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Pregled bibliografske jedinice broj: 865969

Evidence for an angiotensin-converting enzyme (ACE) polymorphism in the crayfish Astacus leptodactylus


Kamech, Nedia; Simunić, Juraj Franklin; Sen, Jeanne; Francis, Sophie; Tabitsika, Maria; Soyez, Daniel
Evidence for an angiotensin-converting enzyme (ACE) polymorphism in the crayfish Astacus leptodactylus // Peptides, 28 (2007), 7; 1368-1374 doi:10.1016/j.peptides.2007.06.009 (međunarodna recenzija, članak, znanstveni)


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Naslov
Evidence for an angiotensin-converting enzyme (ACE) polymorphism in the crayfish Astacus leptodactylus

Autori
Kamech, Nedia ; Simunić, Juraj Franklin ; Sen, Jeanne ; Francis, Sophie ; Tabitsika, Maria ; Soyez, Daniel

Izvornik
Peptides (0196-9781) 28 (2007), 7; 1368-1374

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Angiotensin-converting enzyme ; Zinc-metallopeptidase ; Peptide substrate ; Crustacean ; Crayfish

Sažetak
The present study was initiated to characterize angiotensin- converting enzyme (ACE) in Crustaceans. Using degenerate DNA primers deduced from consensus sequences located upward and downward from the active site of ACEs from different arthropod species, several tissues from the crayfish Astacus leptodactylus were screened by RT-PCR. Amplicons were obtained from hepatopancreas, testis and hemocytes. Analysis of the predicted protein sequences after cloning and Northern blot experiments revealed an original and complex polymorphism of the ACE-like active site. Two variants were obtained in the hepatopancreas, one displaying a 6.4 kb size transcript, probably corresponding to a double domain ACE, with an unusual active site structure while the other had a transcript size of 2.5 kb, close to the size of the transcript obtained in testis and hemocytes (2 and 3 kb, respectively), likely representing single domain enzymes. Functional assays using a synthetic substrate were performed from the different tissues and showed a maximal ACE-like activity associated to membrane fraction from testis and hepatopancreas.

Izvorni jezik
Engleski

Znanstvena područja
Biologija



POVEZANOST RADA


Profili:

Avatar Url Juraj Simunić (autor)

Citiraj ovu publikaciju

Kamech, Nedia; Simunić, Juraj Franklin; Sen, Jeanne; Francis, Sophie; Tabitsika, Maria; Soyez, Daniel
Evidence for an angiotensin-converting enzyme (ACE) polymorphism in the crayfish Astacus leptodactylus // Peptides, 28 (2007), 7; 1368-1374 doi:10.1016/j.peptides.2007.06.009 (međunarodna recenzija, članak, znanstveni)
Kamech, N., Simunić, J., Sen, J., Francis, S., Tabitsika, M. & Soyez, D. (2007) Evidence for an angiotensin-converting enzyme (ACE) polymorphism in the crayfish Astacus leptodactylus. Peptides, 28 (7), 1368-1374 doi:10.1016/j.peptides.2007.06.009.
@article{article, year = {2007}, pages = {1368-1374}, DOI = {10.1016/j.peptides.2007.06.009}, keywords = {Angiotensin-converting enzyme, Zinc-metallopeptidase, Peptide substrate, Crustacean, Crayfish}, journal = {Peptides}, doi = {10.1016/j.peptides.2007.06.009}, volume = {28}, number = {7}, issn = {0196-9781}, title = {Evidence for an angiotensin-converting enzyme (ACE) polymorphism in the crayfish Astacus leptodactylus}, keyword = {Angiotensin-converting enzyme, Zinc-metallopeptidase, Peptide substrate, Crustacean, Crayfish} }
@article{article, year = {2007}, pages = {1368-1374}, DOI = {10.1016/j.peptides.2007.06.009}, keywords = {Angiotensin-converting enzyme, Zinc-metallopeptidase, Peptide substrate, Crustacean, Crayfish}, journal = {Peptides}, doi = {10.1016/j.peptides.2007.06.009}, volume = {28}, number = {7}, issn = {0196-9781}, title = {Evidence for an angiotensin-converting enzyme (ACE) polymorphism in the crayfish Astacus leptodactylus}, keyword = {Angiotensin-converting enzyme, Zinc-metallopeptidase, Peptide substrate, Crustacean, Crayfish} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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