Unique Amyloid Protein Subunit common to Different Types of Amyloid Fibril

Husby, Gunnar; Natvig, J. B.; Michaelsen, T. E.; Sletten, K; Høst, Herman

doi:10.1038/244362a0

Cited by 32 publications

(15 citation statements)

References 8 publications

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“…DISCUSSION The nonimmunoglobulin amyloid protein AS with the reported molecular weight of 7,000-9,000 daltons (10,19,20) corresponding to 76 amino acids (20) is shown to be an integral part of the amyloid substance in secondary amyloidosis (8,10,19). In addition, we have recently demonstrated the presence of protein AS in amyloid preparations derived from patients with primary amyloidosis as well as amyloidosis associated with myelomatosis or macroglobulinemia (9,12). It has been shown that protein AS can form fibrils (8,21,22).…”

Section: Resultsmentioning

confidence: 99%

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A Serum Component Related to Nonimmunoglobulin Amyloid Protein AS, a Possible Precursor of the Fibrils

Husby¹,

Natvig²

1974

J. Clin. Invest.

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179

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Section: Resultsmentioning

confidence: 99%

“…Protein AS was thought to be an essential part of amyloid fibrils in most amyloid substances. Recently, a protein in serum (we call protein ASC), antigenically related to protein AS, was described independently by Levin, Pras, and Franklin (10) and by Husby, Michaelsen, Sletten, Natvig, and H6st (11,12).…”

Section: Introductionmentioning

confidence: 99%

A Serum Component Related to Nonimmunoglobulin Amyloid Protein AS, a Possible Precursor of the Fibrils

Husby¹,

Natvig²

1974

J. Clin. Invest.

Self Cite

179

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“…However, in several patients with amyloidosis and in some patients with monoclonal gammopathies complicated by the nephrotic syndrome, the SAA level was normal or low. It is of interest that in patients with amyloidosis associated with myeloma and those with primary amyloidosis, the increase of the SAA level occurs in the face of tissue deposits of amyloid, which in our experience often contain little or no acid-soluble fraction (34), though some of these do contain this protein (35). This discrepancy suggests the possibility of a blockade in the transfer of the nonimmunoglobulin amyloid precursor from the blood vessels to the tissues, or such a marked excess of light chain production and deposition that the amyloid fibrils consist primarily of light chain fragments.…”

Section: Discussionmentioning

confidence: 99%

Variation with age and disease of an amyloid A protein-related serum component.

Rosenthal¹,

Franklin²

1975

J. Clin. Invest.

203

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“…It has been found that antiserum prepared against protein AA reacts with a 100 to 200-kilodalton (kDal) a-globulin present in normal as well as pathological human serums (3,4). Although different methods of assay have led to different estimates of the normal serum concentration of the AA-related antigenic material (SAA), there is general agreement that increased levels are found in association with a variety of pathological conditions (5)(6)(7)(8)(9).…”

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confidence: 93%

“…ApoSAA was estimated by radioimmunoassay as described (13), using human protein AA as standard and rabbit antiserum thereto as antibody. Before assay, chromatographic effluent samples in 6 M urea at pH 3 were neutralized and diluted with 3 vol of 0.25 M Na2HPO4, and those in 8 M urea at pH 8.2 were diluted with 4 vol of phosphate-buffered saline. ApoSAA levels were computed from the linear portion of a standard curve obtained by a log/logit transformation of the data (16).…”

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confidence: 99%

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

Eriksen¹,

Benditt²

1980

Proc. Natl. Acad. Sci. U.S.A.

107

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Two apoproteins immunologically related to the 9000-dalton abnormal tissue constituent known as amyloid protein AA were isolated from the lipoprotein density interval 1.125-1.21 g/cm3 (HDL3) of a pool of human serums by delipidation, gel filtration, and ion-exchange chromatography. Lesser amounts of the same apoproteins were isolated from the density interval 1.063-1.125 g/cm3 (HDL2). These apoproteins, designated apoSAAI and apoSAA2, have molecular weights near 11,500, almost identical amino acid compositions, and slightly different isoelectric points. Their amino acid sequences are identical as far as determined (30 residues), except that apoSAA2 lacks the NH2-terminal arginine found in apoSAA1. The sequence is homologous with that of amyloid protein AA, which thus has residing in the plasma high density lipoproteins a potential precursor whose biological significance and function remain to be determined.Certain amyloid-containing tissues, in particular those associated with inflammation, yield upon extraction a substance that includes as a major constituent a unique polypeptide, originally called amyloid protein A (1) and now termed amyloid protein AA (2). It has been found that antiserum prepared against protein AA reacts with a 100 to 200-kilodalton (kDal) a-globulin present in normal as well as pathological human serums (3,4). Although different methods of assay have led to different estimates of the normal serum concentration of the AA-related antigenic material (SAA), there is general agreement that increased levels are found in association with a variety of pathological conditions (5)(6)(7)(8)(9).Treatment of native serum with formic or stronger acid converts the bulk of the AA-related antigenic material into a low molecular weight (10,000-15,000) protein, sometimes called SAAL, the putative precursor of the still smaller tissuederived protein AA (10-12). In a study of human serum in which an increased level of SAA had been induced by typhoid vaccination of the donor, we showed that the high molecular weight species was a part of the high density lipoproteins, mainly HDL3, and that acid treatment of the HDL3 released a significant portion of the SAA as a 10-to 15-kDal species (13). We found in mouse plasma a similar association of SAA with HDL, further characterized the protein, and proposed the name apoSAA for the low molecular weight species (14). Another group of investigators has recently described an association between SAA and HDL in rabbit serum (15).We report here on the isolation of apoSAA from the HDL of a pool of human serums, and on the characterization of the purified material, including NH2-terminal amino acid sequences.The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. 6860MATERIALS AND METHODS Isolation and Delipidation of HDL. A pool of patient serums with an elevated level of AA-immunoreactivity (stored at -180C until ...

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Unique Amyloid Protein Subunit common to Different Types of Amyloid Fibril

Cited by 32 publications

References 8 publications

A Serum Component Related to Nonimmunoglobulin Amyloid Protein AS, a Possible Precursor of the Fibrils

A Serum Component Related to Nonimmunoglobulin Amyloid Protein AS, a Possible Precursor of the Fibrils

Variation with age and disease of an amyloid A protein-related serum component.

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

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