Serum amyloid A (SAA): Biochemistry, genetics and the pathogenesis of AA amyloidosis

Husby, Gunnar; Marhaug, G.; Dowtor, Bruce; Sletten, Knut; Sipe, Jean D.

doi:10.3109/13506129409148635

Cited by 162 publications

(177 citation statements)

References 135 publications

Supporting

Mentioning

171

Contrasting

Unclassified

Order By: Relevance

“…5,18 Thus, the isolated fibril protein differs from the precursor protein in that it lacks between 18 and 60 amino acid residues at the C-terminus and, therefore, precursor and fibril proteins may not be accessible to the same proteases. With the second set of experiments we tested whether recombinant MMP-1, -2, and -3 are able to cleave AFP.…”

Section: Degradation Of Afps By Mmp-1 -2 and -3mentioning

confidence: 99%

“…[1][2][3][4] Amyloidoses are characterized by local, organ-limited, or generalized proteinaceous deposits of autologous origin showing fibrillar protein deposits with specific tinctorial and structural properties. [5][6][7] Approximately 45% of all generalized amyloidoses are secondary or AA amyloidosis, 8 -11 and the acute-phase protein serum amyloid A (SAA) is the precursor of the AA fibril protein deposited in this disease. In the West, AA amyloidosis is most commonly related to rheumatoid arthritis.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Proteolysis of AA Amyloid Fibril Proteins by Matrix Metalloproteinases-1, -2, and -3

Stix

Kähne

Sletten

et al. 2001

The American Journal of Pathology

Self Cite

View full text Add to dashboard Cite

We recently demonstrated the presence of matrix metalloproteinases (MMPs)-1, -2, and -3 in AA amyloid deposits, which lead us to speculate that MMPs may participate in amyloidogenesis by either processing the precursor protein, or by degrading the amyloid deposits. Here we investigated this theory by determining the ability of MMP-1, -2, and -3 to degrade human acute-phase serum amyloid A (SAA) and human AA amyloid fibril proteins (AFPs). The following in vitro degradation experiments were performed: using either recombinant MMP-1, -2, or -3 and SAA as a substrate; using either recombinant MMP-1, -2, or -3 and AFP as a substrate; and using THP-1 cells as the protease source and AFP as the substrate. All three MMPs were able to cleave SAA and AFP within the region spanning residues 51 to 57. The following cleavage sites were identified: at 57 to 58 for MMP-1; at 7 to 8 and 51 to 52 for MMP-2; at 7 to 8, 16 to 17, 23 to 24, 51 to 52, 55 to 56, 56 to 57, and 57 to 58 for MMP-3. Cell culture experiments showed that THP-1 cells were able to degrade AFPs. Degradation was significantly delayed after addition of a general metalloproteinase inhibitor (o-phenanthroline) to dextran sulfate-stimulated cells. This is the first study to show that human SAAs and AFPs are susceptible to proteolytic cleavage by MMPs. Immunocytochemistry and electron microscopy showed that degradation takes place in the pericellular or extracellular compartment. (Am J Pathol 2001, 159:561-570)

show abstract

Section: Degradation Of Afps By Mmp-1 -2 and -3mentioning

confidence: 99%

mentioning

confidence: 99%

Proteolysis of AA Amyloid Fibril Proteins by Matrix Metalloproteinases-1, -2, and -3

Stix

Kähne

Sletten

et al. 2001

The American Journal of Pathology

Self Cite

View full text Add to dashboard Cite

show abstract

“…However, in cats, the measurement of SAA concentration has not been used for routine clinical diagnosis and clinical management, due to the difficulties in raising specific antibodies against it. SAA in serum exists as one of apolipoproteins associated with third fraction of high density lipoprotein (HDL3) [4], thus its isolation from blood is laborious, and result is poor yield of insoluble protein. Furthermore, it is also difficult to obtain high titered antibodies due to a poor immunogen of low molecular weight.…”

mentioning

confidence: 99%

Expression of Recombinant Feline Serum Amyloid A(SAA) Protein.

Ohno

Terado

Iwata

et al. 1999

The Journal of Veterinary Medical Science

View full text Add to dashboard Cite

ABSTRACT. Feline serum amyloid A (SAA) cDNA clone was isolated from a hepatic mRNA of a mixed-breed cat. The feline SAA cDNA clone contains 333 nucleotides and deduced amino acid sequence shows 87.4%, 73.9%, and 65.8% homology with dog, human and mouse SAA respectively. Relative to the human and mouse SAA proteins, an additional peptide of eight amino acids is specified in the feline cDNA clone. Recombinant feline SAA (rfSAA) was expressed at high levels using pGEX bacterial expression system. Cleavage from the fusion moiety, and purification using glutathione-sepharose yielded pure soluble form of rfSAA. Antibodies generated against rfSAA were specific for feline SAA and showed no cross-reactivity with human SAA. Furthermore, antibodies against human SAA did not react with feline SAA. These results indicate that antigenicity of feline SAA is totally different from human SAA. -KEY WORDS: acute phase response, amyloid A (AA), recombinant protein, serum amyloid A (SAA).J. Vet. Med. Sci. 61(8): 915-920, 1999

show abstract

“…A amiloidose secundária é uma sé-ria complicação de doenças inflamatórias crônicas, caracterizada pela deposição de fibras protéicas insolúveis em vários órgãos (4) . O principal componente dessas fibras amilóides é derivado da clivagem proteolítica da SAA, por remoção do fragmento C-terminal (5) .…”

Section: Introductionunclassified

Avaliação da proteína amilóide A sérica na atividade clínica da artrite reumatóide

Gayer¹,

Pinheiro²,

Andrade³

et al. 2003

Rev. Bras. Reumatol.

View full text Add to dashboard Cite

show abstract

Serum amyloid A (SAA): Biochemistry, genetics and the pathogenesis of AA amyloidosis

Cited by 162 publications

References 135 publications

Proteolysis of AA Amyloid Fibril Proteins by Matrix Metalloproteinases-1, -2, and -3

Proteolysis of AA Amyloid Fibril Proteins by Matrix Metalloproteinases-1, -2, and -3

Expression of Recombinant Feline Serum Amyloid A(SAA) Protein.

Avaliação da proteína amilóide A sérica na atividade clínica da artrite reumatóide

Contact Info

Product

Resources

About