Amyloid P-component (protein AP) in localized amyloidosis as revealed by an immunocytochemical method.
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Amyloid↗
Biomedical subjects
P Westermark
Publications and source records attributed to P Westermark.
Further structural and antigenic studies of light-chain amyloid proteins.
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 V lambda IV Bence-Jones protein and a previously described A lambda IV amyloid protein. The two A lambda IV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-A lambda IV antiserum raised against one or the other of the two proteins. In addition, another new A lambda V amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the A lambda V 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.
Amino Acid Sequence↗
Structure and antigenic behaviour of kappa I-immunoglobulin light-chain amyloid proteins.
N-terminal amino acid sequence analysis of three amyloid fibril subunit proteins from three different patients revealed a primary structure homologous to KI immunoglobulin light chains. In double immunodiffusion an antiserum against one of these amyloid proteins reacted with all three amyloids showing one line of identity, while an antiserum against one of the other amyloid proteins reacted with only one of the nonhomologous amyloids, appearing as partial identity, These two antisera did not react with any amyloid of lambda I, lambda IV or lambda VI type. The results confirm previous experiments, in which it has been shown that some antisera against amyloid proteins of immunoglobulin origin give a reaction of identity with other amyloids in the same immunoglobulin subgroup, probably owing to subgroup specific antigenic determinants in the variable segments. It was found that the distribution of amyloid varied widely among the three patients. There does not seem to be any correlation between the type of manifestation of amyloidosis and the type of immunoglobulin light chain forming the amyloid fibril.
Aged↗
The Rombo syndrome: a familial disorder with vermiculate atrophoderma, milia, hypotrichosis, trichoepitheliomas, basal cell carcinomas and peripheral vasodilation with cyanosis.
This hitherto unknown and dominantly inherited disorder is characterized by vermiculate atrophoderma, milia, hypotrichosis, trichoepitheliomas, basal cell carcinomas and peripheral vasodilation with cyanosis. It has been present in the family reported for at least four generations. The lesions become visible in late childhood and are most pronounced on the face. Basal cell carcinomas may develop around the age of 35. Histological observations during the early stage include irregularly distributed and atrophic hair follicles, milia, dilated dermal vessels, lack of elastin or elastin in clumps. After light irradiation a tendency to increased repair activity was observed both in epidermis and in the dermal fibroblasts. On exposure to cold the change in the skin temperature of the hands compared with that in the controls was insignificant. The response to adrenalin iontophoresis was weak.
Abnormalities, Multiple↗
Bullous amyloidosis.
The distribution pattern of amyloid deposition varies greatly in systemic amyloidosis. In primary and myeloma-associated amyloidosis, skin manifestations are common. Three patients with myeloma-associated amyloidosis had bullae or signs of increased skin fragility caused by cleavage in extensive dermal amyloid deposits. The bullae in bullous amyloidosis are, therefore, unique since they are intradermal, not subepidermal.
Aged↗
Senile cardiac amyloid: evidence that fibrils contain a protein immunologically related to prealbumin.
Antiserum specific for human prealbumin (HPA) was studied by indirect immunofluorescence on tissue sections of cardiac ventricles containing senile cardiac amyloid. The pattern of reactivity was identical to that previously reported for an antiserum specific for protein ASc1 (formerly designated ASCA present in these tissues. Anti-HPA failed to react with isolated atrial amyloid (IAA), primary amyloid (A lambda I, A lambda IV, A lambda VI), secondary amyloid (AA), amyloid associated with medullary carcinoma of the thyroid (AEt), pancreatic amyloid associated with adult onset diabetes, cerebral amyloid present in Alzheimer's disease or lichen amyloid. THe reaction of anti-HPA was completely blocked by purified human prealbumin but was not influenced by absorption with purified human albumin or proteins extracted from any amyloid types tested. The anti-HPA reaction was also completely blocked by purified protein ASc1, and the reaction of anti-ASc1 was similarly blocked by purified HPA. These studies suggest that senile cardiac amyloid of the ASc1 type contains prealbumin or a protein antigenically closely related to this molecule.
Aged↗
Immunocytochemical study of argyrophil (Sevier Munger) endocrine cells of adult human pancreas.
Bouin-fixed tissues from non-diabetic adult human pancreata display an argyrophil reaction mainly in the periphery of the islets with the silver technique of Sevier-Munger. The nature of these argyrophil cells was examined after restaining by an indirect immunocytochemical method using antibodies against insulin, glucagon, somatostatin and pancreatic polypeptide. After this procedure the argyrophil cells were identified as glucagon (A-) cells and pancreatic polypeptide (PP-) cells, although the latter exhibited a weaker reaction. The insulin (B-) cells and somatostatin (D-) cells were unreactive. The results show that the Seiver-Munger stain is of equal value to the Grimelius silver nitrate stain in adult human pancreatic islets after fixation in Bouin's fluid.
