Abstract
Immunoglobulin G (IgG) from human aneurysmal aorta was used to partially purify an aortic protein with an apparent MW approximately 80 kDa. Amino acid sequencing of a tryptic digest revealed two sequences with homology to mouse tenascin-X. The autoimmune IgG was then shown to react with purified human tenascin, and a rabbit polyclonal anti-human tenascin antibody was found to react with the purified autoantigen. These observations suggest that the autoantigen of abdominal aortic aneurysm disease may be homologous to a calcium-binding member of the tenascin superfamily that has been identified by others in pig and cow.
MeSH terms
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Amino Acid Sequence
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Animals
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Aorta / chemistry
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Aorta / metabolism*
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Aortic Aneurysm, Abdominal / immunology*
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Autoantigens / chemistry*
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Autoantigens / isolation & purification
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Blotting, Western
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Cattle
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Chromatography, High Pressure Liquid
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Contractile Proteins / chemistry*
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Contractile Proteins / isolation & purification
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Elastic Tissue
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Extracellular Matrix Proteins / chemistry
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Humans
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Immunoglobulin G / chemistry*
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Immunoglobulin G / isolation & purification
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Mass Spectrometry
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Mice
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Molecular Sequence Data
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Molecular Weight
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Muscle, Smooth, Vascular / chemistry
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Muscle, Smooth, Vascular / metabolism
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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RNA Splicing Factors
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Sequence Homology, Amino Acid
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Tenascin*
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Trypsin
Substances
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Autoantigens
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Contractile Proteins
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Extracellular Matrix Proteins
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Immunoglobulin G
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Peptide Fragments
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RNA Splicing Factors
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Tenascin
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microfibrillar protein
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tenascin X
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Trypsin