Comparisons of Endothelial Cell G- and F-Actin Distribution in Situ and in Vitro

References

• Blikstad I., Carlsson L. On the dynamics of the microfilament system in HeLa cells. J. Cell Biol. 1982; 93: 122–128
   PubMedGoogle Scholar
• Blikstad I., Markely F., Carlsson L., Persson T., Linberg U. Selective assay of monomeric and filamentous actin in cell extracts using inhibition of deoxyribonuclease I. Cell 1978; 15: 935–943
   PubMed Web of Science ®Google Scholar
• Bottaro D., Shepro D., Peterson S., Hechtman H. B. Serotonin, norepinephrine and histamine mediation of endothelial cell barrier function in vitro. J. Cell Physiol. 1986; 128: 189–194
   PubMedGoogle Scholar
• Bottaro D., Shepro D., Peterson S., Hechtman H. B. Serotonin, norepinephrine, and his-tamine mediation of endothelial cell and vascular smooth muscle cell movement. Am. J. Physiol. 1985; 248: C252–C257, (Cell Physiol. 17)
   Google Scholar
• DuBose D. A., Shepro D., Hechtman H. B. Modulation of phospholipase A2 lytic activity by actin and myosin. Inflammation 1989; 13: 15–29
   PubMedGoogle Scholar
• DuBose D. A., Shepro D., Hechtman H. B. Correlation among endothelial cell shape, F-actin arrangement and prostacyclin synthesis. Life Sci. 1987; 40: 447–453
   PubMedGoogle Scholar
• Gabbiani G., Gabbiani F., Lombardi D., Schwartz S. M. Organization of actin cytoskeleton in normal and regenerating arterial endothelial cells. Proc. Natl. Acad. Sci. USA 1983; 80: 2361–2364
   PubMedGoogle Scholar
• Gabbiani G., Badonnel M. C., Rona G. Cytoplasmic contractile apparatus in aortic endothelial cells of hypertensive rats. Lab. Invest. 1975; 32: 227–234
   PubMed Web of Science ®Google Scholar
• Heacock C. S., Eidsvoog K. E., Bamburg J. R. The influence of contact-inhibited growth and of agents which alter cell morphology on the levels of G- and F-actin in cultured cells. Exp. Cell Res. 1984; 153: 402–412
   PubMedGoogle Scholar
• Heacock C. S., Bamburg J. R. a. Levels of filamentous and globular actin in Chinese hamster ovary cells throughout the cell cycle. Exp. Cell Res. 1983; 147: 240–246
   Google Scholar
• Heacock C. S., Bamburg J. R. b. The quantitation of G- and F-actin in cultured cells. Ann. Biochem. 1983; 135: 22–36
   Google Scholar
• Herman I. M., Pollard T. D., Wong A. J. Contractile proteins in endothelial cells. Ann. N.Y. Acad. Sci. 1982; 401: 50–60
   PubMedGoogle Scholar
• Hitchcock S. E. Actin-deoxyribonuclease I interaction. Depolymerization and nucleotide exchange. J. Biol. Chem. 1980; 255: 5668–5673
   Google Scholar
• Hitchcock S. E., Carlsson L., Lindberg U. Depolymerization of F-actin by deoxyribonuclease I. Cell 1976; 7: 531–542
   PubMedGoogle Scholar
• Jaffe E. A., Nachman R. L., Becker G. C., Minick C. R. Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J. Clin. Invest. 1973; 52: 2745–2756
   PubMed Web of Science ®Google Scholar
• Kalnins V. I., Subrahmanyan L., Gottlieb A. I. Thereorganization of cytoskeletal fibre systems in spreading porcine endothelial cells in culture. Eur. J. Cell Biol. 1981; 24: 36–44
   PubMedGoogle Scholar
• Korn E. D. Actin polymerization and its regulation by proteins from nonmuscle cells. Phpsiol. Rev. 1982; 62: 672–737
   PubMed Web of Science ®Google Scholar
• Mannherz H. G., Goody R. S., Konrad M., Nowak E. The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin. Eur. J. Biochem. 1980; 104: 367–379
   PubMedGoogle Scholar
• Morris A., Tannenbaum J. Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells. Nature 1980; 287: 637–639
   PubMedGoogle Scholar
• Payne M. R., Rudnick S. E. Inhibition of muscle tropomyosin polymerization by DNAse I. Biosci. Reports 1986; 6: 721–726
   PubMedGoogle Scholar
• Rogers K. M., Kalnins V. I. a. A method for examining the endothelial cytoskeleton in situ using immunofluorescence. J. Histochem. Cytochem. 1983; 31: 1317–1320
   PubMedGoogle Scholar
• Rogers K. M., Kalnins V. I. b. Comparison of the cytoskeleton in aortic endothelial cells in situ and in vitro. Lab. Invest. 1983; 49: 650–654
   Google Scholar
• Welles S. L., Shepro D., Hechtman H. B. a. Vasoactive amines modulate actin cables (stress fibers) and surface area in cultured bovine endothelium. J. Cell Physiol. 1985; 123: 337–342
   Google Scholar
• Welles S. L., Shepro D., Hechtman H. B. b. Eicosanoid modulation of stress fibers in cultured bovine aortic endothelial cells. Inflammation 1985; 9: 439–450
   Google Scholar
• White G. E., Fujiwara K. Expression and intracellular distribution of stress fibers in aortic endothelium. J. Cell Biol. 1986; 103: 63–70
   PubMed Web of Science ®Google Scholar
• White G. E., Gimbrone M. A., Fujiwara K. Factors influencing the expression of stress fibers in vascular endothelial cells in situ. J. Cell Biol. 1983; 97: 416–424
   PubMed Web of Science ®Google Scholar
• Weiland T., Faulstich H. Amatoxins. phallotoxins. phallolysin and antaminide: the biologically active components of poisonous amanita mushrooms. CRC Crit. Rev. Biochem. 1978; 5: 185–260
   Google Scholar
• Wong A. J., Pollard T. D., Herman I. M. Actin filaments stress fibers in vascular endothelial cells in vivo. Science 1983; 219: 867–869
   PubMed Web of Science ®Google Scholar