The normal human amniotic fluid supernatant Proteome

被引:0
|
作者
Tsangaris, George T. [1 ]
Kolialexi, Ageliki
Karamessinis, Panagiotis M.
Anagnostopoulos, Athanasios K.
Antsaklis, Aris
Fountoulakis, Michael
Mavrou, Ariadni
机构
[1] Acad Athens, Fdn Biomed Res, Ctr Basic Res, Div Biotechnol,Genom Unit, Athens, Greece
[2] Univ Athens, Sch Med, Dept Obstet & Gynecol 1, GR-10679 Athens, Greece
来源
IN VIVO | 2006年 / 20卷 / 04期
关键词
amniotic fluid supernatant; proteomics; two-dimensional protein database; mass spectrometry;
D O I
暂无
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
Proteomic analysis combining two-dimentional electrophoresis (2DE) and mass spectrometry (MS) has the potential for a wide range of applications in biological and medical sciences, as protein screening in tissues obtained from healthy and diseased conditions can determine drug targets and diagnostic markers. Conventionally, amniotic fluid (AF) samples are routinely used for prenatal diagnosis of a wide range of fetal abnormalities. Proteomics have already been applied in the analysis of tissues from fetuses with Down's syndrome, in order to detect differences in their protein profile as compared to the normal profiles and to determine possible diagnostic tools. A detailed protein 2DE for the normal human AF has not been reported. In the present study, the 2D protein database of the normal human AF supernatant (AFS) was constructed. Ten AFS samples from women carrying normal fetuses were analysed by 2DE. A mean of 412 spots per gel were analyzed and protein identification was carried out by MALDI-MS and MALDI-MS-MS. A 2D protein map comprising of 136 different gene products was constructed. The majority of the identified proteins are regulatory proteins, enzymes, secreted proteins, carriers and immunoglobulins. Twelve hypothetical proteins were also included. The normal AFS proteome map is a valuable tool for the study of aberrant protein expression and the search for proteins as possible markers for the prediction of abnormal fetuses.
引用
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页码:479 / 490
页数:12
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