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  • 1
    Electronic Resource
    Electronic Resource
    Reticular erythematous mucinosis syndrome: report of a case with positive immunofluorescence (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of the European Academy of Dermatology and Venereology 18 (2004), S. 0 
    Details
    ISSN: 1468-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1468-3083.2004.00813.x
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  • 2
    Electronic Resource
    Electronic Resource
    Neonatal alloimmune thrombocytopenia due to anti-HPA 1a antibodies; the level of maternal antibodies predicts the severity of thrombocytopenia in the newborn (2000)
    Oxford, UK : Blackwell Publishing Ltd
    BJOG 107 (2000), S. 0 
    Details
    ISSN: 1471-0528
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Eleven thousand one hundred pregnant women were genotyped for human platelet antigen HPA 1, and 198 HPA 1bb women were followed in the pregnancy with quantitative assay for anti-HPA 1a antibodies. Antibodies were detected in 24 women, and nine children were born with severe thrombocytopenia (〈 50×109/L). All mothers with high levels of antibodies were delivered of children with severe thrombocytopenia. None of the newborn infants had clinical signs of intra-cranial haemorrhage. The level of maternal anti-HPA 1a antibodies is predictive for fetal thrombocytopenia and may be used in decisions related to time and mode of delivery.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-0528.2000.tb13315.x
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  • 3
    Electronic Resource
    Electronic Resource
    Transformation of Amyloid Precursor SAA to Protein AA and Incorporation in Amyloid Fibrils in Vivo (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: Experimental amyloidosis was induced in mice by in t raped toneal injections of endotoxin (lipopolysaccharidc (LPS)). In addition to LPS. a group of mice received high-density lipoprotein (HDL)-SAA complexes isolated from human acute-phase serum, whereas a group of control mice received saline in addition to LPS. Isolated amyloid fibrils from the mice given HDL-SAA contained human AA protein, as shown by immunodiffusion, immunoblot. and enzyme-linked Immunosorbent assay techniques, in addition to mouse AA. In contrast, amyloid from the control mice contained exclusively AA of mouse origin. Thus, the experiments provided solid evidence that SAA is the precursor for amyloid fibril proiein AA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1985.tb01431.x
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of Amyloid Proteins AA and SAA as Apolipoproteins of High Density Lipoprotein (HDL) (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 25 (1987), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: An AA-like protein with a molecular weight of 8600 complexed to high-density lipoprotein (HDL) was demonstrated in several acute-phase sera with high levels of SAA. The protein ‘apo AA’(to distinguish it from tissue AA) was isolated by elution from sodium dodecyl sulphate (SDS)-polyacrylamide gel, and showed antigenic identity with purified tissue protein AA in double immunodiffusion. Normal HDL was shown to bind purified tissue AA in vitro. When the in vitro-associated HDL-AA complexes were given intravenously to mice during induction of amyloidosis, human AA was incorporated in the amyloid fibrils. Both apo AI and apo AII were shown to displace SAA from acute phase HDL when added to HDL-SAA complexes in vitro. This might be of importanee in amyloidogenesis, as the liver and the small intestine, which are the main sites for AI and AII synthesis, are also sites of early amyloid deposition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb02203.x
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  • 5
    Electronic Resource
    Electronic Resource
    Increased Frequency of Antral CD4+ T and CD19+ B Cells in Patients with Helicobacter pylori-Related Peptic Ulcer Disease (2005)
    Oxford, UK; Malden, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 61 (2005), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Only a fraction of Helicobacter pylori (HP)-infected individuals develop clinical disease. Recent research indicates that immunological mechanisms may be important for understanding the pathophysiology of HP infection. Differences in the individual cellular immune response may reflect the clinical diversity. The aim of the present study was to investigate the cellular immune response against HP in three clinically well-defined patient groups: HP-positive peptic ulcer, HP-positive and HP-negative gastritis. Biopsies from gastric mucosa were processed for analysis by flow cytometry and histology. The number of T lymphocytes (CD3+) was significantly higher in HP-positive peptic ulcer (13.8%) than in HP-positive nonulcer gastritis (6.3%). A nonsignificant increase for B lymphocytes (CD19+) was noted as well. Furthermore, a significant difference was seen in mucosal CD4/CD8 ratio between HP ulcer (2.4) and nonulcer HP gastritis (1.0) patients. Thus, B cells (CD19+) and T-helper cells (CD4+) were dominant in gastric mucosa from peptic ulcer patients, and cytotoxic T cells (CD8+) were relatively dominant in gastric mucosa from nonulcer patients. In conclusion, distinct differences in the T-cell subset distribution of mucosal lymphocytes were detected in patients with HP infection, strongly correlated with the presence or absence of peptic ulcer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0300-9475.2005.01537.x
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  • 6
