Synthetic peptides of the effector-binding domain of rab enhance secretion from digitonin-permeabilized chromaffin cells
dc.contributor.author | Senyshyn, Jan | en_US |
dc.contributor.author | Balch, William E. | en_US |
dc.contributor.author | Holz, Ronald W. | en_US |
dc.date.accessioned | 2006-04-10T15:06:57Z | |
dc.date.available | 2006-04-10T15:06:57Z | |
dc.date.issued | 1992-08-31 | en_US |
dc.identifier.citation | Senyshyn, Jan, Balch, William E., Holz, Ronald W. (1992/08/31)."Synthetic peptides of the effector-binding domain of rab enhance secretion from digitonin-permeabilized chromaffin cells." FEBS Letters 309(1): 41-46. <http://hdl.handle.net/2027.42/29893> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T36-44XN752-1NP/2/318ef89d62ea4f880543b4f61d0be306 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/29893 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1324849&dopt=citation | en_US |
dc.description.abstract | There is evidence that the rab class of low molecular weight GTP-binding proteins is involved in vesicular transfer from endoplasmic reticulum to Golgi and between Golgi cisternae. To determine whether similar proteins play a role in regulated exocytosis, the effects of synthetic peptides derived from low molecular weight GTP-binding proteins on catecholamine secretion from digitonin-permeabilized chromaffin cells were investigated. The synthetic peptides represent the putative effector-binding domains of the rab, ras and ral classes of low molecular weight GTP-binding proteins and correspond to ras(33-48). Two rab peptides but neither a ras nor a ral peptide enhanced Ca2+-dependent secretion by approximately 30%. Maximal secretion in response to Ca2+ was increased. The enhancement was not blocked by the pseudosubstrate inhibitor of protein kinase C, PKC(19-31), thus indicating that activation of protein kinase C was not responsible for the enhancement of secretion. Similarly a rab peptide but neither a ras nor a ral peptide enhanced CppNHp-induced secretion 30-70%. The peptides had little or no effet in the absence of Ca2+ or GppNHp. The data are consistent with a protein of the rab class playing a role in regulated exocytosis. | en_US |
dc.format.extent | 743664 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Synthetic peptides of the effector-binding domain of rab enhance secretion from digitonin-permeabilized chromaffin cells | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109-0626, USA | en_US |
dc.contributor.affiliationum | Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109-0626, USA | en_US |
dc.contributor.affiliationother | Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037, USA | en_US |
dc.identifier.pmid | 1324849 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/29893/1/0000247.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0014-5793(92)80735-Y | en_US |
dc.identifier.source | FEBS Letters | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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