Protection against osmotic stress by cGMP-mediated myosin phosphorylation

Science

Volumn 271, Issue 5246, 1996, Pages 207-209

  Kuwayama, Hidekazu ^a   Ecke, Maria ^b   Gerisch, Günther ^b   Van Haastert, Peter J M ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC GMP; GUANOSINE PHOSPHATE; MYOSIN;

ARTICLE; CELL SHAPE; CONTROLLED STUDY; DICTYOSTELIUM DISCOIDEUM; NONHUMAN; OSMOTIC STRESS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION;

EID: 0030024280     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.271.5246.207     Document Type: Article

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38. AAA cells was determined as described in Fig 1 In (B), phosphorylation of myosin II heavy chain was induced in XP55 and KI-8 cells upon incubation with 300 mM glucose with or without 1 mM 8Br-cGMP.
39. Cells were starved for 1 hour in phosphate buffer, incubated in the presence of 300 mM glucose for 10 min and 30 min, and fixed with 15% picric acid and 2% formaldehyde in 10 mM Pipes-HCl (pH 6 0) (28). The fixed cells were incubated simultaneously with fluorescein isothiocyanate-conjugated phalloidin to stain actin filaments and with monoclonal antibody 396 to myosin II [which recognizes both myosin II monomers and filaments (29)] plus tetramethyl rhodamine isothiocyanateconjugated goat antibody to mouse immunoglobulin G. Confocal sections of cells were taken with a 40X Plan-Neofluar objective on a Zeiss LSM 410 fluorescence laser-scanning microscope; the images were color-labeled to red (myosin II) and green (actin).
40. AAA transformant was produced by D. Vielmetter in collaboration with J. A. Spudich, and KI-8 was isolated by H.K. in collaboration with S. Ishida. Supported in part by grant SFB266/07 of the Deutsche Forschungsgemeinschaft.