    Electronic Resource
    Electronic Resource
    The Complete Amino Acid Sequence of Bovine Serum Amyloid Protein A (SAA) and of Subspecies of the Tissue-Deposited Amyloid Fibril Protein A (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 35 (1992), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Bovine serum amyloid A (SAA) was isolated from the acute phase high density lipoprotein (HDL) fraction of a cow suffering from acute mastitis. The elucidated primary structure revealed a protein consisting of 112 amino acid residues. Compared with SAA proteins from other species, the bovine protein was shown to have an insertion of nine amino acid residues between positions 69 and 70. No microheterogeneity could be observed in the protein.Amyloid fibrils extracted from the kidneys were found to contain at least three subspecies of protein AA, consisting of 68, 81 and about 110 amino acid residues. The amino acid sequences established for the protein AA subspecies revealed no microheterogeneity, and were identical to that elucidated for protein SAA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1992.tb02853.x
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of Amyloid Protein AA and Its Serum Precursor SAA in the Horse (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 23 (1986), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Amyloid was extracted from the liver of a horse that had developed amyloidosis after being used for several years for the production of antibodies to bacterial antigens. The amyloid fibrils were shown to he of the AA type. Two AA proteins with molecular weights of 9000 and 11,000 and with identical partial N-terminal amino acid sequences were identified. Marked structural homology with AA from other species including man was seen, although clear species-related antigenic specificity was observed. SAA isolated from an acute phase (septic abortion) horse serum was identical to AA with respect to antigenicity and the 10 first N-terminal amino acid residues that have been studied up to now. The hulk of SAA was present in the high-density lipoprotein complex in serum. Also SAA was heterogeneous with respect to size, most molecules having a molecular weight of 11,000, and a minority 9000.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1986.tb02007.x
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  • 8
    Electronic Resource
    Electronic Resource
    High-Density Lipoprotein has Different Binding Capacity for Different Apoproteins (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 28 (1988), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Purified human amyloid protein A (AA) or serum amyloid protein A (SAA) was incubated with normal human high-density lipoprotein (HDL). After ultracentrifugation the amount of AA or SAA associated with HDL was measured. It was found that the binding capacity of HDL for SAA was higher than that for AA. Incubation of these in vitro associated HDL-AA and HDL-SAA complexes with purified apo AI or apo AII resulted in varying degrees of displace-ment of the associated AA or SAA from HDL. Under the experimental conditions used, apo AI was able to displace AA from HDL, while apo AII was able to displace both SAA and AA. This indicates that the binding capacity of HDL is different for SAA and AA Mouse acute-phase HDL was isolated and the native complexes were incubated with human apo AII SAA2, the amyloidogenic SAA variant in mice, was displaced from HDL to a greater extent than SAA1, indicating a lower binding capacity for the amyloidogenic SAA variant for the HDL complexes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1988.tb01498.x
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  • 9
    Electronic Resource
    Electronic Resource
    The Amino Acid Sequence of an Amyloid Fibril Protein AA Isolated from the Horse (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 26 (1987), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The amino acid sequence of the amyloid fibril protein AA from horse was established from charaeterization of cyanogen bromide fragments, tryptic peptides, and a peptide derived from a digest with Staphylococcus aureus V8 proteinase. The protein was found to consist of 80 amino acid residues. Sequence homologies with protein AA from other species were very striking, and revealed an insertion of two amino acid residues between positions 72 and 73. In position 44, two amino acid residues were found which provide further evidence for a polymorphism in the amyloid fibril protein AA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb02237.x
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  • 10
    Electronic Resource
    Electronic Resource
    The Primary Structure of Equine Serum Amyloid A (SAA) Protein (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 30 (1989), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The complete amino acid sequence of equine serum amyloid A (SAA) was elucidated. The protein consists of 110 amino acid residues and contains an 8-amino acid residue insertion tentatively located between positions 69 and 70, as compared with human SAA. Microheterogeneities were detected at positions 16,44, and 59, compatible with the existence of more than one SAA gene in the horse. This corresponds to the situation in man and mouse. Pronounced homology with SAA from man and several animal species was observed, thus confirming the conserved structure of this acute phase reactant and apoprotein of high-density lipoprotein (HDL).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1989.tb01195.x
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