A lactose-extractable lectin obtained from 14--16-d embryonic chick pectoral muscle and myotube muscle cultures by affinity chromatography inhibited myotube formation in culture. When applied to muscle cultures at 0.09 micrograms/ml, the purified lectin produced variable effects on the inhibition of myotube formation related to the time and length of application, suggesting that components of the culture medium and/or temperature produced inactivation. Hemagglutination assays showed that the lectin was inactivated by horse serum and by chick embryo extract but not by L-15 salt solution at 4 degrees C. Incubation in L-15 solution at 37 degrees C with or without 2 mM dithiothreitol resulted in inactivation in 2--3 h. To maximize the effect of the lectin on the inhibition of myotube formation, primary muscle cultures were grown in low [Ca+2] medium to inhibit fusion, and then [Ca+2] was increased to elicit fusion in the absence and presence of lectin with solution renewal every 2 h. Without lectin, myotube formation was normal, whereas, with lectin, it was inhibited by 93%. Continued incubation at 37 degrees C. without renewal of lectin resulted in myotube formation, suggesting reversibility by lectin inactivation.
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1 June 1980
Article|
June 01 1980
Purified lectin from skeletal muscle inhibits myotube formation in vitro.
R G MacBride
R J Przybylski
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1980) 85 (3): 617–625.
Citation
R G MacBride, R J Przybylski; Purified lectin from skeletal muscle inhibits myotube formation in vitro.. J Cell Biol 1 June 1980; 85 (3): 617–625. doi: https://doi.org/10.1083/jcb.85.3.617
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