CN113820485A - Urine carbonic anhydrase 3 and application of polypeptide fragment thereof in burn - Google Patents
Urine carbonic anhydrase 3 and application of polypeptide fragment thereof in burn Download PDFInfo
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Abstract
本发明提供一种尿液碳酸酐酶3（Carbonic anhydrase 3）及其多肽片段的应用，具体为尿液碳酸酐酶3及其多肽片段在制备用于烧伤诊断、鉴别诊断、烧伤面积及程度评价、治疗效果评价、监测、预后评估及机理研究等制剂的应用。烧伤是日常生活中常见的重要创伤，每年每100万人中约有5000～100000人烧伤，据世界卫生组织统计，每年全球死于烧伤患者超过30万人，严重烧伤救治存活率仍处于较低水平。本发明通过研究证实，与健康人（正常对照组）相比，尿液碳酸酐酶3及其多肽片段在烧伤患者中表达升高。可用于烧伤患者的各种目的应用检测。本发明发挥尿液标本获取无创、可大规模重复取样、保存方便的优势，利用尿液标本检测尿液碳酸酐酶3及其多肽片段。
The invention provides the application of urine carbonic anhydrase 3 (Carbonic anhydrase 3) and its polypeptide fragments, in particular to the preparation of urine carbonic anhydrase 3 and its polypeptide fragments for burn diagnosis, differential diagnosis, burn area and degree evaluation , therapeutic effect evaluation, monitoring, prognostic evaluation and mechanism research and other preparations. Burns are a common and important trauma in daily life. About 5,000 to 100,000 people are burned every year per 1 million people. According to the statistics of the World Health Organization, more than 300,000 people die from burns in the world every year, and the survival rate of severe burns is still low. Level. The present invention confirms through research that compared with healthy people (normal control group), the expression of urinary carbonic anhydrase 3 and its polypeptide fragments is increased in burn patients. Can be used for various purpose application detection in burn patients. The invention utilizes the advantages of non-invasive acquisition of urine samples, large-scale repeated sampling and convenient storage, and utilizes the urine samples to detect urine carbonic anhydrase 3 and its polypeptide fragments.
Description
Technical Field
The invention relates to new application of urine carbonic anhydrase 3 and polypeptide fragments thereof, in particular to application of the urine carbonic anhydrase 3 and the polypeptide fragments thereof in burn diagnosis, differential diagnosis, burn area and degree evaluation, treatment effect evaluation, monitoring, prognosis evaluation, mechanism research and the like.
Background
Burn refers to the injury of skin, tissue and even deep viscera of human body caused by chemical substances such as flame, high-temperature gas, scorching solid or liquid, radioactive rays, electric energy, strong acid and strong alkali, etc., and is a systemic comprehensive disease. After burn, a large amount of reactions such as necrosis, infection, shock, blood coagulation dysfunction and the like of wound tissues can cause a series of pathophysiological changes of organisms. Burns of different degrees have different influences on human bodies, serious burns can damage the environment in the human bodies, the burn patients have pathophysiological changes of complexity of various systems, and relevant detection indexes can correspondingly change along with the difference of the severity of the burns. Timely detection of changes in these indices can provide valuable reference for clinicians in many areas, such as disease diagnosis, disease judgment, treatment selection, and patient prognosis assessment.
However, patients with severe burns have poor skin integrity, and clinical use of hematological tests as invasive tests on the skin in such patients has presented difficulties, and repeated blood draw tests can also exacerbate patient pain. Urine as ultrafiltrate of blood contains abundant biological information, and the collection process has the advantages of non-invasive and convenient operation, and the like, which is particularly obvious in the detection of burn patients. The biomarker which is helpful for burn diagnosis and reflects disease change is searched in urine, so that the life quality and compliance of burn patients can be improved, the pain of blood collection for many times is relieved, and a reference basis which is favorable for disease diagnosis and treatment is better provided for clinicians.
Carbonic anhydrase 3 (CA 3) is abundantly expressed in human skeletal muscle and liver tissue, and can protect cells from oxidative stress. Carbonic anhydrase is a ubiquitous zinc-containing metalloprotease and also a pH-regulating protein, of which CA3 is a more important member of the family. In some studies, two cysteine residues on the surface of CA3 in liver cells are rapidly combined to form S-glutathione under the oxidative stress state; exposure to H２O２The level of Reactive Oxygen Species (ROS) was significantly reduced in comparison to untransfected group after transfection of CA3, suggesting that CA3 may have antioxidant stress effects. In the study, carbonic anhydrase 3 in the urine of the burn patients is up-regulated in expression compared with that of healthy peopleThe protein content increases.
