Murine tissue amyloid protein AA. NH2-terminal sequence identity with only one of two serum amyloid protein (ApoSAA) gene products.
Open Access
- 1 February 1984
- journal article
- Published by Rockefeller University Press in The Journal of Experimental Medicine
- Vol. 159 (2), 641-646
- https://doi.org/10.1084/jem.159.2.641
Abstract
Amyloid protein AA is the presumptive fragment of an acute phase serum apolipoprotein, apoSAA. Two major murine apoSAA isotypes (apoSAA1 and apoSAA2) have been identified. The NH2-terminal amino acid sequences of purified murine apoSAA1 and apoSAA2 have been examined and compared with that of murine amyloid protein AA. Our results indicate that apoSAA1 and apoSAA2 are separate gene products and that amyloid protein AA has NH2-terminal amino acid sequence identity with only one of these isotypes, namely apoSAA2.Keywords
This publication has 21 references indexed in Scilit:
- Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoproteinBiochemistry, 1982
- Amyloid protein SAA is associated with high density lipoprotein from human serum.Proceedings of the National Academy of Sciences, 1977
- Kinetics of serum amyloid protein A in casein-induced murine amyloidosis.JCI Insight, 1977
- Amyloid-Related Serum Protein SAA from Three Animal Species: Comparison with Human SAAThe Journal of Immunology, 1976
- Isolation and Partial Characterization of SAA—An Amyloid-Related Protein from Human SerumThe Journal of Immunology, 1976
- Mouse amyloid protein AA: Homology with nonimmunoglobulin protein of human and monkey amyloid substance.Proceedings of the National Academy of Sciences of the United States of America, 1976
- Variation with age and disease of an amyloid A protein-related serum component.JCI Insight, 1975
- The Complete Amino‐Acid Sequence of Non‐Immunolobulin Amyloid Fibril Protein AS in Rheumatoid ArthritisEuropean Journal of Biochemistry, 1974
- IMMUNOLOGIC STUDIES OF THE MAJOR NONIMMUNOGLOBULIN PROTEIN OF AMYLOIDThe Journal of Experimental Medicine, 1973
- Chemical classes of amyloid substance.1971