HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pimental, R. A. Articles by Carson, D. D. Search for Related Content PubMed PubMed Citation Articles by Pimental, R. A. Articles by Carson, D. D. Social Bookmarking                      What's this?

Volume 271, Number 45, Issue of November 8, 1996 pp. 28128-28137
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Synthesis and Intracellular Trafficking of Muc-1 and Mucins by Polarized Mouse Uterine Epithelial Cells

(Received for publication, April 30, 1996, and in revised form, July 29, 1996)

Ruth A. Pimental , Joanne Julian , Sandra J. Gendler ^§ and Daniel D. Carson

From the  Department of Biochemistry and Molecular Biology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030 and the ^§ Mayo Clinic, Scottsdale, Arizona 85259

Mucins function as a protective layer rendering the apical surface of epithelial cells nonadhesive to a variety of microorganisms and macromolecules. Muc-1 is a transmembrane mucin expressed at the apical cell surface of mouse uterine epithelial cells (UEC) that disappears as UEC become receptive for embryo implantation (Surveyor, G. A., Gendler, S. J., Pemberton, L., Das, S. K., Chakraborty, I., Julian, J., Pimental, R. A., Wegner, C. W., Dey, S. K., and Carson, D. D. (1995) Endocrinology 136, 3639-3647). In the present study, the kinetics of Muc-1 assembly, cell surface expression, release, and degradation were examined in polarized mouse UEC in vitro. Mucins were identified as the predominant glycoconjugates synthesized, apically expressed, and vectorially released in both wild-type and Muc-1 null mice. When mucins were released, greater than 95% were directed to the apical compartment. Approximately half of the cell-associated mucins lost during a 24-h period were found in the apical compartment. Vectorial biotinylation detected apically disposed, cell-surface mucin and indicated that at least 34% of these mucins are released apically within 24 h. This suggests that release of mucin ectodomains is part of the mechanism of mucin removal from the apical cell surface of UEC. The half-lives of total cell-associated mucins and Muc-1 were 19.5 ± 1 and 16.5 ± 0.8 h, respectively. Muc-1 represented approximately 10% of the [³H]glucosamine-labeled, cell-associated mucins. Studies of the kinetics of intracellular transport of Muc-1 indicated transit times of 21 ± 15 min from the rough endoplasmic reticulum to Golgi apparatus and 111 ± 28 min from the Golgi apparatus to the cell surface. Collectively, these studies provide the first comprehensive description of Muc-1 and mucin maturation, metabolism, and release by polarized cells, as well as defining a major metabolic fate for mucins expressed by UEC. Normal metabolic processing appears to be sufficient to account for the removal of Muc-1 protein during the transition of UEC to a receptive state.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				P. Wang, J. A Julian, and D. D Carson The MUC1 HMFG1 Glycoform Is a Precursor to the 214D4 Glycoform in the Human Uterine Epithelial Cell Line, HES Biol Reprod, February 1, 2008; 78(2): 290 - 298. [Abstract] [Full Text] [PDF]

				N. Moniaux, W. M. Junker, A. P. Singh, A. M. Jones, and S. K. Batra Characterization of Human Mucin MUC17: COMPLETE CODING SEQUENCE AND ORGANIZATION J. Biol. Chem., August 18, 2006; 281(33): 23676 - 23685. [Abstract] [Full Text] [PDF]

				A. Thathiah, C. P. Blobel, and D. D. Carson Tumor Necrosis Factor-alpha Converting Enzyme/ADAM 17 Mediates MUC1 Shedding J. Biol. Chem., January 24, 2003; 278(5): 3386 - 3394. [Abstract] [Full Text] [PDF]

				J. Julian, S. K. Das, S. K. Dey, D. Baraniak, V.-T. Ta, and D. D. Carson Expression of Heparin/Heparan Sulfate Interacting Protein/Ribosomal Protein L29 During the Estrous Cycle and Early Pregnancy in the Mouse Biol Reprod, April 1, 2001; 64(4): 1165 - 1175. [Abstract] [Full Text]

				M.M. French, S.E. Smith, K. Akanbi, T. Sanford, J. Hecht, M.C. Farach-Carson, and D.D. Carson Expression of the Heparan Sulfate Proteoglycan, Perlecan, during Mouse Embryogenesis and Perlecan Chondrogenic Activity In Vitro J. Cell Biol., May 31, 1999; 145(5): 1103 - 1115. [Abstract] [Full Text] [PDF]

				L. H. Hoffman, G. E. Olson, D. D. Carson, and B. S. Chilton Progesterone and Implanting Blastocysts Regulate Muc1 Expression in Rabbit Uterine Epithelium Endocrinology, January 1, 1998; 139(1): 266 - 271. [Abstract] [Full Text] [PDF]

				M. Jareb and G. Banker Inhibition of Axonal Growth by Brefeldin A in Hippocampal Neurons in Culture J. Neurosci., December 1, 1997; 17(23): 8955 - 8963. [Abstract] [Full Text] [PDF]