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  • 1
    Electronic Resource
    Electronic Resource
    Senile Cardiac Amyloidosis: Evidence of Two Different Amyloid Substances in the Ageing Heart (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 10 (1979), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In a material of seventy-two persons over 70 years of age. forty-seven cases of amyloidosis of the heart were found. In thirty-nine cases, deposits occurred only in the atria (isolated atrial amyl-oidosis. IAA), while in eight cases amyloid also was seen in the ventricles (senile cardiac amyloidosis, SCA). In some of the latter cases, small amyloid deposits occurred in other organs, especially the lungs. Some definite differences existed between the amyloid substance in SCA and IAA. Thus, tryptophan was demonstrated histochemically in SCA but not in IAA, and, furthermore, amyloid fibrils isolated from patients with IAA lacked protein ASCA, the fibril subunit protein of senile cardiac amyloid. It is concluded that the ageing heart may be the target of two different forms of amyloid, one only affecting the atria, while the other is more widespread within the heart and sometimes also is found in other organs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1979.tb01355.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Senile Cardiac Amyloidosis: Evidence of Two Different Amyloid Substances in the Ageing Heart (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 10 (1979), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In a material of seventy-two persons over 70 years of age. forty-seven cases of amyloidosis of the heart were found. In thirty-nine cases, deposits occurred only in the atria (isolated atrial amyl-oidosis. IAA), while in eight cases amyloid also was seen in the ventricles (senile cardiac amyloidosis, SCA). In some of the latter cases, small amyloid deposits occurred in other organs, especially the lungs. Some definite differences existed between the amyloid substance in SCA and IAA. Thus, tryptophan was demonstrated histochemically in SCA but not in IAA, and, furthermore, amyloid fibrils isolated from patients with IAA lacked protein ASCA, the fibril subunit protein of senile cardiac amyloid. It is concluded that the ageing heart may be the target of two different forms of amyloid, one only affecting the atria, while the other is more widespread within the heart and sometimes also is found in other organs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1979.tb01356.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Tumour-Like Localized Amyloid of the Brain is derived from Immunoglobulin Light Chain (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 37 (1993), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A patient is presented in whom the amyloid component of an intracerebral‘amyloidoma’has been purified and characterized by amino acid sequence analysis. The material originated from an autopsy of a 76-year-old man who 15 years earlier had been operated for an intracerebral‘amyloid tumour'. The tumour had recurred and grown to an almost walnut-sized mass in the right cerebral hemisphere. It was located in the parietal lobe close to the lateral ventricle and had a close connection to the choroid plexus. Histological examination showed large masses of amyloid surrounded by some plasma cells and a few macrophages of the foreign body type, Amino acid sequence analysis of a major fibril subunit protein showed homology with the variable region of a monoclonal lambda immunoglobulin light chain, subgroup III or IV. This shows that the amyloid in the ‘tumour’ was of AL type and presumably derived from local synthesis by plasma cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1993.tb01673.x
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  • 4
    Electronic Resource
    Electronic Resource
    Further Structural and Antigenic Studies of Light-chain Amyloid Proteins (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 14 (1981), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The major subunit protein of amyloid fibrils (758) isolated from a patient with systemic amyloidosis and studied by N-terminal amino acid sequence analysis was found to be almost identical to the sequence of a VλIV Bence-Jones protein and a previously described AλIV amyloid protein. The two AλIV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-AλlV antiserum raised against one or the other of the two proteins. In addition, another new AλV amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the AλV subgroup (the AR protein). Finally, 20 primary or myeloma-associated amyloid proteins were characterized using antisera against the AA and several Ig light-chain-derived amyloid proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1981.tb00187.x
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  • 5
    Electronic Resource
    Electronic Resource
    Coexistence of Protein AA and Immunoglobulin Light-Chain Fragments in Amyloid Fibrils (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Coexistence of amyloid fibril protein AA and homogeneous immunoglobulin light-chain fragments was found in the isolated amyloid fibrils of two patients with amyloidosis secondary to rheumatoid arthritis. The light-chain amyloid fibril protein showed antigenic identity with a light-chain amyloid from a patient with primary amyloidosis, which was identified as the VλIV subgroup by amino acid sequence analysis. In the amyloid fibrils isolated from another patient with primary amyloidosis there was a mixture of VλIV and VλV homogeneous immunoglobulin light chains. Thus, a mixture of protein AA and λ light chains or two different types of homogeneous light chains may be found in the amyloid fibrils of some patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb02989.x
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  • 6
    Electronic Resource
    Electronic Resource
    Biclonal Systemic AL-Amyloidosis with One Glycosylated and One Nonglycosylated AL-Protein (2003)
