The Distribution of Synaptotagmin II in RBL-2H3 and Its Regulation on Exocytosis of Lysosomes in RBL-2H3

被引：0

作者：

Zhang, Jicheng ^{[1
]}

Wu, Jianmin ^{[1
]}

Pan, Shixiu ^{[1
]}

Lv, Wenli ^{[2
]}

机构：

[1] Huazhong Univ Sci & Technol, Tongji Med Coll, Dept Lab Med, Union Hosp, Wuhan 430022, Peoples R China

[2] Wuhan Inst Biol Prod, Wuhan 430060, Peoples R China

来源：

CELLULAR & MOLECULAR IMMUNOLOGY | 2005年 / 2卷 / 03期

基金：

中国国家自然科学基金;

关键词：

calcium binding protein; mast cell; gene expression; lysosome; exocytosis;

D O I：

暂无

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Synaptotagmin (Syt) constitutes a family of membrane-trafficking proteins, so far nearly 20 Syts have been discovered. Extensive work showed that synatotagmins were a potential Ca2+ sensor for regulated exocytosis. This study was to investigate the expression and location of synaptotagmin II (Syt2) in RBL-2H3 (RBL) and its role in regulating exocytosis of RBL. The expression of Syt2 in RBL was confirmed by Western blot. The recombinant expression vector pEGFP-N1-Syt2 was constructed and transfected into RBL by electroporation, the stable transfectant RBL-Syt2-S expressing fusion protein Syt2-EGFP were obtained and Syt2 was highly concentrated at plasma membrane with little detected in cytoplasm. To analyze the role of Syt2 during exocytosis of RBL, the release of cathepsin D was assayed by immunoblotting. Compared with control, the release of cathepsin D by RBL-Syt2-S was markedly decreased. The results indicated that Syt2 played a negative regulation in exocytosis of lysosomes in RBL.

引用

页码：205 / 209

页数：5

共 14 条

[1] Synaptotagmin regulates mast cell functions [J].

Baram, D ;

Mekori, YA ;

Sagi-Eisenberg, R .

IMMUNOLOGICAL REVIEWS, 2001, 179 :25-34

[2] Synaptotagmin gene content of the sequenced genomes [J].

Craxton, M .

BMC GENOMICS, 2004, 5 (1)

[3] The C2B domain of synaptotagmin is a Ca2+-sensing module essential for exocytosis [J].

Desai, RC ;

Vyas, B ;

Earles, CA ;

Littleton, JT ;

Kowalchyck, JA ;

Martin, TFJ ;

Chapman, ER .

JOURNAL OF CELL BIOLOGY, 2000, 150 (05) :1125-1135

[4] Synaptotagmin I functions as a calcium regulator of release probability [J].

Fernández-Chacón, R ;

Königstorfer, A ;

Gerber, SH ;

García, J ;

Matos, MF ;

Stevens, CF ;

Brose, N ;

Rizo, J ;

Rosenmund, C ;

Südhof, TC .

NATURE, 2001, 410 (6824) :41-49

[5] RNA interference-mediated silencing of synaptotagmin IX, but not synaptotagmin I, inhibits dense-core vesicle exocytosis but not in PC12 cells [J].

Fukuda, M .

BIOCHEMICAL JOURNAL, 2004, 380 :875-879

[6] The C terminus of SNAP25 is essential for Ca2+-dependent binding of synaptotagmin to SNARE complexes [J].

Gerona, RRL ;

Larsen, EC ;

Kowalchyk, JA ;

Martin, TFJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (09) :6328-6336

[7] Synaptotagmin IV overexpression inhibits depolarization-induced exocytosis in PC12 cells [J].

Machado, HB ;

Liu, W ;

Vician, LJ ;

Herschman, HR .

JOURNAL OF NEUROSCIENCE RESEARCH, 2004, 76 (03) :334-341

[8] Synaptotagmins in membrane traffic:: Which vesicles do the tagmins tag? [J].

Marquèze, B ;

Berton, F ;

Seagar, M .

BIOCHIMIE, 2000, 82 (05) :409-420

[9] Cutting edge:: Transmembrane phosphoprotein Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched microdomains as a negative feedback regulator of mast cell signaling through the FcεRI [J].

Ohtake, H ;

Ichikawa, N ;

Okada, M ;

Yamashita, T .

JOURNAL OF IMMUNOLOGY, 2002, 168 (05) :2087-2090

[10] Synaptotagmins:: Why so many? [J].

Südhof, TC .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (10) :7629-7632

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