Aged↗
Senile cardiac amyloid is related to prealbumin.
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.
Aged↗
Senile amyloidosis: a protean manifestation of the aging process.
Senile amyloidosis represents a group of diseases which, while sharing features common to other forms of amyloidosis, are unique and differ from one another in their morphology, biochemical behaviour, protein components, and organ distribution. Although the exact prevalence of various forms of this group of amyloidosis is not yet known, it appears that some forms are extremely common in elderly patients and in many patients may have no clinical significance.
Aged↗
[A case of amyloidosis with unusual clinical manifestation].
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Aged↗
Senile cardiac amyloidosis: evidence of two different amyloid substances in the ageing heart.
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 artrial amyloidosis, 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.
Aged↗
Characterization of amyloid of ageing obese-hyperglycaemic mice and their lean littermates.
Amyloid fibrils, 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.
Aging↗
Demonstration of protein AA in subcutaneous fat tissue obtained by fine needle biopsy.
Polarisation microscopy of material obtained by fine needle biopsy of subcutaneous tissue and stained with Congo red is a simple and reliable method for the diagnosis of systemic amyloidosis. It cannot, however, be used to differentiate histologically between different forms of amyloidosis. In the present study extracts of material obtained by fine needle biopsy of subcutaneous fat tissue from 13 patients were examined by double immunodiffusion with an antiserum against protein AA, a unique protein which forms a major part of the fibrils in secondary amyloidosis. Five of the patients showed amyloid deposits round the fat cells by conventional microscopy. In 3 of these, all with rheumatoid arthritis, protein AA was detected. Eight patients without amyloidosis and 2 with myelomatosis and amyloidosis showed no reaction with antiprotein AA antiserum. Thus the material obtained by fine needle biopsy of subcutaneous tissue could be used not only for the histological diagnosis of amyloidosis but also for a classification of systemic amyloidosis into secondary or primary based on the type of amyloid fibril protein involved.
Adipose Tissue↗
Granulomatous inflammation of the vulva and penis--a genital counterpart to cheilitis granulomatosa.
3 patients are described, in whom chronic swelling of the external genitals occurred after recurrent infections. The histological findings were identical to those seen in cheilitis granulomatosa, the dermal component of Melkersson-Rosenthal syndrome. The authors suppose that the disease of the 3 patients is a genital counterpart to cheilitis granulomatosa, and the name vulvitis or posthitis granulomatosa is suggested.
Adult↗
Substance P and enteroglucagon-like immunoreactivity in argentaffin and argyrophil midgut carcinoid tumours.
The presence of serotonin, substance P and enteroglucagon was investigated in 8 argentaffin and argyrophil midgut carcinoid tumours. All tumours were argentaffin and displayed formalin-induced fluorescence indicating a content of serotonin. In addition, all 8 tumours showed substance P immunoreactivity and 7 of them enteroglucagon immunoreactivity. The results indicate that the midgut carcinoid tumours are as a rule multihormonal.
Aged↗
Morphologic and chemical variation of the kidney lesions in amyloidosis secondary to rheumatoid arthritis.
The kidneys of 20 patients who died of secondary systemic amyloidosis due to rheumatoid arthritis were studied histologically, and four of these were shown to have an uncommon pattern of deposition with almost no glomerular involvement but heavy deposits in the outer zone of the medulla. In three of the four patients frozen tissue was available. Immunochemical characterization of amyloid fibrils from these three cases showed that the major subunit amyloid fibril protein was protein AA, typical of secondary amyloidosis. Gel chromatography of fibrils revealed an uncommon elution pattern with two retarded major protein peaks. Both these proteins showed immunologic identity with protein AA and had N-terminal amino acid sequences identical with that protein but differed in size obviously due to a shortening of the C-terminal in one of the proteins. The reason for the correlation between the pattern of deposition of amyloid and alterations in protein AA is unclear but might be due to variations in enzymes responsible for the cleavage of the amyloid fibril subunit precursor protein SAA.
Amino Acid Sequence↗
Amyloidosis of the skin: a comparison between localized and systemic amyloidosis.
Skin biopsies from patients with different forms of localized and systemic amyloidoses were studied. Subepidermal deposits, typical of lichen amyloidosus, were also seen in other types of amyloidosis, least frequent in the secondary systemic form. Amyloid within the epidermis and especially the horny layer as well as pigmented cells close to the deposits were found in all cases of lichen amyloidosus but in no other specimens. Plasma cells, on the other hand, were numerous in nodular amyloidosis but were not found in any other cases. It is concluded that in the pathogenesis of lichen amyloidosus the epidermis and perhaps dermal melanocytes are involved. In the pathogenesis of localized nocular amyloidosis the plasma cells might be of importance.
Amyloidosis↗
[Diagnosis in amyloidosis].
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Adipose Tissue↗