Abstract
The cardiovascular heat shock protein (cvHsp/HspB7) exhibited cardiac-specific expression and is a possiblecandidate of dilated cardiomyopathy in heart failure. The molecular characteristics and biochemical properties of cvHspare only partially understood. This study was aimed to identify the biological properties and molecular high-order structureof cvHsp. The cvHsp protein was prepared by the refined purification at large amount. The pooled fractions were existedas two types of oligomers in solution and exhibited chaperone-like activity. The circular dichroism analyzed ureainducedunfolding processes. Multiple sequence alignment and an automated protein modeling were used to describe thethree-dimensional structural model of the cvHsp monomer and dimer. By the refined purification, the cvHsp appeared inoligomeric and dimeric forms (approximately 17 kDa and 40 kDa, respectively) composed of 18.6-kDa monomers. ThecvHsp prevented dithiothreitol (DTT)-induced aggregation of the insulin B chain and conferred oligomeric unfoldingprocess in urea-containing solution. It exhibited structural stability and conformed to the two-state folding/unfolding oligomerizationmodel. According to sequence alignment of the rat cvHsp gene, three-dimensional model based on the crystallographicstructure of wheat Hsp16.9 was reconstructed. The cvHsp presented two antiparallel β-sheet sandwich structureof sHsp’ core α-crystallin domain, and formed dimeric or oligomeric organization in solution. This work describedthe structural components of cvHsp and existed as the polydispersed molecular oligomers in vitro, which are some commonproperties of the sHsp family. These characteristics of the cvHsp gene is helpful to clarify molecular functionality incardiac diseases.
Keywords:CvHsp, modeling, molecular chaperone, secondary structure, sHsp.
Protein & Peptide Letters
Title:Refined Purification of Large Amounts of Rat cvHsp/HspB7 and Partial Biological Characterization In Vitro
Volume: 21Issue: 5
Author(s):Wei Lin, Zehong Yang, Yongzhi Lu and Xiaojun Zhao
Affiliation:
Keywords:CvHsp, modeling, molecular chaperone, secondary structure, sHsp.
Abstract: The cardiovascular heat shock protein (cvHsp/HspB7) exhibited cardiac-specific expression and is a possiblecandidate of dilated cardiomyopathy in heart failure. The molecular characteristics and biochemical properties of cvHspare only partially understood. This study was aimed to identify the biological properties and molecular high-order structureof cvHsp. The cvHsp protein was prepared by the refined purification at large amount. The pooled fractions were existedas two types of oligomers in solution and exhibited chaperone-like activity. The circular dichroism analyzed ureainducedunfolding processes. Multiple sequence alignment and an automated protein modeling were used to describe thethree-dimensional structural model of the cvHsp monomer and dimer. By the refined purification, the cvHsp appeared inoligomeric and dimeric forms (approximately 17 kDa and 40 kDa, respectively) composed of 18.6-kDa monomers. ThecvHsp prevented dithiothreitol (DTT)-induced aggregation of the insulin B chain and conferred oligomeric unfoldingprocess in urea-containing solution. It exhibited structural stability and conformed to the two-state folding/unfolding oligomerizationmodel. According to sequence alignment of the rat cvHsp gene, three-dimensional model based on the crystallographicstructure of wheat Hsp16.9 was reconstructed. The cvHsp presented two antiparallel β-sheet sandwich structureof sHsp’ core α-crystallin domain, and formed dimeric or oligomeric organization in solution. This work describedthe structural components of cvHsp and existed as the polydispersed molecular oligomers in vitro, which are some commonproperties of the sHsp family. These characteristics of the cvHsp gene is helpful to clarify molecular functionality incardiac diseases.
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Lin Wei, Yang Zehong, Lu Yongzhi and Zhao Xiaojun, Refined Purification of Large Amounts of Rat cvHsp/HspB7 and Partial Biological Characterization In Vitro, Protein & Peptide Letters 2014; 21 (5) .https://dx.doi.org/10.2174/092986652105140218121109
| DOI https://dx.doi.org/10.2174/092986652105140218121109 | Print ISSN 0929-8665 |
| Publisher Name Bentham Science Publisher | Online ISSN 1875-5305 |
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