The aim of this study was to have in-depth knowledge of CypA in this commercially important species.
vannamei CypA (LvCypA) with other known sequences was done using Blast programs (www.ncbi.nim.nih.gov/).
Using Clustal X software, the LvCypA deduced amino acid sequence was compared with other known sequences of CypA available in GenBank database.
The sequence has the similar characters for basic structural function of Cyclophilin A, the cyclophilin type peptidyl-prolylcis-trans isomerases signature and conserved amino acid residues are similar with already investigated CypA in different species (Howard et al., 2003; Piotukh et al., 2005; Eisenmesser et al., 2002; Qiu et al., 2009; Chen et al., 2011).
presumed that the enzymatic activity of CyPA is required for CD147-mediated signalling on the basis of the experiments with mutants of CyPA without PPIase activity .
In addition, CD147 deficiency, CyPA deficiency, or anti-CD147 monoclonal antibody was found to substantially reduce the infarct size at 24 hours and 7 days in acute myocardial infarction after ischemia/reperfusion .
Among the members of the CyPs family, CyPA was first demonstrated to be overexpressed in tumours, such as pancreatic cancer and breast cancer .
In 2009, Dear and his colleagues  demonstrated in cecal ligation and puncture (CLP) induced organ dysfunction by difference in-gel electrophoresis (DIGE) that cyclophilins including CyPA increased in abundance after CLP and sepsis-induced renal dysfunction was significantly attenuated after CD147, the receptor for CyPA, was inhibited by anti-CD147 antibody intraperitoneally.
The research on synovial macrophages of rheumatoid arthritis patients observed that CyPA and CD147 expression were detected and stimulation of CD147 induced the production of MMP-9 and proinflammatory cytokines and promoted cell migration in macrophages.
As for CyPA, it participates in inflammatory response, and, thus, it might be associated with LN.
CsA is also known to exert effects through mechanisms independent of inhibition of PPIase activity of CypA
. The CsA-CypA complex inhibits the signaling pathways involved in immune functions that lead to gene transcription by blocking the highly conserved [Ca.sup.2+]/calmodulin (CaM)-dependent serine/threonine protein phosphatase activity of calcineurin (also known as protein phosphatase 2B).