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  • 1
    Electronic Resource
    Electronic Resource
    The classification of amyloid deposits in clinicopathological practice (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Histopathology 29 (1996), S. 0 
    Details
    ISSN: 1365-2559
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A series of 104 biopsy cases with histopathological proof of amyloid, submitted to our department of pathology over the last 19 years, were re-examined. The survey investigated the medical indication for surgery, the origin and quality of the biopsy and the clinical information as documented on the request form for histopathological examination and in hospital records. Amyloid deposits were classified using antisera directed against five major amyloid fibril proteins, i.e. AA, ATTR, Aλ, Aκ and Aβ2M and optimal conditions were sought for the reliable and early characterization of amyloid disease in clinicopathological practice. This survey revealed that 98% of the biopsy cases already suffered from a disease which was either a cause or a result of amyloidosis. In only 2% of the biopsy cases was amyloidosis detected without any clinical indication. Immunohistochemical classification of the amyloid deposits and comparison with hospital records demonstrated diagnostic pitfalls such as immunostaining of amyloid by two or more antibodies recognizing different fibril proteins, and disagreement between immunohistochemical typing of amyloid and the initial clinical diagnosis. Based on these observations we assume that the characterization of amyloid disease and its biological significance is impossible in clinicopathological practice without clinical information or without immunohistochemical classification of the fibril protein in biopsy specimens. Different aspects of histopathological detection of AA- and AL-amyloidosis are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2559.1996.tb01416.x
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  • 2
    Electronic Resource
    Electronic Resource
    Abdominopelvic perivascular epithelioid cell sarcoma (malignant PEComa) mimicking gastrointestinal stromal tumour of the rectum (2005)
    Oxford, UK : Blackwell Science Ltd
    Histopathology 46 (2005), S. 0 
    Details
    ISSN: 1365-2559
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2559.2005.01991.x
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  • 3
    Electronic Resource
    Electronic Resource
    Plasmacytoma of the tonsil with AL amyloidosis: evidence of post-fibrillogenic proteolysis of the fibril protein (2000)
    Springer
    Virchows Archiv 436 (2000), S. 336-344 
    Details
    ISSN: 1432-2307
    Keywords: Key words Amyloid ; λ Light chain ; Osseous metaplasia ; Plasmacytoma ; Protease ; Tonsil
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  We report of a 58-year-old Caucasian man who was referred to the University Hospital with a greatly enlarged left tonsil which showed calcifications on computed-tomography scans. Histopathology revealed a plasmacytoma with secondary AL amyloidosis, ossifications, and multinucleated foreign-body-type giant cells. N-terminal sequencing of amyloid-fibril proteins purified from the formalin-fixed tissue showed the presence of two proteins of different size; these were of λ-light-chain origin (subgroup V), measured approximately 15.2 kDa and 10.5 kDa, and had identical N-terminal ends (YVLTQPP). When the amyloid deposits were immunolabeled with a polyclonal antibody directed against λ light chain, they showed two staining patterns: some deposits showed intense immunolabeling while others were not immunoreactive. Immunostaining of amyloid was completely absent after protease pre-treatment. Immunoelectron microscopy with gold-labeled secondary antibodies showed staining that was spatially related to amyloid fibrils and suggested that the antibody probably detected the fibril protein. Therefore, our hypothesis in this case is that the different immunostaining patterns are due to a post-fibrillogenic proteolysis of the fibril protein at the C-terminal end of the light chain, as indicated by the presence of two differently sized λ-light-chain fragments with identical N-terminal ends.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050456
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution pattern of matrix metalloproteinases 1, 2, 3, and 9, tissue inhibitors of matrix metalloproteinases 1 and 2, and α2-macroglobulin in cases of generalized AA- and AL amyloidosis (2000)
    Springer
    Virchows Archiv 437 (2000), S. 521-527 
    Details
    ISSN: 1432-2307
    Keywords: Amyloid Protease Protease inhibitors Matrix metalloproteinases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. Matrix metalloproteinases (MMPs) degrade basement membranes and connective tissue and play an essential role in the homeostasis of the extracellular matrix which is disrupted by the deposition of amyloid. This immunohistochemical study investigated the distribution pattern of matrix metalloproteinases (MMP-1, -2, -3, and -9) and their inhibitors [α2-macroglobulin (α2-M), tissue inhibitors of MMPs (TIMP)-1, and TIMP-2] in human AA- and AL amyloid deposits. Specimens of liver, kidney, and spleen from 22 autopsy cases were investigated. Nine patients had suffered from generalized AA amyloidosis, eight from generalized AL amyloidosis, and five from rheumatoid arthritis or tuberculosis with no histological evidence of amyloid. In all amyloidotic and non-amyloidotic patients, each protease and protease inhibitor was detected in almost every organ investigated. In the amyloidotic cases, there was no indication that a specific protease or protease inhibitor was absent or expressed, but a difference was observed in their spatial distribution patterns. The most noticeable difference was found in immunostaining of amyloid. Only MMP-1, -2, and -3, and α2-M were present in AA amyloid deposits, and only TIMP-1 and TIMP-2 were found in deposits of AL amyloid. This is the first study to show that MMP-1, -2, and -3 are present in AA amyloid deposits. They may be involved in tissue remodeling or in proteolysis of the precursor and fibril proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280000271
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  • 5
    Electronic Resource
    Electronic Resource
    Generalized AA-amyloidosis in a 58-year-old Caucasian woman with an 18-month history of gastrointestinal tuberculosis (1999)
    Springer
    Virchows Archiv 434 (1999), S. 95-100 
    Details
    ISSN: 1432-2307
