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) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mezghrani, A. Articles by Miquelis, R. Search for Related Content PubMed PubMed Citation Articles by Mezghrani, A. Articles by Miquelis, R. Social Bookmarking                      What's this?

J Biol Chem, Vol. 275, Issue 3, 1920-1929, January 21, 2000

Protein-disulfide Isomerase (PDI) in FRTL5 Cells
pH-DEPENDENT THYROGLOBULIN/PDI INTERACTIONS DETERMINE A NOVEL PDI FUNCTION IN THE POST-ENDOPLASMIC RETICULUM OF THYROCYTES^*

Alexandre Mezghrani^§, Joel Courageot^§, Jean Claude Mani^¶, Martine Pugniere^¶, Paul Bastiani, and Raymond Miquelis

From the  Laboratoire de Biochimie, Ingénierie des Protéines, UMR 6560, Institut Fédératif Jean Roche, Université de la Méditerranée, Faculté de Médecine-Nord, Boulevard Pierre Dramard, 13916 Marseille Cedex 20 and ^¶ CNRS, UMR 9921, Faculté de Pharmacie, 15, avenue Charles Flahault, 34060 Montpellier Cedex 2, France

Thyroglobulin (TG) is secreted by the thyrocytes into the follicular lumen of the thyroid. After maturation and hormone formation, TG is endocytosed and delivered to lysosomes. Quality control mechanisms may occur during this bidirectional traffic since 1) several molecular chaperones are cosecreted with TG in vivo, and 2) lysosomal targeting of immature TG is thought to be prevented via the interaction, in acidic conditions, between the Ser⁷⁸⁹-Met¹¹⁷² TG hormonogenic domain (BD) and an unidentified membrane receptor. We investigated the secretion and cell surface expression of PDI and other chaperones in the FRTL5 thyroid cell line, and then studied the characteristics of the interaction between TG and PDI. We demonstrated that PDI, but also other chaperones such as calnexin and KDEL-containing proteins are exposed at the cell surface. We observed on living cells or membrane preparations that PDI specifically binds TG in acidic conditions, and that only BD is involved in binding. Surface plasmon resonance analysis of TG/PDI interactions indicated: 1) that PDI bound TG but only in acidic conditions, and that it preferentially recognized immature molecules, and 2) BD is involved in binding even if cysteine-rich modules are deleted. The notion that PDI acts as an "escort" for immature TG in acidic post-endoplasmic reticulum compartments is discussed.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				N. Myhill, E. M. Lynes, J. A. Nanji, A. D. Blagoveshchenskaya, H. Fei, K. Carmine Simmen, T. J. Cooper, G. Thomas, and T. Simmen The Subcellular Distribution of Calnexin Is Mediated by PACS-2 Mol. Biol. Cell, July 1, 2008; 19(7): 2777 - 2788. [Abstract] [Full Text] [PDF]

				R. T. Netea-Maier, S. W. Hunsucker, B. M. Hoevenaars, S. M. Helmke, P. J. Slootweg, A. R. Hermus, B. R. Haugen, and M. W. Duncan Discovery and Validation of Protein Abundance Differences between Follicular Thyroid Neoplasms Cancer Res., March 1, 2008; 68(5): 1572 - 1580. [Abstract] [Full Text] [PDF]

				M. Hinton, A. Gutsol, and S. Dakshinamurti Thromboxane hypersensitivity in hypoxic pulmonary artery myocytes: altered TP receptor localization and kinetics Am J Physiol Lung Cell Mol Physiol, March 1, 2007; 292(3): L654 - L663. [Abstract] [Full Text] [PDF]

				R. Barbouche, R. Miquelis, I. M. Jones, and E. Fenouillet Protein-disulfide Isomerase-mediated Reduction of Two Disulfide Bonds of HIV Envelope Glycoprotein 120 Occurs Post-CXCR4 Binding and Is Required for Fusion J. Biol. Chem., January 24, 2003; 278(5): 3131 - 3136. [Abstract] [Full Text] [PDF]

				T. A. Baldwin and H. L. Ostergaard The Protein-tyrosine Phosphatase CD45 Reaches the Cell Surface via Golgi-dependent and -independent Pathways J. Biol. Chem., December 20, 2002; 277(52): 50333 - 50340. [Abstract] [Full Text] [PDF]

				E. Sargsyan, M. Baryshev, L. Szekely, A. Sharipo, and S. Mkrtchian Identification of ERp29, an Endoplasmic Reticulum Lumenal Protein, as a New Member of the Thyroglobulin Folding Complex J. Biol. Chem., May 3, 2002; 277(19): 17009 - 17015. [Abstract] [Full Text] [PDF]

				M. Marino and R. T. McCluskey Role of thyroglobulin endocytic pathways in the control of thyroid hormone release Am J Physiol Cell Physiol, November 1, 2000; 279(5): C1295 - C1306. [Abstract] [Full Text] [PDF]

				F. Delom, B. Mallet, P. Carayon, and P.-J. Lejeune Role of Extracellular Molecular Chaperones in the Folding of Oxidized Proteins. REFOLDING OF COLLOIDAL THYROGLOBULIN BY PROTEIN DISULFIDE ISOMERASE AND IMMUNOGLOBULIN HEAVY CHAIN-BINDING PROTEIN J. Biol. Chem., June 8, 2001; 276(24): 21337 - 21342. [Abstract] [Full Text] [PDF]

				G. Angelini, S. Gardella, M. Ardy, M. R. Ciriolo, G. Filomeni, G. Di Trapani, F. Clarke, R. Sitia, and A. Rubartelli From the Cover: Antigen-presenting dendritic cells provide the reducing extracellular microenvironment required for T lymphocyte activation PNAS, February 5, 2002; 99(3): 1491 - 1496. [Abstract] [Full Text] [PDF]