H
Harry T. Haigler
Researcher at University of California, Irvine
Publications - 66
Citations - 5714
Harry T. Haigler is an academic researcher from University of California, Irvine. The author has contributed to research in topics: Epidermal growth factor & Annexin. The author has an hindex of 36, co-authored 66 publications receiving 5653 citations. Previous affiliations of Harry T. Haigler include University of Southern California & Vanderbilt University.
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Journal ArticleDOI
Dansylcadaverine inhibits internalization of 125I-epidermal growth factor in BALB 3T3 cells.
TL;DR: It is proposed that dansylcadaverine inhibits EGF internalization by preventing it from clustering in clathrin-coated pits.
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Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431.
TL;DR: The binding and internalization of epidermal growth factor in human epithelioid carcinoma cells (A-431) has been followed with 125I-labeled EGF and by fluorescence microscopy to provide direct confirmation of the previous biochemical data that suggested that cell membrane-bound EGF is rapidly internalized.
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Direct visualization of the binding and internalization of a ferritin conjugate of epidermal growth factor in human carcinoma cells A-431.
TL;DR: A conjugate of epidermal growth factor and ferritin that retains substantial binding affinity for cell receptors and is biologically active is prepared, consistent with other morphological and biochemical studies utilizing 125I-EGF and fluorescein-conjugated EGF.
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Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor.
TL;DR: Biochemical methods showed that HRP uptake in control cultures was directly proportional to the duration of exposure and the tumor-promoter 12-0- tetradecanoyl-phorbol-13-acetate was effective in stimulating an increase in the rate of pinocytosis.
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Characterization of lipocortin I and an immunologically unrelated 33-kDa protein as epidermal growth factor receptor/kinase substrates and phospholipase A2 inhibitors.
TL;DR: The results of these and other experiments raise the possibility that placental lipocortin I inhibits phospholipase A2 activity in this assay by coating theospholipid and thereby blocking interaction of enzyme and substrate.