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    Characterization of Laminin Binding Integrin Internalization in Prostate Cancer Cells

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    Name:
    Das_Characterization_Laminin.pdf
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    2.087Mb
    Format:
    PDF
    Description:
    Final Accepted Manuscript
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    Author
    Das, Lipsa
    Anderson, Todd A.
    Gard, Jaime M.C.
    Sroka, Isis C.
    Strautman, Stephanie R.
    Nagle, Raymond B.
    Morrissey, Colm
    Knudsen, Beatrice S.
    Cress, Anne E.
    Affiliation
    Cancer Biology Program, University of Arizona
    he University of Arizona Cancer Center, University of Arizona
    Department of Pharmacology, University of Arizona, Tucson
    Department of Molecular and Cellular Biology, University of Arizona
    Department of Pathology, University of Arizona
    Department of Cellular and Molecular Medicine, University of Arizona
    Issue Date
    2017-05
    Keywords
    INTEGRIN
    LAMININ
    INTERNALIZATION KINETICS
    ENDOSOMES
    PROSTATE CANCER
    
    Metadata
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    Publisher
    WILEY
    Citation
    Characterization of Laminin Binding Integrin Internalization in Prostate Cancer Cells 2017, 118 (5):1038 Journal of Cellular Biochemistry
    Journal
    Journal of Cellular Biochemistry
    Rights
    © 2016 Wiley Periodicals, Inc.
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    Laminin binding integrins 6 (CD49f) and 3 (CD49c) are persistently but differentially expressed in prostate cancer (PCa). Integrin internalization is an important determinant of their cell surface expression and function. Using flow cytometry, and first order kinetic modeling, we quantitated the intrinsic internalization rates of integrin subunits in a single cycle of internalization. In PCa cell line DU145, 6 integrin internalized with a rate constant (k(actual)) of 3.25min(-1), threefold faster than 3 integrin (1.0min(-1)), 1.5-fold faster than the vitronectin binding v integrin (CD51) (2.2min(-1)), and significantly slower than the unrelated transferrin receptor (CD71) (15min(-1)). Silencing of 3 integrin protein expression in DU145, PC3, and PC3B1 cells resulted in up to a 1.71-fold increase in k(actual) for 6 integrin. The internalized 6 integrin was targeted to early endosomes but not to lamp1 vesicles. Depletion of 3 integrin expression resulted in redistribution of 64 integrin to an observed cell-cell staining pattern that is consistent with a suprabasal distribution observed in epidermis and early PIN lesions in PCa. Depletion of 3 integrin increased cell migration by 1.8-fold, which was dependent on 61 integrin. Silencing of 6 integrin expression however, had no significant effect on the k(actual) of 3 integrin or its distribution in early endosomes. These results indicate that 3 and 6 integrins have significantly different internalization kinetics and that coordination exists between them for internalization. J. Cell. Biochem. 118: 1038-1049, 2017.
    Note
    12 month embargo; Accepted manuscript online: 10 August 2016
    ISSN
    07302312
    DOI
    10.1002/jcb.25673
    Version
    Final accepted manuscript
    Sponsors
    NIH [R01 CA 159406, CA 23074, CA 09213]
    Additional Links
    http://doi.wiley.com/10.1002/jcb.25673
    ae974a485f413a2113503eed53cd6c53
    10.1002/jcb.25673
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