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This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Pierini, L. M. Articles by Maxfield, F. R. Search for Related Content PubMed PubMed Citation Articles by Pierini, L. M. Articles by Maxfield, F. R. Related Collections Focus on Hematology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, Vol. 95 No. 8 (April 15), 2000: pp. 2471-2480 Oriented endocytic recycling of 51 in motile neutrophils Lynda M. Pierini, Moira A. Lawson, Robert J. Eddy, Bill Hendey, and Frederick R. Maxfield From the Department of Biochemistry, Weill Medical College of Cornell University, New York, NY; Department of Dairy and Food Science, The Royal Veterinary and Agricultural University, Frederiksberg, Denmark; and Department of Pharmacology, Rush Medical College, Rush-Presbyterian-St. Luke's-Medical Center, Chicago, IL. During cell migration, integrin attachments to the substratum provide the means to generate the traction and force necessary to achieve locomotion. Once the cell has moved over these attachments, however, it is equally important that integrins detach from the substratum. The fate of integrins after detachment may include release from the cell, lateral diffusion across the cell surface, or endocytosis and redelivery to the cell surface. Polymorphonuclear neutrophils (PMNs) become stuck on the extracellular matrix proteins fibronectin and vitronectin when their intracellular free calcium concentration ([Ca++]i) is buffered. Taking advantage of this feature of PMN migration, we investigated the fate of integrins to differentiate among various models of migration. We demonstrate that 51, one of the fibronectin-binding integrins, is responsible for immobilization of [Ca++]i-buffered PMNs on fibronectin. We find that 5 and 1 are in endocytic vesicles in PMNs and that 5 colocalizes with a marker for an endocytic recycling compartment. When [Ca++]i is buffered, 5 and 1 become concentrated in clusters in the rear of the adherent cells, suggesting that [Ca++]i transients are required for 51 detachment from the substratum. Inhibition of 51 detachment by buffering [Ca++]i results in the depletion of 5 from both endocytic vesicles and the recycling compartment, providing compelling evidence that integrins are normally recycled by way of endocytosis and intracellular trafficking during cell migration. This model is further refined by our demonstration that the endocytic recycling compartment reorients to retain its localization just behind the leading lamella as PMNs migrate, indicating that membrane recycling during neutrophil migration has directionality. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: F. Shi and J. Sottile Caveolin-1-dependent {beta}1 integrin endocytosis is a critical regulator of fibronectin turnover J. Cell Sci., July 15, 2008; 121(14): 2360 - 2371. [Abstract] [Full Text] [PDF] H. H. N. Yan, D. D. Mruk, W. M. Lee, and C. Y. Cheng Blood-testis barrier dynamics are regulated by testosterone and cytokines via their differential effects on the kinetics of protein endocytosis and recycling in Sertoli cells FASEB J, June 1, 2008; 22(6): 1945 - 1959. [Abstract] [Full Text] [PDF] V. Nechyporuk-Zloy, P. Dieterich, H. Oberleithner, C. Stock, and A. 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