Second harmonic generation microscopy probes different states of motor protein interaction in myofibrils

Schurmann, S, von Wegner, F, Fink, RHA, Friedrich, O and Vogel, M (2010) Second harmonic generation microscopy probes different states of motor protein interaction in myofibrils. Biophysical Journal, 99 6: 1842-1851. doi:10.1016/j.bpj.2010.07.005


Author Schurmann, S
von Wegner, F
Fink, RHA
Friedrich, O
Vogel, M
Title Second harmonic generation microscopy probes different states of motor protein interaction in myofibrils
Journal name Biophysical Journal   Check publisher's open access policy
ISSN 0006-3495
1542-0086
Publication date 2010-09-22
Sub-type Article (original research)
DOI 10.1016/j.bpj.2010.07.005
Volume 99
Issue 6
Start page 1842
End page 1851
Total pages 10
Place of publication St Louis, MO, United States
Publisher Cell Press
Collection year 2011
Language eng
Formatted abstract
The second harmonic generation (SHG) signal intensity sourced from skeletal muscle myosin II strongly depends on the polarization of the incident laser beam relative to the muscle fiber axis. This dependence is related to the second-order susceptibility x(2), which can be described by a single component ratio γ under generally assumed symmetries. We precisely extracted γ from SHG polarization dependence curves with an extended focal field model. In murine myofibrillar preparations, we have found two distinct polarization dependencies: With the actomyosin system in the rigor state, γrig. has a mean value of γrig = 0.52 (SD = 0.04, n = 55); in a relaxed state where myosin is not bound to actin, γrel has a mean value of γrel = 0.24 (SD = 0.07, n = 70). We observed a similar value in an activated state where the myosin power stroke was pharmacologically inhibited using N-benzyl-p-toluene sulfonamide. In summary, different actomyosin states can be visualized noninvasively with SHG microscopy. Specifically, SHG even allows us to distinguish different actin-bound states of myosin II using γ as a parameter. © 2010 by the Biophysical Society.
Keyword Rat-tail tendon
Skeletal muscle
Striated-muscle
Myosin rod
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Biomedical Sciences Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 13 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 12 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Mon, 14 Feb 2011, 15:14:07 EST by Bacsweet Kaur on behalf of School of Biomedical Sciences