Identification of two novel amyloid A protein subsets coexisting in an individual patient of AA-amyloidosis |
| |
Authors: | Satoshi Baba Toshie Takahashi Takeshi Kasama Haruyuki Shirasawa |
| |
Institution: | 1. Second Department of Pathology, Hamamatsu University School of Medicine, Hamamatsu-ski, Shizuoka Japan;2. Second Department of Biochemistry, Faculty of Medicine, University of Tokyo, Bunkyo-ku, Tokyo Japan;3. Laboratory for Biomedical Analysis, Tokyo Medical and Dental University, Bunkyo-ku, Tokyo Japan |
| |
Abstract: | Amyloid A protein (AA), the major fibril protein in AA-amyloidosis, is an N-terminal cleavage product of the precursor protein, serum amyloid A (SAA). Using mass spectrometry and amino-acid sequencing, we identified and characterized two novel AA protein subsets co-deposited as amyloid fibrils in an patient having AA-amyloidosis associated with rheumatoid arthritis. One of the AA proteins corresponded to positions 2–76 (or 75) of SAA2α and the other corresponded to positions 2–76 (or 75) of known SAA1 subsets, except for position 52 or 57, where SAA1α has valine and alanine and SAA1β has alanine and valine in position 52 and 57, respectively, whereas the AA protein had alanine at the both positions. Our findings (1), demonstrate that not only one but two SAA subsets could be deposited together as an AA-amyloid in a single individual and (2), support the existence of a novel SAA1 allotype, i.e., SAA152,57Ala. |
| |
Keywords: | Amyloid A protein Serum amyloid A protein Rheumatoid arthritis Amino acid sequence Mass spectrometry AA amyloid A protein SAA serum amyloid A protein HDL high-density lipoprotein LC/FAB-MS liquid chromatography/fast atom bombardment-mass spectrometry |
本文献已被 ScienceDirect 等数据库收录! |
|