Preparation of an active recombinant peptide of crustacean androgenic gland hormone, a heterodimeric glycopeptide.

点击翻译按钮获取中文摘要

The sex differentiation in crustaceans is known to be controlled by a peptide hormone called androgenic gland hormone (AGH). The primary structure of the terrestrial isopod Armadillidium vulgare AGH (Arv-AGH) was finally determined to be a heterodimeric glycoprotein. An N-linked glycan moiety in the mature Arv-AGH was found to be essential for biological activity. Therefore, in this study, a recombinant AGH with a glycan moiety was produced using a baculovirus expression system. Insect Sf9 cells were infected with a recombinant baculovirus expression vector containing an Arv-AGH cDNA insert and subsequently recombinant Arv-AGH was expressed. In Western blot analysis using an anti-Arv-AGH antibody, immunoreactive band of a glycosylated recombinant Arv-AGH was detected.Finally, a cDNA encoding AGH-like peptide (Mar-IAG) was cloned from the giant freshwater prawn Macrobrachium rosenbergii and subsequently a recombinant Mar-IAG with a glycan moiety was expressed by the same methods as recombinant Arv-AGH.