Literature DB >> 3931569

Serum amyloid A protein (SAA) subtypes in acute and chronic inflammatory conditions.

C P Maury, C Ehnholm, M Lukka.   

Abstract

Serum amyloid A (SAA), a polymorphic high density lipoprotein associated plasma protein, is the putative circulating precursor of tissue AA protein fibrils in reactive (secondary) amyloidosis. In the present study we examined the SAA subtype pattern in various acute and chronic inflammatory states in order to find out whether disease-specific SAA isoform profiles exist. The method used to study the subtype pattern is based on electrofocusing of serum followed by immunoblotting. Our results show that the SAA subtype pattern is similar in patients with rheumatoid arthritis with or without amyloid. In addition, in amyloidotic subjects the SAA subtype response to acute tissue injury (arthroplasty) did not differ from that in patients without amyloidosis. Analysis of patients with acute and chronic infectious diseases and non-rheumatic inflammatory conditions showed similar SAA patterns in all subjects. These results suggest that the SAA subtype response to tissue injury and inflammation is similar irrespective of the initiating stimulus.

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Year:  1985        PMID: 3931569      PMCID: PMC1001749          DOI: 10.1136/ard.44.10.711

Source DB:  PubMed          Journal:  Ann Rheum Dis        ISSN: 0003-4967            Impact factor:   19.103


  27 in total

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Authors:  R J HAVEL; H A EDER; J H BRAGDON
Journal:  J Clin Invest       Date:  1955-09       Impact factor: 14.808

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Journal:  J Biol Chem       Date:  1972-09-10       Impact factor: 5.157

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Authors:  B Skogen; L Thorsteinsson; J B Natvig
Journal:  Scand J Immunol       Date:  1980       Impact factor: 3.487

4.  Isolation and characterization of the amyloid-related apoprotein (SAA) from human high density lipoprotein.

Authors:  N Eriksen; E P Benditt
Journal:  Proc Natl Acad Sci U S A       Date:  1980-11       Impact factor: 11.205

Review 5.  Amyloid deposits and amyloidosis: the beta-fibrilloses (second of two parts).

Authors:  G G Glenner
Journal:  N Engl J Med       Date:  1980-06-12       Impact factor: 91.245

6.  Elastase-type proteases on the surface of human blood monocytes: possible role in amyloid formation.

Authors:  G Lavie; D Zucker-Franklin; E C Franklin
Journal:  J Immunol       Date:  1980-07       Impact factor: 5.422

7.  Isolation and characterization of amyloid-related serum protein SAA as a low molecular weight protein.

Authors:  R F Anders; J B Natvig; T E Michaelsen; G Husby
Journal:  Scand J Immunol       Date:  1975       Impact factor: 3.487

8.  Isolation of a low-molecular-weight serum component antigenically related to an amyloid fibril protein of unknown origin.

Authors:  R P Linke; J D Sipe; P S Pollock; T F Ignaczak; G G Glenner
Journal:  Proc Natl Acad Sci U S A       Date:  1975-04       Impact factor: 11.205

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Authors:  E P Benditt; N Eriksen
Journal:  Proc Natl Acad Sci U S A       Date:  1977-09       Impact factor: 11.205

10.  Heterogeneity of human serum amyloid A proteins.

Authors:  L L Bausserman; P N Herbert; K P McAdam
Journal:  J Exp Med       Date:  1980-09-01       Impact factor: 14.307

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  2 in total

1.  Identification of three isoform patterns of human serum amyloid A protein.

Authors:  A F Strachan; F C de Beer; D R van der Westhuyzen; G A Coetzee
Journal:  Biochem J       Date:  1988-02-15       Impact factor: 3.857

2.  Induction of pro-inflammatory genes by serum amyloid A1 in human amnion fibroblasts.

Authors:  Wenjiao Li; Wangsheng Wang; Rujuan Zuo; Chao Liu; Qun Shu; Hao Ying; Kang Sun
Journal:  Sci Rep       Date:  2017-04-06       Impact factor: 4.379

  2 in total

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