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  • 1
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-0528.2000.tb13315.x
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  • 2
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1468-3083.2004.00813.x
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  • 3
    Digitale Medien
    Digitale Medien
    Experimental AA-Amyloidosis in Mice is Inhibited by Treatment with the Anti-Rheumatic Drug Tenidap (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 43 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: In a mouse model for induction of experimental AA-amyloidosis, treatment with tenidap was shown to inhibit the development of amyloidosis. Studies have shown that the drug inhibits the cytokines interleukin (IL)-6, IL-1 and tumour necrosis factor α (TNF-α) which are known to stimulate hepatocytes to synthesize acute phase proteins (APPs). The APP serum amyloid protein (SAA) is the precursor for amyloid protein AA and tenidap treatment reduces the serum levels of SAA in mouse and humans. It is suggested that reduction of SAA levels reduces the risk of AA fibril formation and thus the development of amyloidosis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-74.x
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  • 4
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1986.tb02007.x
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  • 5
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.0300-9475.2005.01537.x
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  • 6
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1985.tb01431.x
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  • 7
    Digitale Medien
    Digitale Medien
    Characterization of Bovine Amyloid Proteins SAA and AA (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 27 (1988), S. 0 
    Details
    ISSN: 1365-3083
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: The bovine serum amyloid A (SAA) and tissue amyloid A (AA) proteins were isolated and characterized. SAA was isolated from acute phase high density lipoprotein (HDL) of a cow suffering from acute mastitis, and was identified by amino acid sequence analysis. No AA-like protein was found in complex with HDL in serum. Amyloid fibrils isolated from a bovine kidney contained a 9 kDa AA protein and a considerable amount of a 14 kDa protein. Amino acid sequence analysis showed that the largest protein probably represents undegraded SAA. This is an interesting observation which confirms previous works indicating that SAA can be incorporated in the amyloid fibrils without a prior degradation to AA. The partial amino acid sequences of bovine SAA and AA were strikingly homologous to the sequences of corresponding proteins in man and other species.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1988.tb02408.x
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  • 8
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb02203.x
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  • 9
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1992.tb02853.x
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  • 10
    Digitale Medien
    Digitale Medien
    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
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: 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).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-3083.1989.tb01195.x
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