Compared with the common clinical blood sample, the urine can be collected in a non-invasive, continuous and large amount; without homeostatic regulation, more various and larger changes can be accumulated, and many pathophysiological changes of the body can be reflected in urine. Some protein polypeptides with relatively small molecular weight, such as hormones and cytokines, are excreted into urine quickly after entering blood, and the probability that the proteins and polypeptides are detected in urine is much higher than that in blood; before urine is collected, a possible protein degradation process in urine is completed, so that urine protein can be kept stable for a longer time. In order to relieve the pain of multiple blood sampling of burn patients, the experiment is expected to realize the diagnosis and disease monitoring of the burn patients by painless, convenient, quick and easily repeated urine detection through the research of urine protein or polypeptide on the basis of the methodology exploration of the early stage, and also lays a foundation for the further research of the urine polypeptide detection kit.
Disclosure of Invention
The invention aims to provide application of urine carbonic anhydrase 3 and polypeptide fragments thereof in preparation of preparations for burn diagnosis, differential diagnosis, burn area and degree evaluation, treatment effect evaluation, monitoring, prognosis evaluation, mechanism research and the like.
Preferably, the amino acid sequence of the urine carbonic anhydrase 3 is as shown in SEQ ID No.1 (MAKEWGYASH NGPDHWHELF PNAKGENQSP VELHTKDIRH DPSLQPWSVS YDGGSAKTIL NNGKTCRVVF DDTYDRSMLR GGPLPGPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL VHWNPKYNTF KEALKQRDGI AVIGIFLKIG HENGEFQIFL DALDKIKTKG KEAPFTKFDP SCLFPACRDY WTYQGSFTTP PCEECIVWLL LKEPMTVSSD QMAKLRSLLS SAENEPPVPL VSNWRPPQPI NNRVVRASFK); or an amino acid sequence which is derived from the amino acid sequence shown in SEQ ID NO.1 and has the same function with the amino acid sequence shown in SEQ ID NO. 1.
Preferably, the preparation is a detection kit for the carbonic anhydrase 3 in urine of burn patients and polypeptide fragments thereof.
Preferably, the kit comprises an immunological method of antigen-antibody reaction and kits thereof such as one or more of an aptamer antibody or antibody fragment capable of specifically binding to carbonic anhydrase 3 and polypeptide fragments thereof.
Preferably, the detection method comprises methods such as mass spectrometry for directly detecting carbonic anhydrase 3 and polypeptide fragments thereof and related kits thereof.
Preferably, the detection method comprises related nucleic acid detection methods for directly detecting carbonic anhydrase 3 and polypeptide fragments thereof and related kits.
Preferably, the kit further comprises a component selected from the group consisting of: the kit comprises a solid phase carrier, a diluent, a reference substance, a standard substance, a quality control substance, a detection antibody, a second antibody diluent, a luminescent reagent, a washing solution, a color development solution and a stop solution, wherein the solid phase carrier is any one or a combination of a plurality of the solid phase carrier, the diluent, the reference substance, the standard substance, the quality control substance, the detection antibody, the second antibody and the second antibody diluent.
Preferably, the standard comprises a carbonic anhydrase 3 standard, a humanized tag antibody standard; preferably, the quality control product comprises: carbonic anhydrase 3 quality control products and humanized label antibody quality control products; preferably, the solid support comprises: particles, microspheres, glass slides, test strips, plastic beads, liquid phase chips, micro-porous plates or affinity membranes and other carriers with the same functions.
Preferably, the solid phase carrier is made of any one of polyvinyl chloride, polystyrene, polyacrylamide and cellulose, and has similar functions.
The inventor firstly collects urine samples of healthy people and burn patients, centrifugates for 5min at 4000r/min, absorbs supernatant, measures the concentration of extracted protein by a Bradford method, and carries out SDS-PAGE enzymolysis. The Label-free mass spectrometry of the urine samples was performed by the OrbitrapFasion type mass spectrometer. And performing quantitative calculation on data obtained in the mass spectrum of the burn group and the normal control group. The differential polypeptide is screened by using the difference of protein expression amount more than 1.5 times and P <0.05 as a reference standard through statistical test. Then the inventor identifies the differential polypeptide with statistical significance, and utilizes a database to search to obtain the differential protein carbonic anhydrase 3.
The research proves that compared with healthy people, the carbonic anhydrase 3 and the polypeptide fragment thereof are highly expressed in urine of burn patients and have better consistency with clinical diagnosis. Therefore, the urine carbonic anhydrase 3 and the polypeptide fragment thereof can be used for auxiliary diagnosis or disease condition monitoring of the burn.
The invention exerts the advantages of noninvasive acquisition, large-scale repeated sampling and convenient preservation of the urine specimen, and utilizes the urine specimen to detect the urine carbonic anhydrase 3 and the polypeptide fragment thereof.
In order to make the aforementioned and other objects, features and advantages of the present invention comprehensible, preferred embodiments accompanied with figures are described in detail below.
