Title : Transforming growth factor-alpha increases tyrosine phosphorylation of microtubule-associated protein kinase in a small intestinal crypt cell line (IEC-6).

Pub. Date : 1994 Oct 15

PMID : 7980404






5 Functional Relationships(s)
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1 Transforming growth factor-alpha increases tyrosine phosphorylation of microtubule-associated protein kinase in a small intestinal crypt cell line (IEC-6). Tyrosine transforming growth factor alpha Rattus norvegicus
2 The small intestinal crypt cell line (IEC-6) is an undifferentiated, untransformed, mitotically active cell used in this study to determine the effect of transforming growth factor-alpha (TGF-alpha) on tyrosine phosphorylation levels of cellular proteins. Tyrosine transforming growth factor alpha Rattus norvegicus
3 Thymidine incorporation increased maximally after addition of 2 ng/ml TGF-alpha for 24 h. At the same dose, TGF-alpha induced the tyrosine phosphorylation of proteins with approximate molecular masses of 42, 44, 52, 80, 150 and 175 kDa as shown by Western blots treated with anti-phosphotyrosine antibody. Tyrosine transforming growth factor alpha Rattus norvegicus
4 Thymidine incorporation increased maximally after addition of 2 ng/ml TGF-alpha for 24 h. At the same dose, TGF-alpha induced the tyrosine phosphorylation of proteins with approximate molecular masses of 42, 44, 52, 80, 150 and 175 kDa as shown by Western blots treated with anti-phosphotyrosine antibody. Tyrosine transforming growth factor alpha Rattus norvegicus
5 We conclude that MAPK is tyrosine phosphorylated in response to TGF-alpha stimulation of IEC-6 cells. Tyrosine transforming growth factor alpha Rattus norvegicus