| Literature DB >> 19696023 |
Masaya Ono1, Junichi Matsubara, Kazufumi Honda, Tomohiro Sakuma, Tomoyo Hashiguchi, Hiroshi Nose, Shoji Nakamori, Takuji Okusaka, Tomoo Kosuge, Naohiro Sata, Hideo Nagai, Tatsuya Ioka, Sachiko Tanaka, Akihiko Tsuchida, Tatsuya Aoki, Masashi Shimahara, Yohichi Yasunami, Takao Itoi, Fuminori Moriyasu, Ayako Negishi, Hideya Kuwabara, Ayako Shoji, Setsuo Hirohashi, Tesshi Yamada.
Abstract
Plasma proteome analysis requires sufficient power to compare numerous samples and detect changes in protein modification, because the protein content of human samples varies significantly among individuals, and many plasma proteins undergo changes in the bloodstream. A label-free proteomics platform developed in our laboratory, termed "Two-Dimensional Image Converted Analysis of Liquid chromatography and mass spectrometry (2DICAL)," is capable of these tasks. Here, we describe successful detection of novel prolyl hydroxylation of alpha-fibrinogen using 2DICAL, based on comparison of plasma samples of 38 pancreatic cancer patients and 39 healthy subjects. Using a newly generated monoclonal antibody 11A5, we confirmed the increase in prolyl-hydroxylated alpha-fibrinogen plasma levels and identified prolyl 4-hydroxylase A1 as a key enzyme for the modification. Competitive enzyme-linked immunosorbent assay of 685 blood samples revealed dynamic changes in prolyl-hydroxylated alpha-fibrinogen plasma level depending on clinical status. Prolyl-hydroxylated alpha-fibrinogen is presumably controlled by multiple biological mechanisms, which remain to be clarified in future studies.Entities:
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Year: 2009 PMID： 19696023 PMCID： PMC2781450 DOI： 10.1074/jbc.M109.041749
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157