Centrifugation shearing exposes filamentous networks in cortical regions of crane-fly spermatocytes.
Open Access
- 1 June 1982
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 93 (3) , 670-679
- https://doi.org/10.1083/jcb.93.3.670
Abstract
Spermatocytes of the crane-fly, Nephrotoma suturalis, were attached to electron microscope grids and then sheared by applying centrifugal force. Transmission electron microscopy of exposed regions of the cell cortex revealed networks containing arrays of filamentous structures. Networks were present in sheared spermatocytes at all stages of meiosis. The networks of dividing spermatocytes (meta- through telophase) were denser and appeared to contain more aggregated material then networks of prophase cells. The appearance of networks in spermatocytes resembled actin-containing networks of sheared and detergent-extracted human erythrocytes. Networks treated with myosin subfragment 1 under conditions in which muscle F-actin was clearly decorated were not distinguishable from those of untreated cells. Exposure to deoxyribonuclease-1 caused the disruption of networks in sheared spermatocytes as well as in erythrocytes. The results of deoxyribonuclease experiments are interpreted as an indication that actin is a component of the cell cortex in crane-fly spermatocytes.Keywords
This publication has 38 references indexed in Scilit:
- The cytoplasmic filamentous network in cultured ovarian granulosa cellsCell, 1980
- Biochemical analysis of actin in crane-fly gonial cells: evidence for actin in spermatocytes and spermatids--but not sperm.The Journal of cell biology, 1980
- DNase-I-dependent dissociation of erythrocyte cytoskeletons.The Journal of cell biology, 1979
- Triton shells of intact erythrocytesJournal of Supramolecular Structure, 1978
- The sub‐membrane reticulum of the human erythrocyte: A scanning electron microscope studyJournal of Supramolecular Structure, 1977
- A Specific 1:1 G‐actin: DNAase I complex formed by the action of DNAase I on F‐actinFEBS Letters, 1975
- Substructure of the myosin molecule: IV. Interactions of myosin and its subfragments with adenosine triphosphate and F-actinJournal of Molecular Biology, 1973
- Cell locomotion, nerve elongation, and microfilamentsDevelopmental Biology, 1973
- Enucleation of mammalian cells with cytochalasin BExperimental Cell Research, 1972
- Polymerization of actin free from nucleotide and divalent cationsBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965