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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

Cited 56 time in Web of Science Cited 62 time in Scopus
Authors
Park, Soo-Jin; Yoon, Won-Gap; Song, Jin-Su; Jung, Hyun Sook; Kim, Chong Jai; Oh, Soo Young; Yoon, Bo Hyun; Jung, Guhung; Kim, Hie-Joon; Nirasawa, Takashi
Issue Date
2005-11-19
Publisher
Wiley-Blackwell
Citation
Proteomics. 2006 Jan;6(1):349-63.
Keywords
Amino Acid SequenceAmnion/*chemistryAmniotic Fluid/*chemistryBase SequenceCalgranulin A/isolation & purificationCalgranulin B/chemistry/isolation & purificationDNA PrimersElectrophoresis, Gel, Two-Dimensional/*methodsHumansMolecular Sequence Data*ProteomeSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/*methodsUreaplasma Infections/metabolism
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.
ISSN
1615-9853 (Print)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16294308

http://hdl.handle.net/10371/13502
DOI
https://doi.org/10.1002/pmic.200500084
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Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Obstetrics & Gynecology (산부인과전공)Journal Papers (저널논문_산부인과학전공)
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