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Claims that intermediate filaments contain F-actin are unwarranted
The Journal of Cell Biology
|August 1, 1981
Summary
Trypsinization removes intermediate filaments from cultured cells, forming atypical filaments from thin filaments. Previous findings suggesting f-actin in normal intermediate filaments are retracted due to this new evidence.
Area of Science:
- Cell Biology
- Cytoskeleton Research
Background:
- Previous studies suggested normal intermediate filaments contain f-actin based on heavy meromyosin binding to atypical filaments.
- Cultured cells (chick embryo fibroblasts, IMR-33, BHK-21) were examined for filament composition.
Purpose of the Study:
- To re-evaluate the composition of intermediate filaments in cultured cells.
- To correct previous misconceptions regarding f-actin presence in normal intermediate filaments.
Main Methods:
- Examination of sectioned and embedded cultured cells (fibroblasts, IMR-33, BHK-21).
- Analysis of filament structures before and after trypsinization.
Main Results:
- Trypsinization eliminated most normal intermediate filaments.
- Atypical intermediate-sized filaments formed from the close apposition of thin filaments.
- Heavy meromyosin binding to atypical filaments was misinterpreted in prior research.
Conclusions:
- The previous suggestion that normal intermediate filaments contain f-actin is unwarranted.
- The study retracts the earlier conclusion, clarifying filament composition.