English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Growth inhibition and changes in morphology and actin distribution in Acetabularia acetabulum by phalloidin and phalloidin derivatives

Sawitzky, H., Hanfstingl, U., & Faulstich, H. (2003). Growth inhibition and changes in morphology and actin distribution in Acetabularia acetabulum by phalloidin and phalloidin derivatives. Protoplasma, 220(3-4), 209-218. doi:10.1007/s00709-002-0041-8.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
Protoplasma_220_2003_209.pdf (Any fulltext), 442KB
 
File Permalink:
-
Name:
Protoplasma_220_2003_209.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Sawitzky, Heiko, Author
Hanfstingl, Uschi1, Author              
Faulstich, Heinz2, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              

Content

show
hide
Free keywords: Acetabularia acetabulum; Phalloidin; Growth inhibition; Actin dynamics; Confocal laser scanning microscopy; Jasplakinolide
 Abstract: Effects on morphology and microfilament structure caused by phalloidin, phallacidin, and some semisynthetic phalloidin derivatives were studied in vegetative cells of the green alga Acetabularia acetabulum (L.) Silva. All phalloidin derivatives (except for phalloidin itself) caused growth stop of the alga after 1 day and (except for the fluorescein-labeled phalloidin) death of the cells after 4-7 days. Hair whorl tip growth and morphology as screened by light microscopy, as well as microfilament structure in tips, suggested that growth stop is correlated with a disorganization of actin filaments similar to that recently described for jasplakinolide (H. Sawitzky, S. Liebe, J. Willingale-Theune, D. Menzel, European Journal of Cell Biology 78: 424-433, 1999). Using rabbit muscle actin as a model target protein, we found that the toxic effects in vivo did not correlate with actin affinity values, suggesting that permeation through membranes must play a role. Indeed, the most lipophilic phalloidin derivatives benzoylphalloidin and dithiolanophalloidin were the most active in causing growth stop at ca. 100 microM. In comparison to the concentration of jasplakinolide required to cause similar effects (<3 microM), the two most active phalloidin derivatives exhibited an activity ca. 30 times lower. Nonetheless, lipophilic phalloidin derivatives can be used in algae, and probably also other cells, to modulate actin dynamics in vivo. In addition, we found that the fluorescent fluorescein isothiocyanate-phalloidin is able to enter living algal cells and stains actin structures brightly. Since it does not suppress actin dynamics, we suggest fluorescein isothiocyanate-phalloidin as a tool for studying rearrangements of actin structures in live cells, e.g., by confocal laser scanning microscopy.

Details

show
hide
Language(s): eng - English
 Dates: 2001-11-052002-08-082002-11-292003-03-01
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Protoplasma
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Wien : Springer-Verlag
Pages: - Volume / Issue: 220 (3-4) Sequence Number: - Start / End Page: 209 - 218 Identifier: ISSN: 0033-183X
CoNE: https://pure.mpg.de/cone/journals/resource/954925435463