Serum amyloid A protein in mink during endotoxin induced inflammation and amyloidogenesis. 1994

C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
Institute of Clinical Medicine, University of Tromsö, Norway.

Two-dimensional electrophoresis was used to study SAA and AA proteins in mink during lipopolysaccharide-induced inflammation and amyloidogenesis. Three isotypes, SAA pI 6.8 and SAA pI 6.5 (both SAA1-like), and SAA pI 6.0 (SAA1- and SAA2-like), were identified in serum after both single and multiple LPS injections. Total SAA serum levels were highest in the early phase of induction, followed by a decrease ranging from 1 to 50% of the peak value during the rest of the experiment. The variation in the total SAA levels correlated with the total SAA mRNA levels. Low total SAA levels were seen both in non-amyloidotic and amyloidotic animals, and a general decrease of all isotypes was demonstrated. In hepatic amyloid fibrils, several AA isotypes, with amino acid sequence homologous exclusively to that of SAA2, were found. In the corresponding splenic material, fragments of histones H2A and H2B constituted most of the low molecular mass proteins, and no protein AA was detected. In spite of low serum levels and a non-specific isotype removal, the results confirm that SAA2 is amyloidogenic in mink.

UI MeSH Term Description Entries
D007249 Inflammation A pathological process characterized by injury or destruction of tissues caused by a variety of cytologic and chemical reactions. It is usually manifested by typical signs of pain, heat, redness, swelling, and loss of function. Innate Inflammatory Response,Inflammations,Inflammatory Response, Innate,Innate Inflammatory Responses
D008070 Lipopolysaccharides Lipid-containing polysaccharides which are endotoxins and important group-specific antigens. They are often derived from the cell wall of gram-negative bacteria and induce immunoglobulin secretion. The lipopolysaccharide molecule consists of three parts: LIPID A, core polysaccharide, and O-specific chains (O ANTIGENS). When derived from Escherichia coli, lipopolysaccharides serve as polyclonal B-cell mitogens commonly used in laboratory immunology. (From Dorland, 28th ed) Lipopolysaccharide,Lipoglycans
D008107 Liver Diseases Pathological processes of the LIVER. Liver Dysfunction,Disease, Liver,Diseases, Liver,Dysfunction, Liver,Dysfunctions, Liver,Liver Disease,Liver Dysfunctions
D008297 Male Males
D008907 Mink Carnivores of genera Mustela and Neovison of the family MUSTELIDAE. The European mink has white upper and lower lips while the American mink lacks white upper lip. American Mink,European Mink,Mustela lutreola,Mustela macrodon,Mustela vison,Neovison vison,Sea Mink,Mink, American,Mink, European,Mink, Sea,Minks,Minks, Sea,Sea Minks,vison, Neovison
D005260 Female Females
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D000685 Serum Amyloid A Protein An ACUTE PHASE REACTION protein present in low concentrations in normal sera, but found at higher concentrations in sera of older persons and in patients with AMYLOIDOSIS. It is the circulating precusor of amyloid A protein, which is found deposited in AA type AMYLOID FIBRILS. Amyloid Protein SAA,Amyloid Serum Protein SAA,Serum A Related Protein,Amyloid A Precursor,Amyloid A Protein,Amyloid A Protein-Related Serum Component,Amyloid Fibril Protein AA,Amyloid Protein AA,Amyloid Protein AA Precursor,Amyloid-Related Serum Protein (SAA),Serum Amyloid A,Serum Amyloid Protein A,Amyloid A Protein Related Serum Component
D000686 Amyloidosis A group of sporadic, familial and/or inherited, degenerative, and infectious disease processes, linked by the common theme of abnormal protein folding and deposition of AMYLOID. As the amyloid deposits enlarge they displace normal tissue structures, causing disruption of function. Various signs and symptoms depend on the location and size of the deposits. Amyloidoses

Related Publications

C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
March 1976, The Journal of experimental medicine,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
December 1993, Biochimica et biophysica acta,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
January 1979, Infection and immunity,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
March 1980, European journal of biochemistry,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
January 1975, Acta veterinaria Scandinavica,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
January 2024, FASEB journal : official publication of the Federation of American Societies for Experimental Biology,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
December 1987, Scandinavian journal of immunology,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
January 1984, Comparative biochemistry and physiology. B, Comparative biochemistry,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
January 2004, Veterinary research,
C Foyn Bruun, and M Rygg, and K Nordstoga, and K Sletten, and G Marhaug
June 1990, The Journal of biological chemistry,
Copied contents to your clipboard!