Ky. Woodfield et al., CDNA CLONING OF RAT MITOCHONDRIAL CYCLOPHILIN, Biochimica et biophysica acta, N. Gene structure and expression, 1351(1-2), 1997, pp. 27-30
Human cyclophilin-3 (hCyp-3) cDNA was used to screen a rat skeletal mu
scle cDNA library which led to the isolation of a full-length cDNA enc
oding the rat homologue. The derived amino acid sequence showed 89.5%
identity with the human sequence, with major differences being restric
ted to the mitochondrial targeting sequence. The N-terminal sequence o
f the purified rat liver mitochondrial cyclophilin (CyP-D) corresponde
d to that derived from the cDNA following 30 amino acids of targeting
sequence. This confirms that hCyp-3 encodes mitochondrial matrix CyP (
CyP-D), which plays a crucial role in the mitochondrial permeability t
ransition. CyP-D mRNA of a single sized (1.5 kb) was shown by Northern
blotting to be present in liver, heart, skeletal muscle and brain. (C
) 1997 Elsevier Science B.V.