Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Application of HSP27 in aspect for improving post-ischemic cardiac systolic function

A technology for heart injury and use, applied in the field of biotechnology or medicine, can solve problems affecting the contraction function of cells

Inactive Publication Date: 2008-02-20
SHANGHAI INST OF BIOLOGICAL SCI CHINESE ACAD OF SCI
View PDF0 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Whether there is a certain relationship between HSP27 and TnI and TnT, and thus affect the contractile function of cells, thereby exerting its cardioprotective effect, has not yet been elucidated.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Application of HSP27 in aspect for improving post-ischemic cardiac systolic function
  • Application of HSP27 in aspect for improving post-ischemic cardiac systolic function
  • Application of HSP27 in aspect for improving post-ischemic cardiac systolic function

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0162] Example 1 Expression of HSP27 in ischemia / reperfusion cardiomyocytes

[0163] In this embodiment, the expression of HSP27 in ischemia / reperfusion cardiomyocytes was determined by Western Blot test.

[0164] The results of Western Blot are shown in Figure 1A and Figure 1B. The results showed that there was no significant difference in the expression of HSP27 total protein at 20 minutes of ischemia, 3 minutes and 30 minutes of reperfusion compared with the balance period, while the expression of phosphorylated protein was significantly different. Significantly increased (P<0.01).

Embodiment 2

[0166] Overexpression of wild-type hsp27 gene can improve the contractility of cardiomyocytes after ischemia / reperfusion

[0167] In order to determine whether HSP27 is related to myocardial contraction, the inventors first detected its effect on contractile function at the level of cardiomyocytes.

[0168] The carriers used in the experiment were divided into the following three groups:

[0169] (1) Transfection of cardiomyocytes with control empty vector AdGFP (i.e. control group (CON));

[0170] (2) AdHSP27wt vector expressing wild-type hsp27 gene; and

[0171] (3) AdHSP27mt vector expressing mutant hsp27 gene.

[0172] The results showed that during the 30-minute reperfusion period after 20 minutes of simulated ischemia, the cell contraction amplitude of the AdGFP group was significantly lower than that before ischemia, while the cell contraction amplitude of the AdHSP27wt group was significantly stronger than that of the control group at the late stage of reperfusion g...

Embodiment 3

[0175] Example 3 Effect of HSP27 on TnI and TnT Degradation Caused by Ischemia / Reperfusion

[0176] In search of the target of HSP27 on myofilament, the inventors found that ischemia / reperfusion injury can cause the degradation of cardiomyocyte TnI and TnT.

[0177] The results of Western Blot showed that in the cells transfected with AdHSP27wt group, the degradation of TnI and TnT small molecular protein was significantly lower than that in the control group (P<0.01); while the degradation degree of TnI and TnT in the cells transfected with AdHSP27mt group was lower than that of the control group. Significantly higher than the control group (P <0.01, Figure 3).

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The present invention pertains to the field of biotechnology and medicine and discloses a usage of Heat Shock Protein 27(HSP27) in the heart protection aspect. The present invention firstly reveals that the HSP27 gene can be applied in the specific myofilament protein for stabilizing ischemia, heart failure and other damages of the heart muscle, so as to improve the contractile function of the heart muscle; the present invention also proves that the HSP27 transfected by the adenovirus vector can improve the contractile function of the heart with ischemia and can provide an effective new target for the treatment of heart diseases.

Description

technical field [0001] The invention belongs to the field of biotechnology or medicine, and more specifically, the invention relates to the use of heat shock protein 27 in heart protection. Background technique [0002] Heart disease is the general term for heart disease, including rheumatic heart disease, congenital heart disease, hypertensive heart disease, coronary heart disease, myocardial disease and other heart diseases. Heart disease is one of the main diseases that endanger human health at present. [0003] Myocardial ischemic disease caused by coronary artery disease is the most common disease and the main cause of death in modern society. Therefore, how to effectively protect the myocardium, improve the resistance of the myocardium to stress injury such as ischemia, and improve cardiac insufficiency after myocardial ischemia are research hotspots in the field of international cardiology. [0004] Heat shock proteins are a group of highly conserved proteins in evo...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/17A61P9/10A61P9/04A61P9/06
Inventor 杨黄恬陆熙园
Owner SHANGHAI INST OF BIOLOGICAL SCI CHINESE ACAD OF SCI
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products