Medical application of CREG1 protein in prevention or treatment of sorafenib-induced myocardial injury
What is Al technical title?
Al technical title is built by PatSnap Al team. It summarizes the technical point description of the patent document.
A myocardial injury, protein technology, applied in the medical use of myocardial injury and related diseases, CREG1 protein or its active fragment field
Pending Publication Date: 2021-06-08
GENERAL HOSPITAL OF THE NORTHERN WAR ZONE OF THE CHINESE PEOPLES LIBERATION ARMY
View PDF3 Cites 1 Cited by
Summary
Abstract
Description
Claims
Application Information
AI Technical Summary
This helps you quickly interpret patents by identifying the three key elements:
Problems solved by technology
Method used
Benefits of technology
Problems solved by technology
However, whether CREG1 regulates sorafenib-induced myocardial injury has not been reported so far
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
Click on the blue label to locate the original text in one second.
Reading with bidirectional positioning of images and text.
Smart Image
Examples
Experimental program
Comparison scheme
Effect test
Embodiment 2
[0046] Example 2 Sarafini intervention induces cardiac tissue and cellular procedural death.
[0047] 1. Western blot Detects myocardial tissue procedural death protein expression.
[0048] Western blot method detection procedural death marker protein RIP3 and P-RIP3 expression. The protein concentration was measured by the RIPA lysate to extract the control group and the Solafini intervention group, and the protein concentration was determined using a BCA colorimetric kit. The expression of CREG protein was detected with Western Blot.
[0049] Specifically, the 40 μg of protein was boiled at 95 ° C for 5 min, and the hydraulic SDS-PAGE electrophoresis was separated by 10%, and the electrophoresis ended time. Samples were transferred to the cellulose membrane at 90V, and the time was 2 h; after normal temperature was closed for 2 hours in TBS-T dilution, it was added to incubate overnight at 4 ° C. The anti-RIP3 antibody (1: 1000, US ABCAM), anti-P-RIP3 antibody (1: 1000, US ABCAM...
Embodiment 3
[0058] Example 3 The expression of CREG1 in myocardial tissue in Sarafini decreased.
[0059] 1. Fluorescence Quantitative PCR Method Detects the expression of Creg1 gene mRNA in the front of the myocardial tissue before Sarafini.
[0060] The tissue RNA was extracted with a Promega kit and a TAKARA reverse transcription kit was used to obtain a reverse transcription reaction to obtain cDNA, followed by a quantitative PCR reaction with a Sybgreen method. Quantitative PCR primer sequences are as follows:
[0061]
[0062] The results showed that there was no significant change in the expression level of CREG gene mRNA in Sarafini group compared to the control group. Figure 2A Indicated.
[0063] 2, Western blot to detect the expression of CREG protein in myocardial tissue.
[0064] In order to detect the expression of CREG in myocardial tissue induced by Sarafini, CREG protein expression was detected by WesternBlot. Specific methods are shown in Example 1. The anti-CREG antibody ...
Embodiment 4
[0066]Example 4 Exogenous administration CREG recombinant protein significantly reduced C57BL / 6J mouse heart functional damage in Sarafini intervention.
[0067] 1. Exogenous CREG protein intervention is administered on the model of Sarafini-induced heart function injury.
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
Login to view more
Abstract
The invention relates to a medical application of E1A activated gene repressor protein, in particular to a medical application of CREG1 protein or an active fragment thereof in prevention and/or treatment of sorafenib-induced myocardial injury and related diseases. Experiments prove that sorafenib intervention causes decline of the heart function of a wild type C57BL/6J mouse, meanwhile, the expression of mRNA and protein of CREG1 gene in myocardial tissue are remarkably reduced, and myocardial injury markers are remarkably increased. Exogenous administration of CREG1 recombinant protein can significantly reduce sorafenib-induced myocardial injury and cardiac dysfunction. The expression of the sorafenib-induced mouse myocardial cell programmed necrosis marker protein is obviously increased, and the death mode is programmed necrosis; exogenous administration of CREG1 recombinant protein can significantly inhibit the occurrence of programmed myocardial cell death induced by sorafenib, and the cardiac function is improved. The CREG1 recombinant protein can be used for preventing or treating myocardial injury and related diseases caused by sorafenib.
Description
Technical field [0001] The present invention relates to medical use of E1A activation gene repuggestions (CREG1) protein, which specifically involves CREG1 proteins or active fragments for preventing and / or treating Sarafini-induced myocardial injury and related diseases. Medical use. Background technique [0002] With the rapid development of clinical tumors therapy, the survival rate and the quality of survival in tumor patients have been greatly improved. However, heart toxicity caused by anti-tumor drugs also exists and cannot be ignored. In August 2016, the European Heart Society (ESC) released the first "2016esc cancer treatment and cardiovascular scientific statement" related to clinical practice, cardiovascular complications related to tumor treatment, such as myocardial function and heart failure , Coronary disease, cardiac valve disease, arrhythmia, high blood pressure, thromboembrays, surrounding vascular diseases and stroke, pulmonary hypertension and cardiac compli...
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
Application Date:The date an application was filed.
Publication Date:The date a patent or application was officially published.
First Publication Date:The earliest publication date of a patent with the same application number.
Issue Date:Publication date of the patent grant document.
PCT Entry Date:The Entry date of PCT National Phase.
Estimated Expiry Date:The statutory expiry date of a patent right according to the Patent Law, and it is the longest term of protection that the patent right can achieve without the termination of the patent right due to other reasons(Term extension factor has been taken into account ).
Invalid Date:Actual expiry date is based on effective date or publication date of legal transaction data of invalid patent.
Login to view more 
Login to view more