Cysteine proteinases substitute for serine proteinases in the midgut glands of Crangon crangon and Crangon allmani (Decapoda: Caridea)
| Autor: | Reinhard Saborowski, Mathias Teschke |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
0106 biological sciences
ved/biology.organism_classification_rank.species Crangon E-64 Aquatic Science 01 natural sciences Serine 03 medical and health sciences chemistry.chemical_compound AEBSF medicine 14. Life underwater Ecology Evolution Behavior and Systematics 030304 developmental biology 0303 health sciences biology ved/biology 010604 marine biology & hydrobiology Crangon crangon Cancer pagurus biology.organism_classification Trypsin chemistry Biochemistry medicine.drug Crangon allmani |
| Zdroj: | EPIC3Journal of experimental marine biology and ecology, 316(2), pp. 213-229, ISSN: 0022-0981 |
| Popis: | The utilization of dietary proteins in crustaceans is facilitated by a set of peptide hydrolases which are often dominated by “trypsin-like” serine proteinases. As expected, the North Sea shrimps Crangon crangon and Crangon allmani showed in their midgut glands high proteolytic activities. However, the majority of animals lacked trypsin and chymotrypsin. Conversely, a minority of about 10% of the animals had elevated trypsin activities. The appearance of trypsin was neither related to the mode of feeding nor to the nutritive state of the animals. When present, trypsin was expressed in both species as a single isoform of apparently 20 kDa. The lack of serine proteinases was also confirmed by inhibitor assays. AEBSF, a serine proteinase inhibitor, slightly reduced total proteinase activity by less than 10%. In contrast E 64, a cysteine proteinase inhibitor, caused a reduction of more than 70% of total proteinase activity, indicating that a substantial share of proteolytic activity is caused by cysteine proteinases. Cathepsin L-like proteinases were identified as major cysteine proteinases. A comparison with the eucarid crustaceans Pandalus montagui , Pagurus bernhardus , Cancer pagurus and Euphausia superba showed a similar high level of total proteinase activity in all species. Trypsin, however, varied significantly between species showing lowest activities in Caridea and the highest activity in E. superba . E 64 suppressed total proteinase activity by more than 70% in Crangon species but not in C. pagurus and E. superba . In contrast, the serine proteinase inhibitor AEBSF had only little effect in Caridea but was most effective in P. bernhardus , C. pagurus and E. superba . The results may indicate different traits of food utilization strategies in some eucarid crustaceans. Caridea may express predominantly cysteine proteinase, while in Anomura, Brachyura and Euphausiacea, serine proteinases may prevail. |
| Databáze: | OpenAIRE |
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