiological target(s).

原文英語
頁(從 - 到)89-94
頁數6
期刊Journal of Peptide Science
15
發行號2
DOIs
出版狀態已發佈 - 2009
對外發佈Yes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Molecular Medicine
  • Structural Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmacology

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