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Blood, 15 March 2004, Vol. 103, No. 6, pp. 2369-2376. Prepublished online as a Blood First Edition Paper on November 13, 2003; DOI 10.1182/blood-2003-09-3050. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-09-3050v1 103/6/2369    most recent 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 Ghosh, S. Articles by Chuck, S. L. Search for Related Content PubMed PubMed Citation Articles by Ghosh, S. Articles by Chuck, S. L. Related Collections Red Cells Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Regulated secretion of glycosylated human ferritin from hepatocytes Sharmistha Ghosh, Sarah Hevi, and Steven L. Chuck From the Molecular Medicine Unit, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA. Serum ferritin has been used widely in clinical medicine chiefly as an indicator of iron stores and inflammation. Circulating ferritin also can have paracrine effects. Despite the clinical significance of serum ferritin, its secretion remains an enigma. The consensus view is that serum ferritin arises from tissue ferritins— principally ferritin light—which can be glycosylated. Ferritin heavy and light chains are cytosolic proteins that form cages of 24 subunits to store intracellular iron. We show that ferritin light is secreted when its expression is increased in stable, transfected HepG2 cells or adenovirus-infected HepG2 cells. Export occurs through the classical secretory pathway and some chains are N-glycosylated. Ferritins do not need to form cages prior to secretion. Secretion is blocked specifically, effectively, and rapidly by a factor in serum. The timing of this inhibition of ferritin secretion suggests that normally cytosolic ferritin L is targeted to the secretory pathway during translation despite the absence of a conventional signal sequence. Thus, secretion of glycosylated and unglycosylated ferritin is a regulated and not a stochastic process. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: T. V. Adamkiewicz, M. R. Abboud, C. Paley, N. Olivieri, M. Kirby-Allen, E. Vichinsky, J. F. Casella, O. A. Alvarez, J. C. Barredo, M. T. Lee, et al. Serum ferritin level changes in children with sickle cell disease on chronic blood transfusion are nonlinear and are associated with iron load and liver injury Blood, November 19, 2009; 114(21): 4632 - 4638. [Abstract] [Full Text] [PDF] C. Kannengiesser, A.-M. Jouanolle, G. Hetet, A. Mosser, F. Muzeau, D. Henry, E. Bardou-Jacquet, M. Mornet, P. Brissot, Y. Deugnier, et al. A new missense mutation in the L ferritin coding sequence associated with elevated levels of glycosylated ferritin in serum and absence of iron overload Haematologica, March 1, 2009; 94(3): 335 - 339. [Abstract] [Full Text] [PDF] D. Ferring-Appel, M. W. Hentze, and B. Galy Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism Blood, January 15, 2009; 113(3): 679 - 687. [Abstract] [Full Text] [PDF] F. Missirlis, S. Kosmidis, T. Brody, M. Mavrakis, S. Holmberg, W. F. Odenwald, E. M. C. Skoulakis, and T. A. Rouault Homeostatic Mechanisms for Iron Storage Revealed by Genetic Manipulations and Live Imaging of Drosophila Ferritin Genetics, September 1, 2007; 177(1): 89 - 100. [Abstract] [Full Text] [PDF] P. R. Wilker, J. R. Sedy, V. Grigura, T. L. Murphy, and K. M. Murphy Evidence for carbohydrate recognition and homotypic and heterotypic binding by the TIM family Int. Immunol., June 1, 2007; 19(6): 763 - 773. [Abstract] [Full Text] [PDF] J M van de Kamp, D J Lefeber, G J G Ruijter, S J Steggerda, N S den Hollander, S M Willems, G Matthijs, B J H M Poorthuis, and R A Wevers Congenital disorder of glycosylation type Ia presenting with hydrops fetalis J. Med. Genet., April 1, 2007; 44(4): 277 - 280. [Abstract] [Full Text] [PDF] C.-H. Yang, J. Szeliga, J. Jordan, S. Faske, Z. Sever-Chroneos, B. Dorsett, R. E. Christian, R. E. Settlage, J. Shabanowitz, D. F. Hunt, et al. Identification of the Surfactant Protein A Receptor 210 as the Unconventional Myosin 18A J. Biol. Chem., October 14, 2005; 280(41): 34447 - 34457. [Abstract] [Full Text] [PDF] P. Maciel, V. T. Cruz, M. Constante, I. Iniesta, M. C. Costa, S. Gallati, N. Sousa, J. Sequeiros, P. Coutinho, and M. M. Santos Neuroferritinopathy: Missense mutation in FTL causing early-onset bilateral pallidal involvement Neurology, August 23, 2005; 65(4): 603 - 605. [Abstract] [Full Text] [PDF]

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