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| THE ANTISENSE HOMOLOGY BOX - A NEW MOTIF WITHIN PROTEINS THAT ENCODES BIOLOGICALLY-ACTIVE PEPTIDES |
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| Author(s): BARANYI L, CAMPBELL W, OHSHIMA K, FUJIMOTO S, BOROS M, OKADA H |
| Source: NATURE MEDICINE Volume: 1 Issue: 9 Pages: 894-901 Published: SEP 1995 |
| Times Cited: 74 References: 79 |
| Abstract: Amphiphilic peptides approximately fifteen amino acids in length and their corresponding antisense peptides exist within protein molecules. These regions (termed antisense homology boxes) are separated by approximately fifty amino acids. Because many sense-antisense peptide pairs have been reported to recognize and bind to each other, antisense homology boxes may be involved in folding, chaperoning and oligomer formation of proteins. The antisense homology box-derived peptide CALSVDRYRAVASW, a fragment of human endothelin A receptor, proved to be a specific inhibitor of endothelin peptide (ET-1) in a smooth muscle relaxation assay. The peptide was able to block endotoxin-induced shock in rats as well. Our finding of endothelin receptor inhibitor among antisense homology box-derived peptides indicates that searching proteins for this new motif may be useful in finding biologically active peptides. |
| Document Type: Article |
| Language: English |
Addresses:
1. NAGOYA CITY UNIV, SCH MED, DEPT PHARMACOL, NAGOYA, AICHI 467 JAPAN
2. NOYORI FUKUSHIMURA HOSP, CHOJU MED INST, TOYOHASHI, AICHI 441 JAPAN
3. ALBERT SZENT GYORGYI MED UNIV, INST EXPTL SURG, H-6723 SZEGED, HUNGARY
4. NAGOYA CITY UNIV, SCH MED, DEPT MOLEC BIOL, NAGOYA, AICHI 467 JAPAN |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology; Medicine, Research & Experimental |
| IDS Number: RT303 |
| ISSN: 1078-8956 |
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