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J. Biol. Chem., Vol. 275, Issue 21, 15948-15954, May 26, 2000
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From the U38 INSERM, Faculté de Médecine,
Université de la Méditerranée,
13385 Marseille cedex 5, France
Human thyroperoxidase (hTPO), a type I
transmembrane glycoprotein, plays a key role in thyroid hormone
synthesis. In a previous paper (Fayadat, L., Niccoli, P., Lanet, J.,
and Franc, J. L. (1998) Endocrinology 139, 4277-4285)
we established that after the synthesis, only 15-20% of the hTPO
molecules were recognized by a monoclonal antibody (mAb15) directed
against a conformational structure and that only 2% were able to reach
the cell surface. In the present study using pulse-chase experiments in
the presence or absence of protease inhibitors followed by
immunoprecipitation procedures with monoclonal antibodies recognizing
unfolded or partially folded hTPO forms we show that: (i) unfolded hTPO
forms are degraded by the proteasome and (ii) partially folded hTPO
forms are degraded by other proteases. It was also established upon
incubating endoplasmic reticulum (ER) membranes in vitro
that the degradation of the partially folded hTPO was carried out by
serine and cysteine integral ER membrane proteases. These data provide
valuable insights into the quality control mechanisms whereby the cells
get rid of misfolded or unfolded proteins. Moreover, this is the first
study describing a protein degradation process involving two distinct
degradation pathways (proteasome and ER cysteine/serine proteases) at
the ER level, depending on the folding state of the protein.
Degradation of Human Thyroperoxidase in the Endoplasmic Reticulum
Involves Two Different Pathways Depending on the Folding State of the
Protein*
§,,
*
This work was supported by INSERM (U38) and by the
Association pour la Recherche sur le Cancer.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported during this work by the Association pour le
Developpement des Recherches Biologiques et Médicales.
§
Present address: Dept. of Biological Sciences, Stanford University,
Stanford, CA 94305-5020.
¶
To whom correspondence should be addressed: U38 INSERM,
Faculté de Médecine, 27 Bd J. Moulin, 13385 Marseille cedex
5, France. Tel.: 33-4-91-32-43-77; Fax: 33-4-91-79-65-11; E-mail:
jean-louis.franc@medecine.univ-mrs.fr.
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