Comparison of the regional distribution of calspectin (nonerythroid spectrin or fodrin), alpha-actinin, vinculin nonerythroid protein 4.1, and calpactin in normal and avian sarcoma virus- or Rous sarcoma virus-induced transformed cells.
With fluorescence and interference reflection microscopy (IRM), we compared the regional distribution of calspectin, its interacting proteins (nonerythroid protein 4.1 and calpactin), alpha-actinin, and vinculin in NRK cells and their avian sarcoma virus (ASV)- or temperature-sensitive (ts) Rous sarcoma virus (RSV)-transformed cells. The localization of these cytoskeletal proteins was determined with the specific antibodies. In NRK cells, alpha-actinin and vinculin were concentrated at adhesion plaques. By contrast, calspectin was distributed throughout the cytoplasm, but not concentrated at adhesion plaques. In ASV- and ts RSV-transformed cells, all three cytoskeletal proteins were concentrated at dot structures representing cellular feet. Nonerythroid protein 4.1 and calpactin were diffusely distributed throughout the cytoplasm of NRK cells and their transformed counterparts. In the case of calpactin, a part of this protein was excluded near regions of the terminal ends of stress fibers. These two proteins did not show the restricted location at the dot structures of transformed cells. From these findings, it is apparent that the accumulation of calspectin into dot structures is a specific event for cell transformation induced by the src protein.
Sobue
K
K
Department of Neurochemistry and Neuropharmacology, Osaka University Medical School, Japan.
Kanda
K
K
Miyamoto
I
I
Iida
K
K
Yahara
I
I
Hirai
R
R
Hiragun
A
A
D000185:Actinin / Q000032:analysis; D000818:Animals; D017302:Annexins; D001358:Avian Sarcoma Viruses; D002135:Calcium-Binding Proteins / Q000032:analysis; D002148:Calmodulin-Binding Proteins / Q000032:analysis*; D002448:Cell Adhesion; D002460:Cell Line; D002461:Cell Line, Transformed; D002471:Cell Transformation, Neoplastic; D002472:Cell Transformation, Viral; D003593:Cytoplasm / Q000032:analysis*; D003598:Cytoskeletal Proteins / Q000032:analysis*; D005455:Fluorescent Antibody Technique; D008565:Membrane Proteins / Q000032:analysis; D008856:Microscopy, Fluorescence; D009124:Muscle Proteins / Q000032:analysis; D009479:Neuropeptides; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols / Q000378:metabolism; D016596:Vinculin
D017302:Annexins; D002135:Calcium-Binding Proteins; D002148:Calmodulin-Binding Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009124:Muscle Proteins; D009479:Neuropeptides; D019269:Phosphatidylinositol 4,5-Diphosphate; D010716:Phosphatidylinositols; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D000185:Actinin; D016596:Vinculin