Drawings
FIG. 1 is a graph showing the content of urine carbonic anhydrase 3 and its polypeptide fragments in burn group and healthy control group.
FIG. 2 is a schematic diagram showing the involvement of carbonic anhydrase 3 in major biological processes.
Detailed Description
Example 1Collection and processing of urine specimens
Burn patients were selected as the burn group, and contemporary physical examiners were selected as the normal control group. 30ml samples of fresh morning urine were collected from each group of subjects after admission, and those who failed to urinate normally collected their morning urine from their catheters and placed in dry, clean containers. Centrifuging the collected urine specimen at 4000r/min for 5min, sucking supernatant, subpackaging 2ml per tube, and storing in a refrigerator at-80 ℃.
Example 2Mass spectrometry and screening of urine polypeptides
Extracting protein from urine sample, and determining the concentration of extracted protein. Mass spectrometry of urine samples was performed by orbitrapfuision type mass spectrometry. And performing quantitative calculation on data obtained in the mass spectrum of the experimental group and the normal control group. The comparison among groups adopts t-test to carry out differential analysis, and differential expression proteins are screened by using the difference of protein expression quantity more than 1.5 times and taking the statistical test that P <0.05 as a reference standard.
Example 3Identification and analysis of differential Polypeptides
The used database is a Unit _ Homo database, the generated mass spectrum original file is processed by MaxQuant software, and the retrieval parameter setting is shown in Table 1.
Compared with healthy people, carbonic anhydrase 3 is highly expressed in urine of burn patients as shown in fig. 1, the main biological processes involved in the same are shown in fig. 2, and the expression of carbonic anhydrase 3 in urine of normal control groups and burn groups is significantly different.
Although the present invention has been described with respect to the preferred embodiments, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the invention as defined by the appended claims.
Sequence listing
<110> Zhang Man
<120> urine carbonic anhydrase 3 and application of polypeptide fragment thereof in burn
<130> 1
<140> 20PCA3
<141> 2020-05-10
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 260
<212> PRT
<213> Human Urine
<400> 1
Met Ala Lys Glu Trp Gly Tyr Ala Ser His Asn Gly Pro Asp His Trp
1 5 10 15
His Glu Leu Phe Pro Asn Ala Lys Gly Glu Asn Gln Ser Pro Val Glu
20 25 30
Leu His Thr Lys Asp Ile Arg His Asp Pro Ser Leu Gln Pro Trp Ser
35 40 45
Val Ser Tyr Asp Gly Gly Ser Ala Lys Thr Ile Leu Asn Asn Gly Lys
50 55 60
Thr Cys Arg Val Val Phe Asp Asp Thr Tyr Asp Arg Ser Met Leu Arg
65 70 75 80
Gly Gly Pro Leu Pro Gly Pro Tyr Arg Leu Arg Gln Phe His Leu His
85 90 95
Trp Gly Ser Ser Asp Asp His Gly Ser Glu His Thr Val Asp Gly Val
100 105 110
Lys Tyr Ala Ala Glu Leu His Leu Val His Trp Asn Pro Lys Tyr Asn
115 120 125
Thr Phe Lys Glu Ala Leu Lys Gln Arg Asp Gly Ile Ala Val Ile Gly
130 135 140
Ile Phe Leu Lys Ile Gly His Glu Asn Gly Glu Phe Gln Ile Phe Leu
145 150 155 160
Asp Ala Leu Asp Lys Ile Lys Thr Lys Gly Lys Glu Ala Pro Phe Thr
165 170 175
Lys Phe Asp Pro Ser Cys Leu Phe Pro Ala Cys Arg Asp Tyr Trp Thr
180 185 190
Tyr Gln Gly Ser Phe Thr Thr Pro Pro Cys Glu Glu Cys Ile Val Trp
195 200 205
Leu Leu Leu Lys Glu Pro Met Thr Val Ser Ser Asp Gln Met Ala Lys
210 215 220
Leu Arg Ser Leu Leu Ser Ser Ala Glu Asn Glu Pro Pro Val Pro Leu
225 230 235 240
Val Ser Asn Trp Arg Pro Pro Gln Pro Ile Asn Asn Arg Val Val Arg
245 250 255
Ala Ser Phe Lys
260
Claims (9)
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Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2011002292A1 (en) * | 2009-07-01 | 2011-01-06 | Brainlabs B.V. | Novel diagnostic method for diagnosing depression |
| CN105497014A (en) * | 2010-12-23 | 2016-04-20 | 阿马曾提斯公司 | Compositions and methods for improving mitochondrial functions |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2011002292A1 (en) * | 2009-07-01 | 2011-01-06 | Brainlabs B.V. | Novel diagnostic method for diagnosing depression |
| CN105497014A (en) * | 2010-12-23 | 2016-04-20 | 阿马曾提斯公司 | Compositions and methods for improving mitochondrial functions |
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