By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators discuss new findings in Proteins. According to news reporting from Tokyo, Japan, by NewsRx journalists, research stated, "In this study, we have investigated the specific binding proteins of Zinc-l-carnosine (Polaprezinc) using Polaprezinc-affinity column chromatography in vitro. A protein having a 70-kDa molecular mass was eluted by the linear gradient of 01.0 mM Polaprezinc from the affinity column and the protein was identified as the molecular chaperone HSP70 by immunoblotting."
The news correspondents obtained a quote from the research from Juntendo University, "The chaperone activity of HSP70 was completely suppressed by Polaprezinc. The ATPase activity of HSP70 was affected to some extent by the reagent. In the circular dichroism (CD) spectrum, the secondary structure of HSP70 was changed in the presence of Polaprezinc, i.e. it decreased in the alpha-helix. We have determined the Polaprezinc-binding domain of HSP70 by using recombinant HSP70N- and C-domains. Although Polaprezinc could bind to both the N-terminal and the C-terminal of HSP70, the HSP70N-domain has a high affinity to the drug. Regarding the peptide cleavage of the HSP70N- and C-domains with proteinase K, the intact HSP70N still remained in the presence of Polaprezinc. On the other hand, the quantity of the intact C-domain slightly decreased under the same conditions along with the newly digested small peptides appeared."
According to the news reporters, the research concluded: "It has been suggested that Polaprezinc binds to HSP70 especially in the N-domains, suppresses the chaperone activity and delays an ATPase activities of HSP70."
For more information on this research see: Zinc-l-carnosine binds to molecular chaperone HSP70 and inhibits the chaperone activity of the protein. Journal of Biochemistry, 2013;154(3):249-256. Journal of Biochemistry can be contacted at: Oxford Univ Press, Great Clarendon St, Oxford OX2 6DP, England. (Oxford University Press - www.oup.com/; Journal of Biochemistry - jb.oxfordjournals.org)
Our news journalists report that additional information may be obtained by contacting A. Haga, Juntendo University, Dept. of Gastroenterol, Sch Med, Bunkyo Ku, Tokyo 1138421, Japan. Additional authors for this research include T. Okamoto, S. Yamada, T. Kubota, A. Sanpei, S. Takahashi, M. Nakayama, M. Nagai, M. Otaka, T. Miyazaki, W. Nunomura, E. Grave and H. Itoh (see also Proteins).
Keywords for this news article include: Asia, Tokyo, Japan, Proteins, Molecular Chaperones
Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2013, NewsRx LLC