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Proteome analysis of human amnion and amniotic fluid by two‐dimensional electrophoresis and matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry
Author(s) -
Park SooJin,
Yoon WonGap,
Song JinSu,
Jung Hyun Sook,
Kim Chong Jai,
Oh Soo Young,
Yoon Bo Hyun,
Jung Guhung,
Kim HieJoon,
Nirasawa Takashi
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500084
Subject(s) - amnion , amniotic fluid , proteome , proteomics , mass spectrometry , biology , chemistry , andrology , bioinformatics , chromatography , medicine , biochemistry , pregnancy , fetus , genetics , gene
Abstract Proteome analysis by 2‐DE and PMF by MALDI‐TOF MS was performed on human amnion and amniotic fluid at term. Ninety‐two soluble and nineteen membrane proteins were identified from amnion. Thirty‐five proteins were identified from amniotic fluid. Calgranulin A and B were found in all patients infected with Ureaplasma urealyticum , but not in any of the patients without infection, indicating that they are potential markers of intrauterine infection. Identity of calgranulin A and B was confirmed by MALDI‐TOF/TOF MS. This study represents the first extensive analysis of the human amnion and amniotic fluid proteome at term and demonstrates that 2‐DE and MALDI‐TOF MS is a useful tool for identifying clinically significant biomarkers of problematic pregnancies.