2010 Student Research Conference:
23rd Annual Student Research Conference

Mechanism of Uptake of Cystatin C by B16F10 Melanoma Cells
Lauren E. Deady
Dr. James Cox (A.T. Still University) and Dr. Timothy D. Walston, Faculty Mentors

The cystatins belong to a family of cysteine protease inhibitors that are known to play multiple roles in cell physiology. Little is known about the uptake of cystatins by cells. Here, the uptake of fluorescently labeled chicken cystatin C into cultured murine B16F10 metastatic melanoma cells was investigated. Uptake of cystatin was apparently distinct from that of Texas Red labeled dextran. Cystatin uptake was found to be independent of caveolin-1, a protein indicative of caveolae based endocytosis. Cells were pretreated with several inhibitors to test for their effects on cystatin uptake. Neither blebbistatin, an inhibitor of myosin II ATPase, nor colchicine, a microtubule inhibitor, had a dramatic effect. Wortmannin, a PI3-kinase inhibitor that disrupts receptor mediated endocytosis, did significantly decrease the amount of uptake. These studies show that the uptake of cystatin C by melanoma cells is through a selective endocytotic pathway that is most likely receptor mediated.

Keywords: Cystatin C, Endocytosis


Presentation Type: Poster

Session: 8-5
Location: SUB-GEO
Time: 4:15

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