The Protein Journal

, Volume 25, Issue 7, pp 517–528

Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone

Article

DOI: 10.1007/s10930-006-9038-z

Cite this article as:
Takeuchi, S. Protein J (2006) 25: 517. doi:10.1007/s10930-006-9038-z

Abstract

Apoptosis of heart tissues followed by hypoxia and ischemia leads finally to cardiac insufficiency. The full-length coding sequence of 3301 bp including cDNA(s) of the ER chaperone ORP150, which was specifically induced by hypoxia stress, was cloned from human cardiac infarct. Phylogenetic analyses reveal that human heart ORP150 shares a highly conserved N-terminal ATPase domain among its related family members. Moreover, hydropathic profiling reveals that their ca. 70 N-terminal residues and unique C-terminal halves exhibit similar hydropathy profiles among members. These findings suggest that ORP150 is structurally and functionally well conserved in distant species.

Keywords

Hypoxia-ischemiathe ER chaperone ORP150the ATPase domainphylogenyhydropathy

Abbreviations

SHSP

small heat-shock protein

ORP150

150 kDa oxygen-regulated protein

ER

endoplasmic reticulum.

Copyright information

© Springer Science+Business Media, LLC 2006

Authors and Affiliations

  1. 1.Department of Protein ResearchHibergenome (formerly ProstaColon)TakamatsuJapan