Rat hemopexin. Molecular cloning, primary structural characterization, and analysis of gene expression. Academic Article uri icon

abstract

  • A full-length hemopexin cDNA was isolated from a rat liver cDNA library and the derived amino acid sequence was obtained. Rat hemopexin shows a 76% amino acid homology with human hemopexin. The amino-terminal domain of rat hemopexin contains two histidine residues that are conserved in the human and rat sequences and are the most likely heme axial ligands. Analogous to human hemopexin, the rat hemopexin consists of 10 internal repeating peptide motifs characteristic of the pexin gene family. A complete conservation of cysteine residues is seen between the human and rat sequences suggesting an identical disulfide bridge structure in both proteins. Our analysis of the primary structure of rat hemopexin reveals characteristics typical for members of the pexin gene family and suggests a conserved evolutionary role for the C-terminal (non-heme-binding) domain of this protein. The full-length rat hemopexin cDNA was used to analyze changes in hemopexin gene expression during development and experimental inflammation. RNA blot analysis showed a single 2.0-kb hemopexin mRNA present in fetal liver at day 14. Hemopexin-specific mRNA was not detected in embryonic or fetal tissues at earlier stages of development and was confined to the liver throughout fetal, newborn, and adult life. The abundance of hemopexin mRNA was found to increase throughout gestation, with a sharp increase in the first postnatal weeks, reaching maximum levels in adult animals. Endotoxin-induced inflammation resulted in a 5-fold increase in hepatic hemopexin mRNA content within 48 h without associated changes in hemopexin transcript size. Adult animals exposed to hyperoxia (95% oxygen) showed a 3-fold increase in hepatic hemopexin mRNA content.(ABSTRACT TRUNCATED AT 250 WORDS)

publication date

  • January 22, 1991