Two peptide transmitters co-packaged in a single neurosecretory vesicle.
Numerous neurosecretory cells are known to secrete more than one peptide, in both vertebrates and invertebrates. These co-expressed neuropeptides often originate from differential cleavage of a single large precursor, and are then usually sorted in the regulated pathway into different secretory vesicle classes to allow separable release dynamics. Here, we use immuno-gold electron microscopy to show that two very different neuropeptides (the nonapeptide crustacean cardioactive peptide (CCAP) and the 30 kDa heterodimeric bursicon) are co-packaged within the same dense core vesicles in neurosecretory neurons in the abdominal ganglia of Periplaneta americana. We suggest that this co-packaging serves a physiological function in which CCAP accelerates the distribution of bursicon to the epidermis after ecdysis to regulate sclerotization of the newly formed cuticle.
Woodruff
Elvin A
EA
Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235, USA.
Broadie
Kendal
K
Honegger
Hans-Willi
HW
D000818:Animals; D017952:Ganglia, Invertebrate / Q000378:metabolism* / Q000648:ultrastructure; D007447:Invertebrate Hormones / Q000378:metabolism*; D007814:Larva / Q000378:metabolism / Q000648:ultrastructure; D016253:Microscopy, Immunoelectron; D009474:Neurons / Q000378:metabolism / Q000648:ultrastructure; D009479:Neuropeptides / Q000378:metabolism*; D010526:Periplaneta / Q000378:metabolism* / Q000648:ultrastructure; D022142:Secretory Vesicles / Q000378:metabolism* / Q000648:ultrastructure
D007447:Invertebrate Hormones; D009479:Neuropeptides; C058620:crustacean cardioactive peptide; C002295:bursicon