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Title: Growth factor regulation of sugar uptake in cultured cells

Thesis/Dissertation ·
OSTI ID:7108217

Mouse EGF stimulates the uptake of 2-deoxygluclose (dGIc), a non-metabolized glucose analogue, into cultured mouse 3T3 fibroblasts (Clone 1) 2 to 4 fold, and EGF dependent Balb/MK-1 epidermal kerotinocytes, 5 to 8 fold. Initial stimulation is detected at 15 minutes. Maximal effects are seen at 2 hours with 10 ng/ml EGF. Binding of /sup 125/I-labeled EGF to cells is rapid and complete by 2 hours at 37/sup 0/C. Antibodies which specifically inhibit /sup 125/I-labeled EGF binding to cells inhibit EGF stimulation as much as 85%. Human platelet derived TGF-..beta.. stimulates dGlc uptake up to 5 fold. Maximum effects are seen with 1 ng/ml TGF-..beta.. within 2 hours and stimulation is detected 30 minutes after exposure to 0.1 ng/ml, the minimum effective concentration. TGF-..beta.., like EGF, stimulates sugar transport into Balb/MK-1 cells without additional factors. However, neither stimulates uptake in a 3T3 variant, NR-6, which is EGF-receptor negative. The co-addition of EGF and/or PDGF enhances TGF-..beta.. stimulation. Binding of /sup 125/I-labeled TGF-..beta.. is nearly complete by 1 hour at 37/sup 0/C, but continues to increase for as long as 4 hours after addition. Antibodies which inhibit EGF binding have no effect on TGF-..beta.. binding, but they block TGF-..beta.. stimulation of hexose uptake. It is concluded from these results that the TGF-..beta.. receptor is distinct from the EGF receptor, and that although TGF-..beta.. stimulation of dGLc uptake does not require exogenously added EGF, it does require an active or available EGF receptor kinase system.

Research Organization:
Vanderbilt Univ., Nashville, TN (USA)
OSTI ID:
7108217
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English

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