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  • Title: No significant tyrosine phosphorylation of muscle fatty acid-binding protein.
    Author: Prinsen CF, Werten PJ, Maassen JA, Veerkamp JH.
    Journal: Biochim Biophys Acta; 1994 Nov 17; 1215(1-2):103-8. PubMed ID: 7947990.
    Abstract:
    As suggested by the work on adipocyte fatty acid-binding protein (FABP), other FABPs with a tyrosine kinase consensus sequence could possibly be phosphorylated by the insulin receptor tyrosine kinase. Upon stimulation with insulin, recombinant human muscle fatty acid-binding protein (M-FABP) was phosphorylated in vitro by the insulin receptor tyrosine kinase only to a slight extent (< 0.1%). Rat soleus muscle shows at incubation autophosphorylation of insulin receptors but not phosphorylation of M-FABP after insulin stimulation. Vanadate and phenylarsine oxide had no effect on the extent of phosphorylation of M-FABP in vitro and in soleus muscle. Our results do not indicate that tyrosine phosphorylation of M-FABP is an important physiological phenomenon.
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