N‐Terminal Amino Acid Sequence of Amyloid Fibril Protein AR, Prototype of a New λ‐Variable Subgroup, VλV

Sletten, K; Husby, Gunnar; Natvig, J. B.

doi:10.1111/j.1365-3083.1974.tb01319.x

Cited by 39 publications

(20 citation statements)

References 16 publications

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“…Nevertheless, the following facts can be interpreted as evidence for structural pecularities in amyloidogenic L-chains: a) only approximately 10% of all myeloma patients develop amyloidosis^1 1 ; b) λ-type L-chains are more frequently associated with amyloidosis than are κ-type chains' 13^; c) the incidence of λ-chains of subgroup VI forming amyloid fibrils in vivo is higher than expected from their concentration in plasma [6,7,14] ; d) no Η-chain material has been detected in amyloid fibrils; and e) amyloid-like material resulted from the limited enzymatic degradation of certain Bence-Jones proteins 115 " 171 . Die Molekularmasse des gereinigten, vorherrschenden Polypeptids betrug ungefähr 5000 Da.…”

Section: Ein Amyloidfibrillenprotein (Har) Das Sich Aus Fragmenten Dmentioning

confidence: 99%

Amyloid Fibrils Derived from V-Region together with C-Region Fragments from a λII-Immunoglobulin Light Chain (HAR)

Eulitz¹,

Linke²

1985

Biological Chemistry Hoppe-Seyler

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Section: Ein Amyloidfibrillenprotein (Har) Das Sich Aus Fragmenten Dmentioning

confidence: 99%

Amyloid Fibrils Derived from V-Region together with C-Region Fragments from a λII-Immunoglobulin Light Chain (HAR)

Eulitz¹,

Linke²

1985

Biological Chemistry Hoppe-Seyler

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“…Proteins of the XVI subgroup are of special interest because two of the three prototype hydantoin; C, constant domain; V, variable domain; VL, light chain variable domain. XVI proteins2 were found in the splenic fibrils of patients with primary amyloidosis (5,6).…”

Section: Introductionmentioning

confidence: 99%

“…The two proteins could be readily distinguished on the basis of molecular weight and antigenic determinants. As determined by gel filtration and SDS polyacrylamide gel electrophoresis, the spleen-derived pro-FIGURE 5 Immunological detection of XVI light chain-containing immunoglobulins in patients with primary or myeloma-associated amyloidosis AL(X). Immunoelectrophoretic analyses of serum from a normal subject (NHS) and from two patients with amyloidosis AL(X) (PT 50 and PT 45).…”

mentioning

confidence: 99%

Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda).

Solomon¹,

Frangione²,

Franklin³

1982

J. Clin. Invest.

235

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A B S T R A C T An antiserum prepared against a ABence Jones protein from a patient (SUT) who had multiple myeloma and amyloidosis had specificity for X-light chains of the chemically defined variable (V) region X-chain subgroup XVI. Sequence analyses of protein SUT and of five other X-light chains recognized immunologically as of the VAVI subgroup revealed that all six proteins had the N-terminal sequence characteristic for prototype XVI proteins. The isotypic nature of the VAVI subgroup was demonstrated immunochemically: XVI molecules were detected among light chains isolated from the IgG proteins of each of 12 normal individuals and XVI antigenic determinants were also detectable on the intact IgG proteins. The frequency of XVI molecules among X-type light chains is estimated to be -5% based on the finding that 5 of 91 X Bence Jones proteins were of the V,\vI subgroup.Proteins of the VAVI subgroup, in contrast to those of the other five chemically-classified X chain subgroup, appear to be preferentially associated with the amyloid process as evidenced by the fact that all six XVI proteins were obtained from patients with amyloidosis AL and, in addition, 5 of 42 X-type monoclonal immunoglobulins from patients with primary or myelomaassociated amyloidosis were classified by immunodiffusion analyses as having XVI-type light chains.

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“…subgroup λVI, seems to be especially prone to form amyloid [17]. Characteristically, the examination of an amyloid fibril protein led to the discovery of these subgroups [18]. Amyloid deposition was most often found to occur in the heart, tongue (macroglossia), skin, gastrointestinal tract and in peripheral nerves, but also the spleen, liver, kidneys and lungs may be involved [6,10,15,16].…”

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Amyloid formation from Immunoglobulin chains

Eulitz¹

1992

Biological Chemistry Hoppe-Seyler

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Amyloid 1 was first discovered during the examination of tissue by Rudolf Virchow in 1854.Because it could be stained in a similar manner as starch with iodine in Lugol's solution it was named "amyloid" by Virchow [1]. The deposition of this substance occurs extracellularly in small blood vessels and various organs. Examination under the light microscope reveals a homogeneous eosinophilic substance with hyaline appearance. Nowadays the diagnosis of amyloidosis still depends mainly on the examination of bioptic material from involved organs. Main criteria are the staining of amyloid with Congo red [2] and a characteristic green birefringence in polarized light.The formation of amyloid is associated with many different disorders and impairs the normal organ function when the deposits are severe. There have been controversial discussions about the nature of this substance for more than one hundred years. The observation by electron microscopy that the deposited material is composed of fibrils was a first step toward the unraveling of the mysteries of this disease [3]. A further major breakthrough happened when it became possible to extract amyloid fibrils from the tissue [4]. It was proven by serological and chemical methods that proteins are the main constituents of extracted amyloid fibrils and not, as supposed for a long time, starchlike polysaccharides. Particularly amino acid sequence analysis was applied successfully to identify the individual proteins which participate in the formation of amyloid deposits. These studies revealed that amyloidosis is not a single entity but is connected to a still growing range of various disorders and diseases. The current state of research in this field has been summarized by an international nomenclature committee at the Vlth International Symposium on Amyloidosis [5], which was held in Oslo in 1990.Because several excellent reviews on amyloidosis have been published [6-10], this paper concentrates only on amyloid formation from immunoglobulin chains. Magnus-Levy (in 1931 [11]) and Apitz (in 1940 [12]) were the first authors to report on correlations between multiple myeloma 1 Abbreviations: Protein A = amyloid associated protein; apoSAA = serum precursor of protein AA; AL-type = amyloid derived from immunoglobulin light chains; VHjjj = V-regions of immunoglobulin heavy (H) chains, subgroup III; CH = constant regions of H-chains

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N‐Terminal Amino Acid Sequence of Amyloid Fibril Protein AR, Prototype of a New λ‐Variable Subgroup, VλV

Cited by 39 publications

References 16 publications

Amyloid Fibrils Derived from V-Region together with C-Region Fragments from a λII-Immunoglobulin Light Chain (HAR)

Amyloid Fibrils Derived from V-Region together with C-Region Fragments from a λII-Immunoglobulin Light Chain (HAR)

Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda).

Amyloid formation from Immunoglobulin chains

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