Show simple item record

dc.contributor.authorPatki, Varsha
dc.contributor.authorBuxton, Joanne M.
dc.contributor.authorChawla, Anil
dc.contributor.authorLifshitz, Lawrence M.
dc.contributor.authorFogarty, Kevin E.
dc.contributor.authorCarrington, Walter A.
dc.contributor.authorTuft, Richard A.
dc.contributor.authorCorvera, Silvia
dc.date2022-08-11T08:09:33.000
dc.date.accessioned2022-08-23T16:35:17Z
dc.date.available2022-08-23T16:35:17Z
dc.date.issued2001-02-13
dc.date.submitted2009-03-24
dc.identifier.citationMol Biol Cell. 2001 Jan;12(1):129-41.
dc.identifier.issn1059-1524 (Print)
dc.identifier.pmid11160828
dc.identifier.urihttp://hdl.handle.net/20.500.14038/38523
dc.description.abstractA novel imaging technology, high-speed microscopy, has been used to visualize the process of GLUT4 translocation in response to insulin in single 3T3-L1 adipocytes. A key advantage of this technology is that it requires extremely low light exposure times, allowing the quasi-continuous capture of information over 20-30 min without photobleaching or photodamage. The half-time for the accumulation of GLUT4-eGFP (enhanced green fluorescent protein) at the plasma membrane in a single cell was found to be of 5-7 min at 37 degrees C. This half-time is substantially longer than that of exocytic vesicle fusion in neuroendocrine cells, suggesting that additional regulatory mechanisms are involved in the stimulation of GLUT4 translocation by insulin. Analysis of four-dimensional images (3-D over time) revealed that, in response to insulin, GLUT4-eGFP-enriched vesicles rapidly travel from the juxtanuclear region to the plasma membrane. In nontransfected adipocytes, impairment of microtubule and actin filament function inhibited insulin-stimulated glucose transport by 70 and 50%, respectively. When both filament systems were impaired insulin-stimulated glucose transport was completely inhibited. Taken together, the data suggest that the regulation of long-range motility of GLUT4-containing vesicles through the interaction with microtubule- and actin-based cytoskeletal networks plays an important role in the overall effect of insulin on GLUT4 translocation.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=11160828&dopt=Abstract">Link to Article in PubMed</a>
dc.subject3T3 Cells
dc.subjectAdipocytes
dc.subjectAnimals
dc.subjectCytoskeleton
dc.subjectDiagnostic Imaging
dc.subjectExocytosis
dc.subjectGlucose Transporter Type 4
dc.subjectGreen Fluorescent Proteins
dc.subjectHalf-Life
dc.subjectInsulin
dc.subjectLuminescent Proteins
dc.subjectMice
dc.subjectMicroscopy, Confocal
dc.subjectMonosaccharide Transport Proteins
dc.subject*Muscle Proteins
dc.subjectProtein Transport
dc.subjectRats
dc.subjectRecombinant Fusion Proteins
dc.subjectTransport Vesicles
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleInsulin action on GLUT4 traffic visualized in single 3T3-l1 adipocytes by using ultra-fast microscopy
dc.typeJournal Article
dc.source.journaltitleMolecular biology of the cell
dc.source.volume12
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2394&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/1395
dc.identifier.contextkey794892
refterms.dateFOA2022-08-23T16:35:17Z
html.description.abstract<p>A novel imaging technology, high-speed microscopy, has been used to visualize the process of GLUT4 translocation in response to insulin in single 3T3-L1 adipocytes. A key advantage of this technology is that it requires extremely low light exposure times, allowing the quasi-continuous capture of information over 20-30 min without photobleaching or photodamage. The half-time for the accumulation of GLUT4-eGFP (enhanced green fluorescent protein) at the plasma membrane in a single cell was found to be of 5-7 min at 37 degrees C. This half-time is substantially longer than that of exocytic vesicle fusion in neuroendocrine cells, suggesting that additional regulatory mechanisms are involved in the stimulation of GLUT4 translocation by insulin. Analysis of four-dimensional images (3-D over time) revealed that, in response to insulin, GLUT4-eGFP-enriched vesicles rapidly travel from the juxtanuclear region to the plasma membrane. In nontransfected adipocytes, impairment of microtubule and actin filament function inhibited insulin-stimulated glucose transport by 70 and 50%, respectively. When both filament systems were impaired insulin-stimulated glucose transport was completely inhibited. Taken together, the data suggest that the regulation of long-range motility of GLUT4-containing vesicles through the interaction with microtubule- and actin-based cytoskeletal networks plays an important role in the overall effect of insulin on GLUT4 translocation.</p>
dc.identifier.submissionpathoapubs/1395
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentDepartment of Physiology
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages129-41


Files in this item

Thumbnail
Name:
11160828.pdf
Size:
6.072Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record