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J Biol Chem, Vol. 273, Issue 16, 9495-9500, April 17, 1998
From the Extracellular matrix and growth factors cooperate
to regulate signaling pathways and gene transcription in adherent
cells. However, the mechanism of extracellular matrix signaling is
poorly defined. In mammary gland, the expression of milk protein genes is controlled by cross-talk between signals derived from the basement membrane protein, laminin, and the lactogenic hormone, prolactin. Signals from basement membrane are transduced by
Regulation of Mammary Differentiation by Extracellular Matrix
Involves Protein-tyrosine Phosphatases
,,
School of Biological Sciences, University of
Manchester, 3.239 Stopford Building, Oxford Road, Manchester, M13 9PT,
United Kingdom, § NIDDK, Laboratory of Biochemistry and
Metabolism, National Institutes of Health, Bethesda, Maryland 20892, and the ¶ Unite d'Endocrinologie Moleculaire, Institute National
de la Researche Agronomique, 78352 Jouy-en-Josas Cedex, France
1
integrins and are required for prolactin to activate DNA binding of the milk protein gene transcription factor, Stat5. Here we show that basement membrane is necessary for tyrosine phosphorylation of the
prolactin receptor and thus directly affects cytokine signaling and
differentiation at the level of the plasma membrane. Prolactin does not
induce tyrosine phosphorylation of its receptor, Jak2, or Stat5 in
nondifferentiated breast epithelia cultured on collagen I, and we show
that this is due to a vanadate-sensitive activity that inhibits the
prolactin pathway. We suggest that protein-tyrosine phosphatases are
novel targets for regulation by extracellular matrix and in mammary
cells represent an additional control to the requirement of integrins
for milk protein production.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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