Purification, characterization and developmental expression of chick (Gallus domesticus) liver PSP protein

We have isolated a perchloric acid-soluble protein designated as C-PSP from the post-mitochondria supernatant fraction of chick liver. It is soluble in 5% perchloric acid and purified by ammonium sulfate, fractionation and CM-Sephadex chromatography. The C-PSP showed approximately 70% homology with PSP isolated from rat liver (L-PSP1) with its partial amino acid sequences. The protein has a molecular mass of approximately 14 kDa which was slightly higher than that of L-PSP1. It inhibited protein synthesis in a rabbit reticulocyte lysate system. C-PSP was mainly expressed in liver and kidney and was also expressed in intestine, gizzard, glandular stomach, heart, brain and spleen though its expression was low. The expression of C-PSP in liver increased gradually from the 1st day to the 2nd week and it remained almost the same until the 13th week. C-PSP was also found in day 8 chick embryonic tissues. Interestingly, we found that C-PSP was expressed as a differentiation-dependent manner in the nervous cells of chick embryos. Thus, our findings are the first report on the presence of a PSP in avian tissues which may be involved in the regulation of cellular growth and differentiation.