A chimeric recombinant crustacean hyperglycemic hormone from Litopenaeus schmitti (Burkenroad) obtained as C‐terminus fusion protein boost hemolymph glucose concentration in Litopenaeus vannamei (Boone). Issue 7 (13th March 2012)
- Record Type:
- Journal Article
- Title:
- A chimeric recombinant crustacean hyperglycemic hormone from Litopenaeus schmitti (Burkenroad) obtained as C‐terminus fusion protein boost hemolymph glucose concentration in Litopenaeus vannamei (Boone). Issue 7 (13th March 2012)
- Main Title:
- A chimeric recombinant crustacean hyperglycemic hormone from Litopenaeus schmitti (Burkenroad) obtained as C‐terminus fusion protein boost hemolymph glucose concentration in Litopenaeus vannamei (Boone)
- Authors:
- Morera, Yuliet
Lugo, Juana Maria
Ramos, Laida
Rodríguez‐Ramos, Tania
Huberman, Alberto
Estrada, Mario Pablo - Abstract:
- <abstract abstract-type="main" id="are3110-abs-0001"> <title>Abstract</title> <p>To date, no hormonal treatments are available for control of shrimp reproduction and only eyestalk ablation is of practical use. The crustacean hyperglycemic hormone (CHH) is the most abundant neuropeptide of the eyestalk CHH family. It plays an important role in the regulation of hemolymph glucose levels, as its principal function, but it is also implicated in additional physiological processes such as moulting and reproduction. In the present study, the cDNA encoding <italic>Litopenaeus schmitti</italic> (Burkenroad) mature CHH was cloned into the <italic>Escherichia coli</italic> pTYB2 expression vector. Using this strategy we have obtained, for the first time, the recombinant CHH from <italic>L. schmitti</italic> with its C‐terminus fused to an intein tag. The expected fused protein of about 63 KDa was expressed in <italic>E. coli</italic> forming inclusion bodies. It was purified in a soluble form by electroelution following molecular size fractionation in sodium dodecil sulphate polyacrylamide gel electrophoresis. The ability of the chimeric CHH protein to elevate glucose levels in the hemolymph of the eyestalk‐ablated <italic>Litopenaeus vannamei</italic> (Boone) shrimps indicates that its biological activity as hyperglycemic protein is preserved. The results provide an alternative tool to obtain soluble recombinant proteins from the CHH family of neuropeptides to get a better<abstract abstract-type="main" id="are3110-abs-0001"> <title>Abstract</title> <p>To date, no hormonal treatments are available for control of shrimp reproduction and only eyestalk ablation is of practical use. The crustacean hyperglycemic hormone (CHH) is the most abundant neuropeptide of the eyestalk CHH family. It plays an important role in the regulation of hemolymph glucose levels, as its principal function, but it is also implicated in additional physiological processes such as moulting and reproduction. In the present study, the cDNA encoding <italic>Litopenaeus schmitti</italic> (Burkenroad) mature CHH was cloned into the <italic>Escherichia coli</italic> pTYB2 expression vector. Using this strategy we have obtained, for the first time, the recombinant CHH from <italic>L. schmitti</italic> with its C‐terminus fused to an intein tag. The expected fused protein of about 63 KDa was expressed in <italic>E. coli</italic> forming inclusion bodies. It was purified in a soluble form by electroelution following molecular size fractionation in sodium dodecil sulphate polyacrylamide gel electrophoresis. The ability of the chimeric CHH protein to elevate glucose levels in the hemolymph of the eyestalk‐ablated <italic>Litopenaeus vannamei</italic> (Boone) shrimps indicates that its biological activity as hyperglycemic protein is preserved. The results provide an alternative tool to obtain soluble recombinant proteins from the CHH family of neuropeptides to get a better understanding of shrimp endocrinology.</p> </abstract> … (more)
- Is Part Of:
- Aquaculture research. Volume 44:Issue 7(2013:Jun.)
- Journal:
- Aquaculture research
- Issue:
- Volume 44:Issue 7(2013:Jun.)
- Issue Display:
- Volume 44, Issue 7 (2013)
- Year:
- 2013
- Volume:
- 44
- Issue:
- 7
- Issue Sort Value:
- 2013-0044-0007-0000
- Page Start:
- 1066
- Page End:
- 1075
- Publication Date:
- 2012-03-13
- Subjects:
- Aquaculture -- Periodicals
Fishery management -- Periodicals
639.8 - Journal URLs:
- http://www.blackwellpublishing.com/journal.asp?ref=1355-557X&site=1 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2109 ↗
https://www.hindawi.com/journals/are/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/j.1365-2109.2012.03110.x ↗
- Languages:
- English
- ISSNs:
- 1355-557X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 1581.866120
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3306.xml