    Keywords: Key words Amyloid ; Gastrointestinal tuberculosis ; Mycobacterium bovis ; Crohn’s disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  We report on a 58-year-old Caucasian woman who went to a general practitioner about recurrent abdominal pain, night sweats and weight loss of a few weeks’ duration. Once gynaecological disease had been ruled out, the patient was admitted to hospital with severe abdominal pain and intestinal obstruction and a right-sided hemicolectomy was performed. Following the investigation of osteolytic lumbar vertebrae, 18 months after visiting the general practitioner the patient was finally found to be suffering from generalized AA-amyloidosis secondary to gastrointestinal tuberculosis. This had been misinterpreted as Crohn’s disease. Re-examination of the specimens from the right-sided hemicolectomy demonstrated that scanty deposits of AA-amyloid were present 9 months after the first presentation. AA-amyloid can thus be present in serious inflammatory disease even during the first 9 months after the initial clinical presentation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050311
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  • 6
    Electronic Resource
    Electronic Resource
    Comparison of the binding and endocytosis of high-density lipoprotein from healthy (HDL) and inflamed (HDLSAA) donors by murine macrophages of four different mouse strains (1998)
    Springer
    Virchows Archiv 432 (1998), S. 547-555 
    Details
    ISSN: 1432-2307
    Keywords: Key words Amyloid ; High-density lipoprotein ; Macrophage ; Endocytosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Serum amyloid A (SAA) is a plasma acute phase protein and the precursor of the AA-fibril protein deposited in AA-amyloidosis. SAA is bound mainly to high-density lipoproteins (HDLSAA). Previous investigations have demonstrated that peritoneal macrophages (mØ) from mice are capable of binding and endocytosing HDLSAA. This observation may indicate a pathway by which SAA enters the mØ and where its intracellular metabolism may be followed by degradation and/or amyloidogenesis. Since binding and internalization defects of lipoproteins may be associated with different diseases, it is possible that mouse strain susceptibility to amyloidosis is associated with qualitative differences in the binding and internalization of HDLSAA. To test this hypothesis a series of binding and internalization experiments was performed in vitro with mØ from four different mouse strains, CD-1, A/J, C57BL/6J and C3H/HeJ, which differ in their susceptibility to AA-amyloidosis. Using colloidal gold-labelled lipoproteins, it was evident by light and electron microscopy that mØ from all four mouse strains are capable of binding and internalizing HDL (without SAA) and HDLSAA. HDL and HDLSAA were found in such compartments of the receptor-mediated pathway as coated pits, coated vesicles, endosomes and multivesicular bodies and in lipid droplets; no qualitative differences were observed. Therefore, it is unlikely that a defect in binding and uptake of HDLSAA is related to the different susceptibilities of these mouse strains to develop AA-amyloidosis. However, the results do not exclude the possibility that differences in the intracellular processing of SAA following endocytosis of HDLSAA is involved in this differing susceptibility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050204
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  • 7
    Electronic Resource
    Electronic Resource
    Senile amyloidoses of the pituitary and adrenal glands (1996)
    Springer
    Virchows Archiv 429 (1996), S. 293-299 
    Details
    ISSN: 1432-2307
    Keywords: Intracellular amyloid ; Pituitary ; Adrenal gland ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The pituitary and adrenal glands are a functional endocrine unit affected by local or organ-limited senile amyloid syndromes. These occur as interstitial (pituitary only) or intracellular (pituitary and adrenal) varieties. The pituitary and right adrenal glands of each of 108 consecutive autopsy cases of individuals aged 85 years and over were investigated for the prevalence, distribution and immunostaining characteristics of local amyloid. Intracellular amyloid was detected in 77 (71%) pituitaries and 73 (68%) adrenals. Interstitial amyloid was found in 86 pituitaries (80%). Immunohistochemical studies, investigating different amyloid fibril proteins, amyloid P component, ubiquitin, intermediate filaments and pituitary hormones, failed to demonstrate any similarities, and a common origin is unlikely. Statistical analyses demonstrated significant correlations between the occurrences of all three local amyloids. The clinical and histopathological significance of local pituitary and adrenal amyloid remains obscure. The results suggested that the pathogenesis of the local senile amyloidoses of the pituitary and adrenals may be influenced by a common, still uncharacterized variable. It is not clear whether this variable also contributes to the pathogenesis of other senile amyloid syndromes, such as those associated with Alzheimers' disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198345
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  • 8
    Electronic Resource
    Electronic Resource
    Amyloid: Mikroskopischer Nachweis, Klassifikation und klinischer Bezug (1998)
    Springer
    Der Pathologe 19 (1998), S. 345-354 
    Details
    ISSN: 1432-1963
    Keywords: Schlüsselwörter Amyloidnachweis ; Amyloidklassifikation ; Immunhistologie ; Key words Amyloid ; Amyloid classification ; Immunostaining ; Amyloidoses
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Amyloid is a biophysically defined, biochemically non-uniform protein which is deposited in the tissue, forming a cross-beta configuration. In paraffin sections it is demonstrated using Congo red staining according to Puchtler et al. and a polarizing microscope with a tension-free clean optic system that shows a typical apple-green birefringence. The identification of amyloid has to be followed by immunostaining for AA, ATTR, Alambda, Akappa and Aβ2 microglobulin and possibly further types of amyloids for classification purposes. Considering the localization, expansion and type localized and generalized types probably can be differentiated. The latter should be correlated to a basic disease. The treatment of the basic disease is the only chance for reducing or eliminating the amyloid deposits. In this review, the modern morphological methods for demonstration and both immunohistological and clinical classification of amyloid and amyloidoses are presented. Rare types are mentioned in the tables.