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 57 (2003), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The amyloid fibril protein AL was isolated from the spleen of a patient with systemic amyloidosis. Size-exclusion chromatography of the solubilized amyloid fibrils revealed a distinct, retarded asymmetric peak. The symmetrical part of the peak showed on SDS-PAGE two positive periodic acid Schiff-staining bands at 14 and 16 kDa. Staining with Coomassie Brilliant Blue revealed in addition two proteins with masses of 13 and 20 kDa. The 14 and 16 kDa bands were the strongest ones. N-Terminal analyses of the four blotted bands showed that the N-termini were the same in all cases. Elucidation of the amino acid sequence established an AL-chain of 157 residues as well as a fragment covering positions 188–207 of the constant region. Two tryptic peptides derived from the same region, positions 25–46, showed an identical sequence, except for position 34 where both alanine and threonine residues occurred. Monosaccharide compositional analysis of the threonine-containing peptide revealed an oligosaccharide in the N-glycosylation site, position 32–34. Mass analysis of the glycopeptide verified the oligosaccharide. The AL-chains belong to the kappa 3a germline gene and verifies that the glycosylated chain is a mutated form. The AL-chains differ from that of the germline in 14 positions. The J-segment is of JκIII and is mutated in position 106.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.2003.01230.x
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  • 7
    Electronic Resource
    Electronic Resource
    Identification and Characterization of Different Amyloid Fibril Proteins in Tissue Sections (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 6 (1977), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Antisera specific for 4 different classes of amyloid fibril proteins, amyloid protein AA and the immunoglobulin light-chain amyloid proteins AλI, AλIV, and AλV, were used to identify these proteins directly in tissue sections from 25 patients with amyloidosis. The specificity of these reactions was established by blocking experiments with purified amyloid fibril proteins and Bence Jones proteins of known variable subgroups. Protein AA was detected in 17 patients, including all 13 with secondary amyloidosis, 2 with primary amyloidosis and 2 with Waldenström's macroglobulinemia. Immunoglobulin light-chain proteins Aλ I, AλIV, and Aλ V were found in 3, 1, and 2 patients, respectively, all of whom had primary or myeloma/macroglobulinemia-associated amyloidosis. Antiserum specific for the amyloid-related serum protein SAA reacted with the same tissues as anti-AA and had the same pattern of staining in tissue sections.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1977.tb00344.x
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of Amyloid of Ageing Obese–Hyperglycaemic Mice and their Lean Littermates (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 9 (1979), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Amyloid fibrits, isolated from 18-month-old obese–hyperglycaemic mice and their lean littermates, were characterized immunologically and chemically. The main amyloid fibril subunit protein was protein AA, which cross-reacted completely with an antiserum against amyloid from mice with experimentally induced amyloidosis and had an amino acid composition and N-terminal amino acid sequence identical to that protein. These results indicate that the spontaneously occurring amyloidosis in obese–hyperglycaemic mice and their lean littermates corresponds to human, secondary amyloidosis and may serve as a model for that disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1979.tb02722.x
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  • 9
    Electronic Resource
    Electronic Resource
    Prealbumin in Swedish Patients with Senile Systemic Amyloidosis and Familial Amyloidotic Polyneuropathy (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 21 (1985), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A prealbumin (PA)-like protein was demonstrated in amyloid fibrils both from a patient with senile systemic amyloidosis (SSA) and from a patient in northern Sweden with familial amyloidotic polyneuropathy (FAP). The investigated properties of this protein were similar in the two types of fibrils. The protein had molecular weight, antigenic determinants, and at least one eysteinyl residue in common with the subunit of normal PA. In contrast to normal PA. it contained disulphide-linked subunits and was to some extent bound to the fibril via the eysteinyl residues. The noncovalent forces between its subunits were weaker than in normal PA. It constituted part of the previously described AScl protein of the SSA fibrils. Proteins with lower molecular weight than the PA monomer were major proteins in both SSA and FAP fibrils. These proteins had similar properties in the two kinds of fibril and may be derived from PA. PA in serum from Swedish patients with FAP and SSA was normal with regard to the isoclectric pH of the monomers and tetramers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1985.tb01412.x
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  • 10
    Electronic Resource
    Electronic Resource
    Senile Cardiac Amyloid is Related to Prealbumin (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 12 (1980), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The major component, protein ASC, isolated from the amyloid fibrils in senile cardiac amyloidosis, was characterized by structural studies of some peptic peptides. One of the peptides has an amino acid sequence identical to residues 70–90 in human prealbumin, and three other smaller peptides have a primary structure identical to that in positions 96–107, 109–115 and 121–127. The amino acid composition of the protein resembles that of human prealbumin but shows some characteristic differences. The protein has a blocked N-terminus and gives no visible precipitin reaction with antiserum to human prealbumin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1980.tb00098.x
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