. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 266 REPORTS FROM THE MBL GENERAL SCIENTIFIC MEETINGS. Figure 1. Vanadate-inditced actin filament bundles in clam oocyte extracts: the DIC (top row) and corresponding fluorescent images (bottom row) of extracts that were stained with rhodamine-phalloidin. Actin filaments were present in control samples (C> at the initial time point (15 min) as well as the final time point (60 min). In vanadate (I mM)-treated samples (V), bundles rather than filaments were detected at the 15 and 60 min time points. Concentrated extracts of
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 266 REPORTS FROM THE MBL GENERAL SCIENTIFIC MEETINGS. Figure 1. Vanadate-inditced actin filament bundles in clam oocyte extracts: the DIC (top row) and corresponding fluorescent images (bottom row) of extracts that were stained with rhodamine-phalloidin. Actin filaments were present in control samples (C> at the initial time point (15 min) as well as the final time point (60 min). In vanadate (I mM)-treated samples (V), bundles rather than filaments were detected at the 15 and 60 min time points. Concentrated extracts of clam oocytes were clarified, incubated at 1S°C for 45 min, and stained with jiM rhodamine-phalloidin which stabilizes actin filaments and enables their detection through fluorescence microscopy. Scale bar, 5 fim. does not allow us to state categorically that the effect we observed is due solely to inhibition of protein tyrosine dephosphorylation. To resolve this potential complication, future experiments are planned to determine the level of tyrosine phosphorylation in the extract when vanadate is present, and to monitor the level of phosphotyrosine in specific actin cross-linking proteins. Literature Cited I DePina, A. S., and G. M. Langford. 1999. Microsc. Res. Tech. (In press). 2. Gilbert-McClain, L. I., A. D. Verin, S. Shi, R. P. Irwin, and J. G. Garcia. 1998. J. Cell. Biochem. 70: 141-15?. 3. Moreau, V., and M. Way. 1998. FEBS Lett. 427: 353-356. 4. Ma, L., L. C. Cantley, P. A. Janmey, and M. W. Kirschner. 1998. J. Cell Biol. 140: 1125-1136. 5. Swarup, G., S. Cohen, and D. L. Garbers. 1982. Biochem. Bio- plivs. Res. Commtin. 107: 1104-1109. 6. Goodno, C. C. 1982. Methods Enzymol. 85: 116-123. 7. Goodno, C. C. 1979. Proc. Nail. AcaJ. Sci. U. S. A. 76: 2620-2624. 8. Huang, W. H., and A. Askari. 1984. J. Biol. Chem. 259: 13287- 13291. 9. Vescina, C. M., V. C. Salice, A. M. Cortizo, and S. B. Etcheverry. 1996. Biol. Trace Elcm. «o. 53: 185-191. 10. Seargeant, L. E., and
Size: 2330px × 1073px
Photo credit: © Library Book Collection / Alamy / Afripics
License: Licensed
Model Released: No
Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
