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pro vyhledávání: '"J. E. Koda"'
Publikováno v:
Clinical chemistry. 42(4)
Amylin is a 37-amino-acid polypeptide synthesized in and secreted from pancreatic beta cells along with insulin. Its biological actions include the slowing and reduction of postmeal increases in plasma glucose concentrations. Studies of the basic amy
Publikováno v:
Hypertension (Dallas, Tex. : 1979). 19
The experimental evidence supporting a direct role for hyperinsulinemia as a cause of insulin resistance remains equivocal. Amylin, an islet beta-cell peptide cosecreted with insulin in response to nutrient stimuli, causes insulin resistance when inf
Autor:
M Bernfield, J E Koda
Publikováno v:
Journal of Biological Chemistry. 259:11763-11770
Mouse mammary epithelial cells (NMuMG cells) deposit at their basal surfaces an extracellular heparan sulfate-rich proteoglycan that binds to type I collagen. The binding of the purified proteoglycan to collagen was studied by (i) a solid phase assay
Publikováno v:
The Journal of biological chemistry. 260(13)
A heparan sulfate-rich proteoglycan is on the surface of NMuMG mouse mammary epithelial cells apparently intercalated into their plasma membranes. Mild treatment of the cells with trypsin releases the GAG-bearing region (ectodomain) of this molecule
Autor:
J E, Koda, M, Bernfield
Publikováno v:
The Journal of biological chemistry. 259(19)
Mouse mammary epithelial cells (NMuMG cells) deposit at their basal surfaces an extracellular heparan sulfate-rich proteoglycan that binds to type I collagen. The binding of the purified proteoglycan to collagen was studied by (i) a solid phase assay
Publikováno v:
Ciba Foundation symposium. 108
We have analysed the reciprocal interactions between mouse embryo submandibular epithelium and mesenchyme which result in branching morphogenesis of the epithelium. The interactions modify the composition and metabolism of the basal and reticular lam