Histamine-releasing reaction induced by the N-terminal domain of Vibrio vulnificus metalloprotease
| Autor: | Masayoshi Hosokawa, Shin Ichi Miyoshi, Koji Kawata, Ken Ichi Tomochika, Sumio Shinoda |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Male
medicine.medical_treatment Vibrio vulnificus Histamine Release General Biochemistry Genetics and Molecular Biology Cell membrane chemistry.chemical_compound Bacterial Proteins In vivo Catalytic Domain medicine Animals Mast Cells Rats Wistar General Pharmacology Toxicology and Pharmaceutics Metalloproteinase Protease Dose-Response Relationship Drug biology Metalloendopeptidases General Medicine biology.organism_classification Mast cell Peptide Fragments Recombinant Proteins In vitro Protein Structure Tertiary Rats Cell biology medicine.anatomical_structure chemistry Biochemistry Peritoneum Histamine |
| Zdroj: | Life Sciences. 72:2235-2242 |
| ISSN: | 0024-3205 |
| DOI: | 10.1016/s0024-3205(03)00094-8 |
| Popis: | A zinc metalloprotease secreted by Vibrio vulnificus, an opportunistic human pathogen causing septicemia and wound infection, stimulates exocytotic histamine release from rat mast cells. This protease consists of two functional domains: the N-terminal domain that catalyzes proteolytic reaction and the C-terminal domain that promotes the association with a protein substrate or cell membrane. Like the intact protease, the N-terminal domain alone also induced histamine release from rat peritoneal mast cells in a dose- and time-dependent manner. However, the reaction induced was apparently weak and went on more slowly. The nickel-substituted protease or its N-terminal domain, each of which has the reduced proteolytic activity due to decreased affinity to a substrate, showed much less histamine-releasing activity. When injected into the rat dorsal skin, the N-terminal domain also evoked enhancement of the hypodermic vascular permeability, while the activity was comparable to that of the protease. Taken together, the protease may stimulate histamine release through the action of the catalytic center of the N-terminal domain on the target substance(s) on the mast cell membrane. The C-terminal domain may support the in vitro action of the N-terminal domain by coordination of the association of the protease with the membrane, but it may not modulate the in vivo action. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect