title: [Amyloid typing from formalin-fixed paraffin-embedded tissues using LMD-LC-MS/MS system].
abstract: Amyloidosis is one of the protein conformational disorders in which normally soluble proteins accumulate insoluble amyloid fibrils, leading to severe organ dysfunction. To date, 30 different amyloidogenic proteins have been reported. Immunohistochemistry (IHC) is usually used to identify the amyloid precursor protein, but the results may be inconclusive owing to a loss of epitopes or small amounts of amyloid deposits, comprising unknown amyloidogenic protein. Recently, laser microdissection (LMD)-liquid chromatography tandem mass spectrometry (LC-MS/MS) has been used in a novel method to identify amyloid precursor protein from amyloid-laden formalin-fixed paraffin embedded (FFPE) tissues. We describe the usefulness of the system for amyloid typing in this report.
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Tasaki
authors.forename: Konen
authors.initials: K
authors.lastname: Obayashi
authors.forename: Mitsuharu
authors.initials: M
authors.lastname: Ueda
authors.forename: Yukio
authors.initials: Y
authors.lastname: Ando
mesh_terms: D000682:Amyloid / Q000032:analysis*; D000686:Amyloidosis / Q000175:diagnosis* / Q000378:metabolism; D005557:Formaldehyde; D006801:Humans; D061346:Laser Capture Microdissection / Q000379:methods*; D016612:Paraffin Embedding / Q000379:methods; D053719:Tandem Mass Spectrometry / Q000379:methods*
chemical_list: D000682:Amyloid; D005557:Formaldehyde