CDNA CLONING AND SEQUENCE DETERMINATION OF THE PHEROMONE BIOSYNTHESIS ACTIVATING NEUROPEPTIDE FROM THE SEABUCKTHORN CARPENTERWORM, Holcocerus hippophaecolus (LEPIDOPTERA: COSSIDAE). Issue 4 (29th January 2013)
- Record Type:
- Journal Article
- Title:
- CDNA CLONING AND SEQUENCE DETERMINATION OF THE PHEROMONE BIOSYNTHESIS ACTIVATING NEUROPEPTIDE FROM THE SEABUCKTHORN CARPENTERWORM, Holcocerus hippophaecolus (LEPIDOPTERA: COSSIDAE). Issue 4 (29th January 2013)
- Main Title:
- CDNA CLONING AND SEQUENCE DETERMINATION OF THE PHEROMONE BIOSYNTHESIS ACTIVATING NEUROPEPTIDE FROM THE SEABUCKTHORN CARPENTERWORM, Holcocerus hippophaecolus (LEPIDOPTERA: COSSIDAE)
- Authors:
- Li, Juan
Zhou, Jiao
Sun, Rongbo
Zhang, Haolin
Zong, Shixiang
Luo, Youqing
Sheng, Xia
Weng, Qiang - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>The PBAN (pheromone biosynthesis activating neuropeptide)/pyrokinin peptides comprise a major neuropeptide family characterized by a common FXPRL amide at the C‐terminus</italic>. <italic>These peptides are actively involved in many essential endocrine functions. For the first time, we reported the cDNA cloning and sequence determination of the PBAN from the seabuckthorn carpenterworm, Holcocerus hippophaecolus, by using rapid amplification of cDNA ends. The full‐length cDNA of Hh‐DH‐PBAN contained five peptides: diapause hormone (DH) homolog, α‐neuropeptide (NP), β‐NP, PBAN, and γ‐NP. All of the peptides were amidated at their C‐terminus and shared a conserved motif, FXPR (or K) L. Moreover, Hh‐DH‐PBAN had high homology to the other members of the PBAN peptide family: 56% with Manduca sexta, 66% with Bombyx mori, 77% with Helicoverpa zea, and 47% with Plutella xylostella. Phylogenetic analysis revealed that Hh‐DH‐PBAN was closely related to PBANs from Noctuidae, demonstrated by the relatively higher similarity compared with H. zea. In addition, real‐time quantitative PCR (qRT‐PCR) analysis showed that Hh‐DH‐PBAN mRNA expression peaked in the brain–subesophageal ganglion (Br–SOG) complex, and was also detected at high levels during larval and adult stages. The expression decreased significantly after pupation. These results provided information concerning molecular structure<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>The PBAN (pheromone biosynthesis activating neuropeptide)/pyrokinin peptides comprise a major neuropeptide family characterized by a common FXPRL amide at the C‐terminus</italic>. <italic>These peptides are actively involved in many essential endocrine functions. For the first time, we reported the cDNA cloning and sequence determination of the PBAN from the seabuckthorn carpenterworm, Holcocerus hippophaecolus, by using rapid amplification of cDNA ends. The full‐length cDNA of Hh‐DH‐PBAN contained five peptides: diapause hormone (DH) homolog, α‐neuropeptide (NP), β‐NP, PBAN, and γ‐NP. All of the peptides were amidated at their C‐terminus and shared a conserved motif, FXPR (or K) L. Moreover, Hh‐DH‐PBAN had high homology to the other members of the PBAN peptide family: 56% with Manduca sexta, 66% with Bombyx mori, 77% with Helicoverpa zea, and 47% with Plutella xylostella. Phylogenetic analysis revealed that Hh‐DH‐PBAN was closely related to PBANs from Noctuidae, demonstrated by the relatively higher similarity compared with H. zea. In addition, real‐time quantitative PCR (qRT‐PCR) analysis showed that Hh‐DH‐PBAN mRNA expression peaked in the brain–subesophageal ganglion (Br–SOG) complex, and was also detected at high levels during larval and adult stages. The expression decreased significantly after pupation. These results provided information concerning molecular structure characteristics of Hh‐DH‐PBAN, whose expression profile suggested that the Hh‐DH‐PBAN gene might be correlated with larval development and sex pheromone biosynthesis in females of the H. hippophaecolus</italic>.</p> </abstract> … (more)
- Is Part Of:
- Archives of insect biochemistry and physiology. Volume 82:Issue 4(2013:Apr.)
- Journal:
- Archives of insect biochemistry and physiology
- Issue:
- Volume 82:Issue 4(2013:Apr.)
- Issue Display:
- Volume 82, Issue 4 (2013)
- Year:
- 2013
- Volume:
- 82
- Issue:
- 4
- Issue Sort Value:
- 2013-0082-0004-0000
- Page Start:
- 183
- Page End:
- 195
- Publication Date:
- 2013-01-29
- Subjects:
- Insects -- Physiology -- Periodicals
Insect biochemistry -- Periodicals
595.701572 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1520-6327 ↗
http://www3.interscience.wiley.com/cgi-bin/jhome/109921022 ↗
http://www3.interscience.wiley.com/cgi-bin/jhome/35786 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/arch.21084 ↗
- Languages:
- English
- ISSNs:
- 0739-4462
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 1634.650000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3125.xml