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The effect of denervation on mammalian sarcolemmal proteins and glycoproteins
Author(s) -
Leung Wing Nang,
Jeffrey Peter L.,
Rostas John A. P.
Publication year - 1984
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880070107
Subject(s) - denervation , glycoprotein , sarcolemma , chemistry , microbiology and biotechnology , biology , medicine , biochemistry , anatomy , myocyte
The effects of surgical denervation on proteins and glycoproteins of sarcolemmal membranes have been investigated using sarcolemmal fractions prepared from mixed rat muscles. Denervation did not cause any gross change in the protein composition but some consistent quantitative changes were detected. Denervation caused a significant increase in the binding of 125 l‐labeled concanavalin A (ConA), Ricinus communis agglutinin (RCA 120 ), and wheat germ agglutinin (WGA) to intact membranes. This increased binding appears to be brought about by two mechanisms: the synthesis of more binding‐sites with the same apparent K D and the unmasking of previously cryptic binding sites. The activity of sialyl‐, galactosyl‐, and N‐acetylglucosaminyltransferases in the sarcolemmal fractions increased, whereas fucosyl‐glycoprotein‐transferase activity decreased following denervation. Kinetic analysis of the sialyl‐ and galactosyltransferase activities showed that the change was due to an increase in V max with no change in K m . These results are consistent with an increase in the turnover of sarcolemmal glycoproteins following denervation.