Isolation and properties of androgenic gland hormone from the terrestrial isopod, Armadillidium vulgare

Temporal Silencing of an Androgenic Gland-Specific Insulin-Like Gene Affecting Phenotypical Gender Differences and Spermatogenesis

“…Evidence for the importance and evolutionary conservation of insulin-like peptides in the context of sex differentiation is scarce. The small amount of data that is available comes from scattered reports on tissue-specific expression in male sex-differentiating glands in taxa as far removed from each other as Crustacea [AGs (18,21,26)] and Mammalia [Leydig cells (46)]. Moreover, evidence for the necessity of insulin-like peptide receptors for normal development of male mice testis (47) strengthens the notion that insulin-like factors might have a role in sex differentiation, and the results reported in the present study add valuable information in this respect.…”

“…Three insulin-like prothoracicotropic hormones (bombyxin I, II, and III), expressed in the brain of the silkworm Bombyx mori, regulate molt (20). In Crustacea the first AG hormone to be reported was found in isopods; it was assigned to the insulin family of hormones because it possesses B and A chains with a skeleton of conserved cysteine residues, separated by a C peptide that is present in the pro-hormone but undergoes cleavage to contribute to the mature hormone (18,(21)(22)(23)(24)(25). Extensive efforts to discover orthologous genes, through the use of sequence similarity and RT-PCR, in the important group of decapod species have come to nothing.…”

Regulation of hemolymph trehalose level by an insulin-like peptide through diel feeding rhythm of the beet armyworm, Spodoptera exigua

“…Proinsulin processing is not well studied in insects. An isopod invertebrate, A. vulgare, produces an ILP called as an androgenic gland hormone (AGH), which stimulates the immatures to have male sexual characters ('masculinization') [26]. Though AGH is produced in a prohormone containing signal peptide and B-C-A chains, a recombinant protein containing B-C-A chain does not have bioactivity, but it is activated by removing C peptide with a lysyl endopeptidase [40].…”

Endocrine and genetic control of sex differentiation in the Malacostracan Crustacea

“…1975, Katakura and. The AGH of A. vulgare seems to have some monomeric proteins consisting of 157 and 166 amino acid residues, having isoelectric points of about 4.5 and 4.3, respectively (Hasegawa, et al 1987). The primordia are highly sensitive to the AGH in the early stage of postembryonic development.…”