Team:Brasil-SP/Project/Cystatin

From 2014.igem.org

(Difference between revisions)
Line 13: Line 13:
<br>
<br>
-
<h3 align="center">Crystallografic Structure of Human Cystatin C - Protein Data Bank 1GAX</h3>
+
<h3 align="center">Crystallografic Structure of Human Cystatin C - Protein Data Bank<a href="http://www.rcsb.org/pdb/explore/explore.do?structureId=3GAX"> 3GAX </a></h3>
<p align="center"><img src="https://static.igem.org/mediawiki/2014/c/c8/Crystal_structure_of_human_cystatin_C.png" width="800" height "auto" </p>
<p align="center"><img src="https://static.igem.org/mediawiki/2014/c/c8/Crystal_structure_of_human_cystatin_C.png" width="800" height "auto" </p>
<br>
<br>

Revision as of 14:52, 17 October 2014

Cystatin C

     Cystatin C (Cys C), an inhibitor of cysteine proteases, has 120 amino acid residues and it is produced by all nucleated cells. It is an excellent biomarker for renal dysfunction, especially for the Chronic Kidney Disease (CDK), due to its constant rate in the blood and its independence of the aforementioned variables (diet, gender, ethnicity, age, muscle mass, and others), varying only with changes in the glomerular filtration rate (GFR). More specifically, Cys C levels rises when GFR descreases and falls when the GFR increases.

     In order to work with a system capable of detecting a inhibitor like Cys C, choose a enzyme that has its activity inhibited specifically by the Cys C, so we could measure the Cys C levels through alteration in the enzyme activity. Several scientific studies have shown that Cystatin C has inhibitory activity against Papain and Cathepsin S illustrated in the table below.

ABRAHAMSON M.,1994

Crystallografic Structure of Human Cystatin C - Protein Data Bank 3GAX


References

ABRAHAMSON M., Cystatins, Meth. Enzymol. 240: 685-700 (1994)