| First Author | Huang S | Year | 1992 |
| Journal | FASEB J | Volume | 6 |
| Issue | 5 | Pages | A1670 (Abstr.) |
| Mgi Jnum | J:671 | Mgi Id | MGI:49206 |
| Citation | Huang S, et al. (1992) Molecular characterization of a 72-KDa human stress protein: A homologue of murine ERp72. FASEB J 6(5):A1670 (Abstr.) |
| abstractText | Full text of Abstract: 4247. MOLECULAR CHARACTERIZATION OF A 72-KDA HUMAN STRESS PROTEIN: A HOMOLOGUE OF MURINE ERp72. S. Huang, C. Gomer, G. Sun, S. Wong, C. Wu, Y. Liu and J. Holcenberg. (SPON: H.J. Forman) Childrens Hospital Los Angeles, Los Angeles, CA 90027. ERP72 is a recently sequenced major endoplasmic reticulum protein isolated from a murine cDNA library [J. Biol. Chem. (1990) 265:1094-1101]. It has a high degree of homology with a set of proteins containing CGHC amino acid fragments. These proteins have been called polypeptide chain binding (PCB) proteins or molecular chaperons and may be involved in mediating optimal folding of other proteins [Cell (1989) 59:591-601]. Recently, we reported that a 2.9 kb human cDNA clone (pA3) encoding a 72 KDa protein has 86% and 89% homology with murine ERp72 at DNA sequence and amino acid sequence levels, respectively [J. Biol. Chem. (1991) 266:5353]. The further characterizations by immunoblotting and RNA blotting analyses indicated that pA3 clone is the human homologue of murine ERp72. The levels of mRNA of our human homologue appear to be controlled in a manner similar to murine ERp72 and other glucose-regulated proteins (GRP) when exposed to glycosylation inhibitors and calcium ionophore. Northern blotting analysis indicated that, after 16-h treatments, glucosamine (10 mM) and A23187 (10 uM) significantly enhanced the steady state level of pA3 mRNA. Increased ERp72 mRNA expression was also observed in cells treated with porphyrin photosensitization which induces oxidative stress. Hyperthermia treatments, which enhance expression of HSP70 mRNA, do not cause any increase in mRNA levels of the human ERp72. These data indicate that human ERp72 is a glucose- regulated protein without heat-inducible expression. |
