Effects of VIP and VIP-DAP on proliferation and lipid peroxidation metabolism in human KB cells

被引:3
作者
Caraglia, Michele
Dicitore, Alessandra
Giuberti, Gaia
Cassese, Diana
Lepretti, Marilena
Carteni, Maria
Abbruzzese, Alberto
Stiuso, Paola
机构
[1] Univ Naples 2, Dipartimento Biochim & Biofis, I-80138 Naples, Italy
[2] Univ Naples 2, Dept Sperimental Med, I-80138 Naples, Italy
[3] Natl Canc Inst, Fdn G Pascale, Dept Expt Oncol, Expt Pharmacol Unit, I-80131 Naples, Italy
来源
VIP, PACAP, AND RELATED PEPTIDES: FROM GENE TO THERAPY | 2006年 / 1070卷
关键词
limited proteolysis; vasoactive intestinal peptide; vasoactive intestinal peptide analogs; conformational analysis; intracellular lipid peroxidation; cell cycle modulation;
D O I
10.1196/annals.1317.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the present study, we have utilized the transglutaminase (TGase) enzyme to modify the primary structure of VIP with diamminopropane (DAP) at the level of the Gln16. We have investigated the conformational stability of VIP and VIP-DAP in solution by limited proteolysis experiments. The VIP-DAP appears to be more resistant to the proteolytic attack of trypsin, thus indicating that the derivatization in position 16 is able to stabilize the structure of the peptide. However, we have studied their role in cell cycle modulation and antioxidant activity in the oropharyngeal epidermoid carcinoma KB cells.
引用
收藏
页码:167 / 172
页数:6
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