FAD-linked sulfhydryl oxidase QSOX: Topographic, cellular, and subcellular immunolocalization in adult rat central nervous system

被引:35
作者
Mairet-Coello, G
Tury, A
Esnard-Feve, A
Fellmann, D
Risold, PY
Griffond, B
机构
[1] Univ Franche Comte, Histol Lab, Equipe Estrogenes Express Gen & Pathol Syst Nerve, Fac Med & Pharm, F-25041 Besancon, France
[2] Univ Tours, Fac Med, INSERM, EMIU 0010,Lab Enzymol & Chim Prot, F-37032 Tours, France
关键词
brain; disulfide bond; immunohistochemistry; oxidative stress; rQSOX;
D O I
10.1002/cne.20126
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The distribution of the sulfhydryl oxidase QSOX in the rat brain was mapped using immunohistochemistry. QSOX is specifically expressed by neurons throughout the rostrocaudal extent of the brain as well as in the spinal cord. Although a majority of neurons express QSOX, different intensities of labeling were observed depending on the area: the strongest labeling was observed in the olfactory bulbs, isocortex, hippocampus, basal telencephalon, several thalamic and hypothalamic nuclei, cerebellum, and numerous brainstem nuclei. This study also describes the ultrastructural localization of QSOX in neuronal cells and demonstrates that the enzyme is associated with the Golgi apparatus. Finally, selected double immunohistochemistry showed that in the hypothalamus the highest levels of QSOX labeling were colocalized in neuron populations that express disulfide-bounded neuropeptides. These observations are consistent with a role of the enzyme in secreted peptide/protein folding. Data presented herein will serve as a basis for further investigations of the physiological function of QSOX in the central nervous system. (C) 2004 Wiley-Liss, Inc.
引用
收藏
页码:334 / 363
页数:30
相关论文
共 44 条
[1]   Rat seminal vesicle FAD-dependent sulfhydryl oxidase -: Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family [J].
Benayoun, B ;
Esnard-Fève, A ;
Castella, S ;
Courty, Y ;
Esnard, F .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (17) :13830-13837
[2]   An evaluation of the role of mitochondria in neurodegenerative diseases: mitochondrial mutations and oxidative pathology, protective nuclear responses, and cell death in neurodegeneration [J].
Cassarino, DS ;
Bennett, JP .
BRAIN RESEARCH REVIEWS, 1999, 29 (01) :1-25
[3]   EPIDIDYMAL SULFHYDRYL OXIDASE - SPERM-PROTECTIVE ENZYME FROM MALE REPRODUCTIVE-TRACT [J].
CHANG, TSK ;
MORTON, B .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1975, 66 (01) :309-315
[4]   DISTRIBUTION OF SULFHYDRYL OXIDASE ACTIVITY IN RAT AND HAMSTER MALE REPRODUCTIVE-TRACT [J].
CHANG, TSK ;
ZIRKIN, BR .
BIOLOGY OF REPRODUCTION, 1978, 18 (05) :745-748
[5]   PURIFICATION AND PROPERTIES OF SULFHYDRYL OXIDASE FROM BOVINE PANCREAS [J].
CLARE, DA ;
PINNIX, IB ;
LECCE, JG ;
HORTON, HR .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1988, 265 (02) :351-361
[6]   Regulation of the quiescence-induced genes: Quiescin Q6, decorin, and ribosomal protein S29 [J].
Coppock, D ;
Kopman, C ;
Gudas, J ;
Cina-Poppe, DA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 269 (02) :604-610
[7]  
COPPOCK DL, 1993, CELL GROWTH DIFFER, V4, P483
[8]   The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: Thioredoxin and ERV1 [J].
Coppock, DL ;
Cina-Poppe, D ;
Gilleran, S .
GENOMICS, 1998, 54 (03) :460-468
[9]   Antioxidants, oxidative stress, and degenerative neurological disorders [J].
Floyd, RA .
PROCEEDINGS OF THE SOCIETY FOR EXPERIMENTAL BIOLOGY AND MEDICINE, 1999, 222 (03) :236-245
[10]   Pathways for protein disulphide bond formation [J].
Frand, AR ;
Cuozzo, JW ;
Kaiser, CA .
TRENDS IN CELL BIOLOGY, 2000, 10 (05) :203-210