Expression of the secreted FAD-dependent sulfydryl oxidase (QSOX) in the guinea pig central nervous system

被引:17
作者
Amiot, C
Musard, JF
Hadjiyiassemis, M
Jouvenot, M
Fellmann, D
Risold, PY
Adami, P
机构
[1] Fac Med & Pharm, Lab Histol Embryol, F-25030 Besancon, France
[2] UFR Sci & Tech, Lab Biochim Biol Mol, Lille, France
来源
MOLECULAR BRAIN RESEARCH | 2004年 / 125卷 / 1-2期
关键词
sulfydryl oxidase; disulfide bond; oxidative stress; Quiescin;
D O I
10.1016/j.molbrainres.2004.02.024
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
cpQSOx1 is a member of the QSOx family of proteins, expressed in the guinea pig (Cavia porcellus) and ortholog of the rat rQSOx1. In this study, in vitro experiments were conducted and showed that, as other member of this family, cpQSOx1 has a sulfydryl oxidase activity, and is a secreted protein. Then, the expression of this enzyme was researched in the guinea pig brain, as very little information exists yet on the expression of QSOx family members in the central nervous system. By immunohistochemistry, RT-PCR and in situ hybridization, cpQSOx1 is synthesized by neurons throughout the whole guinea pig central nervous system. Reticular structures as the basal forebrain, reticular thalamic nucleus and reticular nuclei of the brainstem contained the densest labeling. These results are discussed in terms of putative roles of this protein in synaptic strengthening and in redox activities. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:13 / 21
页数:9
相关论文
共 17 条
  • [1] [Anonymous], 1998, CENTRAL NERVOUS SYST
  • [2] Rat seminal vesicle FAD-dependent sulfhydryl oxidase -: Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family
    Benayoun, B
    Esnard-Fève, A
    Castella, S
    Courty, Y
    Esnard, F
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (17) : 13830 - 13837
  • [3] INSITU HYBRIDIZATION HISTOCHEMISTRY FOR THE ANALYSIS OF GENE-EXPRESSION IN THE ENDOCRINE AND CENTRAL-NERVOUS-SYSTEM TISSUES - A 3-YEAR EXPERIENCE
    BLOCH, B
    POPOVICI, T
    LEGUELLEC, D
    NORMAND, E
    CHOUHAM, S
    GUITTENY, AF
    BOHLEN, P
    [J]. JOURNAL OF NEUROSCIENCE RESEARCH, 1986, 16 (01) : 183 - 200
  • [4] CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
  • [5] Regulation of the quiescence-induced genes: Quiescin Q6, decorin, and ribosomal protein S29
    Coppock, D
    Kopman, C
    Gudas, J
    Cina-Poppe, DA
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 269 (02) : 604 - 610
  • [6] TISSUE SULFHYDRYL GROUPS
    ELLMAN, GL
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1959, 82 (01) : 70 - 77
  • [7] Yeast Erv2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family
    Gerber, J
    Mühlenhoff, U
    Hofhaus, G
    Lill, R
    Lisowsky, T
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (26) : 23486 - 23491
  • [8] Sulfhydryl oxidase from egg white - A facile catalyst for disulfide bond formation in proteins and peptides
    Hoober, KL
    Sheasley, SL
    Gilbert, HF
    Thorpe, C
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (32) : 22147 - 22150
  • [9] Development of cDNA microarray for expression profiling of estrogen-responsive genes
    Inoue, A
    Yoshida, N
    Omoto, Y
    Oguchi, S
    Yamori, T
    Kiyama, R
    Hayashi, S
    [J]. JOURNAL OF MOLECULAR ENDOCRINOLOGY, 2002, 29 (02) : 175 - 192
  • [10] SULFHYDRYL OXIDASE-CATALYZED FORMATION OF DISULFIDE BONDS IN REDUCED RIBONUCLEASE
    JANOLINO, VG
    SWAISGOOD, HE
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1987, 258 (01) : 265 - 271