Publication: Structure and expression of a shrimp prohormone convertase 2
2
Issued Date
2012-09-01
Resource Type
ISSN
10956840
00166480
00166480
Other identifier(s)
2-s2.0-84862732915
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Mahidol University
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SCOPUS
Bibliographic Citation
General and Comparative Endocrinology. Vol.178, No.2 (2012), 185-193
Suggested Citation
Amornrat Tangprasittipap, Saisunee Chouwdee, Kornsunee Phiwsaiya, Seansook Laiphrom, Saengchan Senapin, Timothy W. Flegel, Kallaya Sritunyalucksana Structure and expression of a shrimp prohormone convertase 2. General and Comparative Endocrinology. Vol.178, No.2 (2012), 185-193. doi:10.1016/j.ygcen.2012.05.005 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/13619
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Title
Structure and expression of a shrimp prohormone convertase 2
Abstract
Although many crustacean neuroendocrine hormones have been reported, the enzymes responsible for post-translational modification of neuroendocrine hormones have rarely been characterized. A prohormone convertase 2 (PC2)-like enzyme has been isolated from the optic lobe of the giant tiger shrimp, Penaeus monodon and referred as PmPC2. The full length cDNA sequence of PmPC2 has been identified and found to resemble evolutionarily conserved PC2 enzymes of vertebrates and invertebrates. PmPC2 was expressed in all larval developmental stages and in neuroendrocrine cells in the adult optic lobe. Its expression was found to be negatively related with shrimp body weight by qPCR (P < 0.05). Immunohistochemistry results using an anti-rPmPC2 antibody with adult shrimp revealed high staining intensity in specific neurosecretory cells including the sinus gland, the organ of Hanström (also referred to as the medullar terminalis X-organ) and the organ of Bellonci (also referred to as the sensory or X-organ). By using the yeast two hybrid technique, PmPC2 was found to bind with P. monodon hyperglycemic hormone (Pem-CHH1) that plays an important role in glucose metabolism. Since PmPC2 is a subtilisin-like serine proteinase, it is expected to cleave the synthetic substrate, pyr-RTKR-MCA, but the expressed recombinant catalytic domain of PmPC2 (rPmPC2-cat) showed no enzymatic activity as expected. In vivo injection of dsRNA-PmPC2 resulted in reduced transcripts for both PmPC2 and Pem-CHH1 on day 3 post injection, but there was no accompanying reduction of glucose level in the hemolymph. Taken together, PmPC2 localization, expression and activity suggest that it has a function(s) in the shrimp neuroendrocrine system and that it may not only activate Pem-CHH1 but also affect its expression. However, there is no obvious explanation for the negative correlation between PmPC2 expression level and shrimp body weight. © 2012 Elsevier Inc.