Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology
Gespeichert in:
Verfasser / Beitragende:
[Erick Perera, Leandro Rodríguez-Viera, Rolando Perdomo-Morales, Vivian Montero-Alejo, Francisco Moyano, Gonzalo Martínez-Rodríguez, Juan Mancera]
Ort, Verlag, Jahr:
2015
Enthalten in:
Journal of Comparative Physiology B, 185/1(2015-01-01), 17-35
Format:
Artikel (online)
Online Zugang:
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| 024 | 7 | 0 | |a 10.1007/s00360-014-0851-y |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00360-014-0851-y | ||
| 245 | 0 | 0 | |a Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology |h [Elektronische Daten] |c [Erick Perera, Leandro Rodríguez-Viera, Rolando Perdomo-Morales, Vivian Montero-Alejo, Francisco Moyano, Gonzalo Martínez-Rodríguez, Juan Mancera] |
| 520 | 3 | |a Trypsin enzymes have been studied in a wide variety of animal taxa due to their central role in protein digestion as well as in other important physiological and biotechnological processes. Crustacean trypsins exhibit a high number of isoforms. However, while differences in properties of isoenzymes are known to play important roles in regulating different physiological processes, there is little information on this aspect for decapod trypsins. The aim of this review is to integrate recent findings at the molecular level on trypsin enzymes of the spiny lobster Panulirus argus, into higher levels of organization (biochemical, organism) and to interpret those findings in relation to the feeding ecology of these crustaceans. Trypsin in lobster is a polymorphic enzyme, showing isoforms that differ in their biochemical features and catalytic efficiencies. Molecular studies suggest that polymorphism in lobster trypsins may be non-neutral. Trypsin isoenzymes are differentially regulated by dietary proteins, and it seems that some isoenzymes have undergone adaptive evolution coupled with a divergence in expression rate to increase fitness. This review highlights important but poorly studied issues in crustaceans in general, such as the relation among trypsin polymorphism, phenotypic (digestive) flexibility, digestion efficiency, and feeding ecology. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2014 | ||
| 690 | 7 | |a Digestion biochemistry |2 nationallicence | |
| 690 | 7 | |a Ecological physiology |2 nationallicence | |
| 690 | 7 | |a Panulirus argus |2 nationallicence | |
| 690 | 7 | |a Protein digestion |2 nationallicence | |
| 690 | 7 | |a Trypsin polymorphism |2 nationallicence | |
| 690 | 7 | |a Spiny lobster |2 nationallicence | |
| 700 | 1 | |a Perera |D Erick |u Center for Marine Research, University of Havana, Havana, Cuba |4 aut | |
| 700 | 1 | |a Rodríguez-Viera |D Leandro |u Center for Marine Research, University of Havana, Havana, Cuba |4 aut | |
| 700 | 1 | |a Perdomo-Morales |D Rolando |u Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba |4 aut | |
| 700 | 1 | |a Montero-Alejo |D Vivian |u Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba |4 aut | |
| 700 | 1 | |a Moyano |D Francisco |u Department of Applied Biology, University of Almeria, Almería, Spain |4 aut | |
| 700 | 1 | |a Martínez-Rodríguez |D Gonzalo |u ICMAN-CSIC, Apartado Oficial, 11510, Puerto Real, Cádiz, Spain |4 aut | |
| 700 | 1 | |a Mancera |D Juan |u Department of Biology, Faculty of Marine and Environmental Science, University of Cadiz, Cádiz, Spain |4 aut | |
| 773 | 0 | |t Journal of Comparative Physiology B |d Springer Berlin Heidelberg |g 185/1(2015-01-01), 17-35 |x 0174-1578 |q 185:1<17 |1 2015 |2 185 |o 360 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00360-014-0851-y |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a review-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00360-014-0851-y |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Perera |D Erick |u Center for Marine Research, University of Havana, Havana, Cuba |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Rodríguez-Viera |D Leandro |u Center for Marine Research, University of Havana, Havana, Cuba |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Perdomo-Morales |D Rolando |u Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Montero-Alejo |D Vivian |u Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Moyano |D Francisco |u Department of Applied Biology, University of Almeria, Almería, Spain |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Martínez-Rodríguez |D Gonzalo |u ICMAN-CSIC, Apartado Oficial, 11510, Puerto Real, Cádiz, Spain |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mancera |D Juan |u Department of Biology, Faculty of Marine and Environmental Science, University of Cadiz, Cádiz, Spain |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Journal of Comparative Physiology B |d Springer Berlin Heidelberg |g 185/1(2015-01-01), 17-35 |x 0174-1578 |q 185:1<17 |1 2015 |2 185 |o 360 | ||