| First Author | Colgan JD | Year | 2000 |
| Journal | MGI Direct Data Submission | Mgi Jnum | J:59375 |
| Mgi Id | MGI:1351491 | Citation | Colgan JD, et al. (2000) Isolation and characterization of mouse Ppia, the gene encoding Cyclophilin A. MGI Direct Data Submission |
| abstractText | Cyclophilins are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase and chaperone activities in vitro, suggesting that they regulate protein folding in cells. Cyclophilins also bind with varying affinities to the immuno- suppressive drug cyclosporine. The founding member of the family, Cyclophilin A (CYPA) is a highly abundant, ubiquitously expressed protein whose biological function remains unknown. Here, we describe the isolation and characterization of mouse Ppia, the gene that encodes CYPA. Ppia was isolated from a genomic library using a PCR screen that distinguishes the bonafide gene from multiple pseudogenes present in the mouse genome. Mouse Ppia consists of 5 exons and 4 introns spanning roughly 5kb and maps to chromosome 11 near the centromere. The proximal promoter region of Ppia contains a TATA box as well as sites recognized by several transcriptional regulators. This region was sufficient to drive high levels of reporter gene expression in transfected cells. Both copies of Ppia were disrupted in murine embryonic stem (ES) cells via gene targeting. Ppia -/- ES cells grew normally and could be induced to differentiate into hematopoeitic precursor cells in vitro, indicating that CyPA is not essential for cell viability. |