    Notes: Zusammenfassung Amyloid ist ein biophysikalisch definiertes, biochemisch uneinheitliches Protein, das im Gewebe zumeist extrazellulär in Fibrillenform mit β-Faltblattstruktur abgelagert wird. Es ist in Paraffinschnitten mittels der Kongorotfärbung nach Puchtler et al. [42] an Hand seiner typischen phosphorgrünen Doppelbrechung im Polarisationsmikroskop bei einwandfreier Optik sicher und zweifelsfrei nachzuweisen. Der Nachweis sollte die weitere immunhistologische Aufarbeitung zur Klassifikation nach sich ziehen. Dazu sollten Antikörper gegen AA, ATTR, Alambda, Akappa und evtl. gegen weitere Amyloidtypen eingesetzt werden. Je nach Lage, Ausdehnung und Typ kann dann noch zwischen wahrscheinlich lokalisierten und vermutlich generalisierten Formen unterschieden werden, wobei letztere ggf. einer Grundkrankheit zugeordnet werden. In der Behandlung einer solchen Grundkrankheit liegt die therapeutische Chance zur Reduktion oder gar Eliminierung der Amyloidablagerungen. In der Übersicht wird versucht, den aktuellen Stand über den pathomorphologischen Nachweis sowie die immunhistologische und klinische Klassifikation von Amyloid und Amyloidosen darzulegen. Auf seltenere Formen wird nur tabellarisch eingegangen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002920050296
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  • 9
    Electronic Resource
    Electronic Resource
    56jähriger Patient mit segmental florider Colitis und Colonamyloidose (1999)
    Springer
    Der Internist 40 (1999), S. 668-672 
    Details
    ISSN: 1432-1289
    Keywords: Schlüsselwörter Colonamyloidose ; Chronisch-entzündliche Darmerkrankung ; Ischämische Colitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Zusammenfassung Bei einem 56jährigen Patienten wird 1/97 die Erstdiagnose einer chronisch-entzündlichen Darmerkrankung des Kolons gestellt, die am ehesten einem Morbus Crohn entspricht. Sechs Monate später wird histologisch eine massive Colonamyloidose beschrieben, die retrospektiv bereits bei der Erstmanifestation der Erkrankung vorlag. Weitere Organbeteiligungen können nicht nachgewiesen werden können. Die immunhistochemischen Untersuchungen schließen eine AA-Amyloidose aus. Vermutlich liegt eine Leichtkettenamyloidose vor. Unter Therapie mit 5-ASA befindet sich der Patient seit über einem Jahr in klinischer Remission. Die Amyloidablagerungen persistieren, dagegen findet sich weiterhin kein Anhalt für eine Beteiligung anderer Organsysteme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001080050387
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  • 10
    Electronic Resource
    Electronic Resource
    Improved acoustic emission locations (1986)
    Springer
    Journal of nondestructive evaluation 5 (1986), S. 133-143 
    Details
    ISSN: 1573-4862
    Keywords: Acoustic emission location ; anisotropic velocity ; transducer size effects ; rock deformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Mathematics
    Notes: Abstract Acoustic emission locations have been determined in a modest-size specimen of Westerly granite (∼ 50×50×200 mm) under uniaxial compressive loading to failure. Periodically during the experiment acoustic pulses were transmitted from a set of source transducers to an acoustic emission receiver array. Axial and transverse velocities were determined from these transmission data. The piezoelectric transducers used in this study were too large to be treated as points. A separate experiment was performed to determine the effect of finite transducer size and incident angle on observed arrival times. Velocity pulse arrival times were inverted for the known source transducer positions using (1) an isotropic, fixed velocity model, (2) the observed anisotropic, stress dependent velocity field, and (3) transducer size corrections. Incorporation of the observed velocity field and transducer size effects dramatically improved location accuracy. Acoustic emissions were located using this technique. Synthetic data, exact and with realistic “errors,” were inverted to determine location uncertainties at various locations throughout the sample. Suggestions are made for further improvements.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00570622
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