Biomaterial Database

Regulated release of multiple peptides from the bag cell neurons of Aplysia californica. 1990

R W Newcomb, and R H Scheller

Department of Biological Sciences, Stanford University, CA 94305.

The bag cell neurons of Aplysia californica synthesize and store large amounts of peptides derived from the egg-laying-hormone (ELH) neuropeptide precursor. Different sets of peptides derived from the amino- and carboxyl-terminal regions of the prohormone possess unique biological activities, and are packaged in distinct sets of secretory granules. We report here quantitative measurements of the amounts of the peptide products stored in and released from the bag cell neurons using high pressure liquid chromatography (HPLC) and amino acid composition analysis. These studies demonstrate that both the autocrine acting bag cell peptides (BCPs) and ELH are released coincident with electrical activity in the bag cell cluster. The composition of the released peptide mixture is similar to that stored in the bag cells. ELH and other carboxy-terminal derived peptides are most often present at 5-fold greater levels than the BCPs. These results provide further insight into the use of multiple chemical messengers by the bag cell neurons.

UI	MeSH Term	Description	Entries
D007447	Invertebrate Hormones	Hormones produced by invertebrates, usually insects, mollusks, annelids, and helminths.	Hormones, Invertebrate
D009474	Neurons	The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.	Nerve Cells,Cell, Nerve,Cells, Nerve,Nerve Cell,Neuron
D011498	Protein Precursors		Precursors, Protein
D011499	Protein Processing, Post-Translational	Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.	Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001048	Aplysia	An opisthobranch mollusk of the order Anaspidea. It is used frequently in studies of nervous system development because of its large identifiable neurons. Aplysiatoxin and its derivatives are not biosynthesized by Aplysia, but acquired by ingestion of Lyngbya (seaweed) species.	Aplysias