| The organization of F-actin and microtubules in growth cones exposed to a brain-derived collapsing factor. | |
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MedLine Citation:
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PMID: 8491778 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In previous work we characterized a brain derived collapsing factor that induces the collapse of dorsal root ganglion growth cones in culture (Raper and Kapfhammer, 1990). To determine how the growth cone cytoskeleton is rearranged during collapse, we have compared the distributions of F-actin and microtubules in normal and partially collapsed growth cones. The relative concentration of F-actin as compared to all proteins can be measured in growth cones by rationing the intensity of rhodamine-phalloidin staining of F-actin to the intensity of a general protein stain. The relative concentration of F-actin is decreased by about one half in growth cones exposed to collapsing factor for five minutes, a time at which they are just beginning to collapse. During this period the relative concentration of F-actin in the leading edges of growth cones decreases dramatically while the concentration of F-actin in the centers decreases little. These results suggest that collapse is associated with a net loss of F-actin at the leading edge. The distributions of microtubules in normal and collapsing factor treated growth cones were examined with antibodies to tyrosinated and detyrosinated isoforms of alpha-tubulin. The tyrosinated form is found in newly polymerized microtubules while the detyrosinated form is not. The relative proximal-distal distributions of these isoforms are not altered during collapse, suggesting that rates of microtubule polymerization and depolymerization are not greatly affected by the presence of collapsing factor. An analysis of the distributions of microtubules before and after collapse suggests that microtubules are rearranged, but their polymerization state is unaffected during collapse. These results are consistent with the hypothesis that the brain derived collapsing factor has little effect on microtubule polymerization or depolymerization. Instead it appears to induce a net loss of F-actin at the leading edge of the growth cone. |
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Authors:
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J Fan; S G Mansfield; T Redmond; P R Gordon-Weeks; J A Raper |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of cell biology Volume: 121 ISSN: 0021-9525 ISO Abbreviation: J. Cell Biol. Publication Date: 1993 May |
Date Detail:
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Created Date: 1993-06-11 Completed Date: 1993-06-11 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0375356 Medline TA: J Cell Biol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 867-78 Citation Subset: IM |
Affiliation:
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Department of Neurosciences, University of Pennsylvania School of Medicine, Philadelphia 19104. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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physiology* Animals Axons / physiology Biological Factors / physiology* Brain / physiology*, ultrastructure Cell Movement Cells, Cultured Chick Embryo Chickens Cytochalasins / pharmacology Ganglia, Spinal / metabolism, ultrastructure Microtubules / physiology* Videotape Recording |
| Grant Support | |
ID/Acronym/Agency:
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T32-HD-07067/HD/NICHD NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Actins; 0/Biological Factors; 0/Cytochalasins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
| Full Text | |
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Journal Information Journal ID (nlm-ta): J Cell Biol ISSN: 0021-9525 ISSN: 1540-8140 Publisher: The Rockefeller University Press |
Article Information Download PDF  Print publication date: Day: 2 Month: 5 Year: 1993 Volume: 121 Issue: 4 First Page: 867 Last Page: 878 ID: 2119785 Publisher Id: 93260019 PubMed Id: 8491778 |
| The organization of F-actin and microtubules in growth cones exposed to a brain-derived collapsing factor | |
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