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Generation of Amyloid A Protein by the Cell Lines from Amyloid‐Susceptible and ‐Resistant Mice
Author(s) -
Ham D.,
Skoryna S. C.
Publication year - 2004
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.0300-9475.2004.01361.x
Subject(s) - amyloidosis , amyloid (mycology) , clearance , serum amyloid a , incubation , chemistry , cell culture , serum amyloid p component , microbiology and biotechnology , incubation period , amyloid precursor protein , serum amyloid a protein , amyloid β , macrophage , biochemistry , immunology , biology , in vitro , medicine , alzheimer's disease , c reactive protein , genetics , disease , urology , inorganic chemistry , inflammation
It has been proposed that impaired degradation is the cause of amyloid A (AA) formation in reactive amyloidosis (Ham et al ., Scand J Immunol 1997; 45: 354–60). The current SDS‐PAGE of the culture medium showed that the macrophage cell line from the amyloid‐susceptible mouse strain (ANA1) degraded amyloid precursor protein serum amyloid A into the AA‐like amyloidogenic product of approximately 8.6 kDa but went no further, whereas cells from the resistant strain (A/J10) cleared the AA‐like derivates proceeding to approximately 7.7 kDa products within the incubation period. Degradation occurred in the chemically defined medium at a slower rate than in the medium with serum. This may imply that a lack of the serum components as well as impaired degradation could contribute to the development of amyloidosis.