Does the N-terminal pyroglutamate residue have any physiological significance for crab hyperglycemic neuropeptides?
A characteristic feature of all crustacean hyperglycemic hormones (CHH) is that they are always present in the sinus gland as multiple forms or isoforms. The amino acid sequence of the minor form of CHH from the green shore crab, Carcinus maenas, was determined by automated microsequencing and MS, and was almost identical to that of the major form, except that the N-terminal residue was glutamine rather than pyroglutamate. Limited analysis (electrospray MS and amino acid composition) of the two corresponding forms of CHH from the edible crab, Cancer pagurus, suggested a similar phenomenon in this species. For C. maenas, both forms were indistinguishable in terms of their ability to cause sustained hyperglycemia in vivo and repression of ecdysteroid synthesis in vitro. Similarly, the two forms were immunologically identical in RIA, and exhibited similar binding characteristics in competitive-receptor-binding assays. CD studies showed only minor differences in presumed secondary structur
