QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, January 21, 2009, 29(3):863-870; doi:10.1523/JNEUROSCI.2818-08.2009

This Article Full Text Full Text (PDF) Supplemental Data Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (2) Citing Articles via Google Scholar Google Scholar Articles by Berberian, K. Articles by Lindau, M. Search for Related Content PubMed PubMed Citation Articles by Berberian, K. Articles by Lindau, M.

 Previous Article  |  Next Article 

Cellular/Molecular
F-Actin and Myosin II Accelerate Catecholamine Release from Chromaffin Granules

Khajak Berberian,^1,2 * Alexis J. Torres,^3 * Qinghua Fang,¹ Kassandra Kisler,¹ and Manfred Lindau¹

¹School of Applied and Engineering Physics, and Departments of ²Biomedical Engineering and ³Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853

Correspondence should be addressed to Dr. Manfred Lindau, School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853. Email: ml95{at}cornell.edu

The roles of nonmuscle myosin II and cortical actin filaments in chromaffin granule exocytosis were studied by confocal fluorescence microscopy, amperometry, and cell-attached capacitance measurements. Fluorescence imaging indicated decreased mobility of granules near the plasma membrane following inhibition of myosin II function with blebbistatin. Slower fusion pore expansion rates and longer fusion pore lifetimes were observed after inhibition of actin polymerization using cytochalasin D. Amperometric recordings revealed increased amperometric spike half-widths without change in quantal size after either myosin II inhibition or actin disruption. These results suggest that actin and myosin II facilitate release from individual chromaffin granules by accelerating dissociation of catecholamines from the intragranular matrix possibly through generation of mechanical forces.

Key words: chromaffin cells; exocytosis; actin; myosin II; amperometry; capacitance; fluorescence microscopy; fusion pore

---

Received June 19, 2008; revised Nov. 28, 2008; accepted Dec. 15, 2008.

Correspondence should be addressed to Dr. Manfred Lindau, School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853. Email: ml95{at}cornell.edu

This article has been cited by other articles:

				N. Wang, C. Kwan, X. Gong, E. P. de Chaves, A. Tse, and F. W. Tse Influence of Cholesterol on Catecholamine Release from the Fusion Pore of Large Dense Core Chromaffin Granules J. Neurosci., March 17, 2010; 30(11): 3904 - 3911. [Abstract] [Full Text] [PDF]

				B. W. Doreian, T. G. Fulop, R. L. Meklemburg, and C. B. Smith Cortical F-Actin, the Exocytic Mode, and Neuropeptide Release in Mouse Chromaffin Cells Is Regulated by Myristoylated Alanine-rich C-Kinase Substrate and Myosin II Mol. Biol. Cell, July 1, 2009; 20(13): 3142 - 3154. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help