Neuropeptide precursor processing detected by triple immunolabeling
dc.contributor.author | McCormick, John P. | en_US |
dc.contributor.author | Nichols, Ruthann | en_US |
dc.contributor.author | Lim, I. A. | en_US |
dc.date.accessioned | 2006-09-08T20:09:28Z | |
dc.date.available | 2006-09-08T20:09:28Z | |
dc.date.issued | 1999-07 | en_US |
dc.identifier.citation | McCormick, J.; Lim, I.; Nichols, R.; (1999). "Neuropeptide precursor processing detected by triple immunolabeling." Cell & Tissue Research 297(2): 197-202. <http://hdl.handle.net/2027.42/42272> | en_US |
dc.identifier.issn | 0302-766X | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/42272 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=10470489&dopt=citation | en_US |
dc.description.abstract | Peptides that play critical physiological roles are often encoded in precursors that contain several gene products. Differential processing of a polypeptide precursor by cell-specific proteolytic enzymes can yield multiple messengers with diverse distributions and functions. We have isolated SDNFMRFamide, DPKQDFMRFamide, and TPAEDFMRFamide from Drosophila melanogaster . The peptides are encoded in the FMRFamide gene and have a common C-terminal FMRFamide but different N-terminal extensions. In order to investigate the regulation of expression of FMRFamide peptides, we generated antisera to distinguish between the structurally related neuropeptides. We established a triple-label immunofluorescence protocol using antisera raised in the same host species and mapped the neural distribution of SDNFMRFamide, DPKQDFMRFamide, and TPAEDFMRFamide. Each peptide has a unique, nonoverlapping cellular expression pattern, suggesting that the precursor is differentially processed. Thus, our data indicate that D. melanogaster contains cell-specific proteolytic enzymes to cleave a polypeptide protein precursor, resulting in unique expression patterns of neuropeptides. | en_US |
dc.format.extent | 315033 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Springer-Verlag; Springer-Verlag Berlin Heidelberg | en_US |
dc.subject.other | Neuropeptide | en_US |
dc.subject.other | Precursor Processing | en_US |
dc.subject.other | Proteolytic Enzymes | en_US |
dc.subject.other | Legacy | en_US |
dc.subject.other | Key Words FMRFamide | en_US |
dc.subject.other | Drosophila Melanogaster (Insecta) | en_US |
dc.title | Neuropeptide precursor processing detected by triple immunolabeling | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Undergraduate Honors Program, University of Michigan, 830 N. University Ave., Ann Arbor, MI 48109–1048, USA, US | en_US |
dc.contributor.affiliationum | Undergraduate Honors Program, University of Michigan, 830 N. University Ave., Ann Arbor, MI 48109–1048, USA, US | en_US |
dc.contributor.affiliationum | Biology Department, University of Michigan, 830 N. University Ave., Ann Arbor, MI 48109–1048, USA, US | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 10470489 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/42272/1/441-297-2-197_92970197.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/s004410051347 | en_US |
dc.identifier.source | Cell & Tissue Research | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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