Antipeptide antibodies discriminate between different SAA proteins in human plasma

Saı̈le, Rachid; Hocke, Gerti; Tartar, André; Fruchart, Jean‐Charles; Steinmetz, Armin

doi:10.1016/0304-4165(89)90106-2

Cited by 7 publications

(1 citation statement)

References 11 publications

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“…Clinical, pathological and laboratory findings in all the patients are summarized in Table 1. AA amyloidosis and localization were diagnosed with the use of an anti-human amyloid A antibody against synthetic peptide (Saile et al 1988(Saile et al , 1989. Patient 3 was studied again 8 months later.…”

Section: Introductionmentioning

confidence: 99%

Iodine-123-labelled serum amyloid P component scintigraphy in amyloidosis

et al. 1993

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This study describes the results of scintigraphy with iodine-123-labelled serum amyloid P component (SAP) as a means of establishing the distribution of organ involvement in amyloidosis. The significance of 123I-SAP scans obtained in 15 patients with biopsy-proven AA or AL amyloidosis is discussed. Biopsy-proven amyloidosis was typically confirmed by scintigraphy, though such confirmation was not obtained in the kidneys in six patients with histological proof of extensive renal amyloid deposition. This lack of uptake may have been due to the accumulation of a major part of the 123I-SAP in the spleen and/or liver. Twenty-four hour whole-body retention of 123I-SAP was higher in patients with amyloidosis than in controls. Twenty-four hour tracer accumulation of the radioactivity in the extravascular compartment was notably greater in patients than in controls and appeared to be a good diagnostic criterion. We conclude that 123I-SAP scintigraphy may be helpful for the evaluation of organ involvement not only in patients with biopsy-proven amyloidosis but also when a biopsy cannot be performed or when a strong suspicion of amyloidosis exists in spite of repeated negative biopsies.

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Section: Introductionmentioning

confidence: 99%

Iodine-123-labelled serum amyloid P component scintigraphy in amyloidosis

et al. 1993

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Isoproteins and an isoelectric focusing mutant of human apoprotein serum amyloid A

et al. 1990

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On isoelectric focusing of human plasma and subsequent immunoblotting, using antii-human serum amyloid A (SAA) antibodies, a genetic variant of SAA was detected in a family of Turkish origin. All affected members of the family were apparent heterozygotes for the mutant protein, which underwent a charge shift of about one charge unit toward the anode. The variant is likely to be a mutant of the most prominent forms of SAA (SAA1 and SAA2, or SAA1 and SAA1 des Arg). The appearance of a genetic variant of two of the six reported SAA-isoforms in human plasma supports the concept of SAA proteins being products of different genes.

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