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Fig. 3. Phosphorylation of p38-MAPK by more intense extracellular alkalosis (pH
9.5) (A top, B) or acidosis (pH 6.5) (C top, D). (A) Phospho-p38-MAPK was
detected in extracts (50 µg of protein) from control hearts (Co) and hearts
perfused with a Tris–Tyrode's perfusion buffer of pH 9.5 for the
indicated times (top). Total p38-MAPK levels were detected in identical
samples as a control for loading (bottom). (C) The p38-MAPK phosphorylation
was also measured by immunoblot analysis in samples from hearts subjected to
extracellular acidosis (pH 6.5) for increasing periods of time using the
MES–Tyrode's perfusion buffer (top), as described in Materials and
methods. Equal loading was assessed, as previously, using a p38-MAPK antibody
(bottom). As a positive control, extract from hearts perfused with 0.5 mol
l–1 sorbitol (Sor) for 15 min was used. (B,D) Densitometric
analysis of phospho-p38-MAPK bands by laser scanning. Results are means
± s.e.m. for three independent experiments. *P<0.05,
**P<0.01, 
P<0.001 vs
control value.
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