potassium-permanganate and Amyloidosis

potassium-permanganate has been researched along with Amyloidosis* in 33 studies

Reviews

2 review(s) available for potassium-permanganate and Amyloidosis

ArticleYear
Waldenström's macroglobulinemia associated with AA amyloidosis.
    International journal of hematology, 2001, Volume: 74, Issue:1

    It is widely accepted that amyloidosis in Waldenström's macroglobulinemia (WM) is exclusively due to amyloid light-chain deposition. However, only a small number of previous reports have actually characterized the type of amyloid in WM. We now report the third patient with WM and amyloid A protein (AA) amyloidosis. This patient developed malabsorption, nephrotic syndrome, and orthostatic hypotension. AA was immunohistochemically demonstrated in the rectal biopsy. In conjunction with previous examples of AA amyloidosis, the present report raises the possibility that AA amyloidosis may also occur in WM patients.

    Topics: Aged; Amyloidosis; Coloring Agents; Congo Red; Fatal Outcome; Humans; Male; Potassium Permanganate; Serum Amyloid A Protein; Waldenstrom Macroglobulinemia

2001
Amyloidosis: Part 1.
    International journal of dermatology, 1980, Volume: 19, Issue:10

    Topics: Amyloid; Amyloidosis; Bence Jones Protein; Congo Red; Female; Gentian Violet; Glycoproteins; Humans; Male; Middle Aged; Potassium Permanganate; Serum Amyloid A Protein; Staining and Labeling

1980

Other Studies

31 other study(ies) available for potassium-permanganate and Amyloidosis

ArticleYear
Head and neck amyloidosis: clinicopathological features and immunohistochemical analysis of 14 cases.
    Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology, 2012, Volume: 41, Issue:2

    Amyloidosis is associated with or caused by amyloid deposition. These fibrillar proteins may be deposited extracellularly causing tissue damage or impairment.. The aim of the study was to retrospectively review pathology archives in two oral diagnostic centers for cases fulfilling criteria of amyloidosis and to differentiate AA and AL types of amyloidosis.. The clinicopathological features, alkaline Congo red staining, with and without pretreatment with potassium permanganate, and immunohistochemical (IHC) staining with anti-AA, anti-kappa (κ), and anti-lambda (λ) light chain antibodies were carried out and analyzed.. The search identified 14 cases. Ten patients were women and four were men, with a mean age of 58 years. Eleven patients had systemic involvement by amyloidosis (associated either with multiple myeloma or plasma cell dyscrasia/monoclonal gammopathies), while three presented the localized type, one of them associated with plasmacytoma. All cases showed positivity for κ or λ light chains (AL-amyloid) and presented resistance to the potassium permanganate pretreatment.. Our results show that the head and neck region is preferentially affected by systemic AL-amyloidosis, usually associated with plasma cell dyscrasia. Interestingly, two cases affected by inflammatory rheumatic diseases presented AL-amyloid deposition. Moreover, even after pretreatment with potassium permanganate, which was helpful in highlighting the presence of AL-amyloid, in agreement with the IHC findings, clinical classifications should be carefully made in systemic amyloidosis.

    Topics: Adult; Aged; Aged, 80 and over; Amyloid; Amyloidosis; Coloring Agents; Congo Red; Face; Female; Follow-Up Studies; Humans; Immunoglobulin kappa-Chains; Immunoglobulin lambda-Chains; Indicators and Reagents; Lip Diseases; Male; Middle Aged; Monoclonal Gammopathy of Undetermined Significance; Mouth Diseases; Multiple Myeloma; Neck; Palate; Paraproteinemias; Potassium Permanganate; Retrospective Studies; Serum Amyloid A Protein; Tongue Diseases

2012
Histochemical and immunohistochemical differential diagnosis of amyloidosis--a brief illustrated essay and personal experience with Romhányi's method.
    Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2000, Volume: 7, Issue:3

    The histochemical and immunohistochemical differential diagnosis of amyloidosis in surgical pathology in a referral center is presented. Different forms of amyloidosis are considered e.g. systemic generalized amyloidosis: secondary (AA), primary (AL), senile, hemodialysis-associated, hereditary and organ (tissue)-limited (localized) amyloidosis: cerebral, dystrophic (age-related, so-called "senile"), endocrine-related, localized to tumours, focal (concentrated secretion), and isolated plasma cell (solitary plasmacytoma, B-cell) dyscrasia related amyloidosis. The amyloid deposits were identified and characterized histochemically by Congo red staining after performate pre-treatment at 20 degrees C for 1, 3, 5, 10, 15, 20 or 25 sec, and with oxidation induced proteolysis by trypsin digestion at 20 degrees C for 5, 10, or 30 sec, 1, 2, 3, 4, 5, 6 or 10 min and covered with gum-arabic according to Romhányi, and confirmed by streptavidin-biotin-complex/horseradish peroxidase immunohistochemical reactions. The "sensitivity" or "resistance" to pre-treatment of amyloid deposits depends on the type of amyloid, and the length of pre-treatment. Secondary (AA) amyloid is sensitive to KMnO4 oxidation, followed by trypsin digestion (for 1 min), and its green birefringence under polarized light disappears, while primary (AL) (for 1-5 min), senile (for 1-10 min), and most forms of organ (tissue)-limited (localized) amyloid (for 1-10 min) are resistant. Performate pre-treatment is followed by pronounced congophilia. Secondary (AA) is sensitive to performate pre-treatment (for 1 sec), while primary (AL) amyloid (for 1-20 sec), senile (for 1-25 sec), and most forms of organ (tissue)-limited (localized, isolated) amyloid deposits (for 1-25 sec) are resistant, and are constantly positively birefringent. Early identification and differentiation of amyloid deposits is important for the prognosis and for the choice of therapy. The authors conclude that the presented classical histochemical methods are useful as first line screens for the histological identification of amyloidosis.

    Topics: Amyloid; Amyloid beta-Peptides; Amyloidosis; Autoimmune Diseases; Autopsy; Biopsy; Birefringence; Coloring Agents; Congo Red; Diagnosis, Differential; Formates; Humans; Immunoenzyme Techniques; Immunoglobulin kappa-Chains; Organ Specificity; Potassium Permanganate; Reproducibility of Results; Serum Amyloid A Protein; Serum Amyloid P-Component; Staining and Labeling; Trypsin

2000
The systemic amyloidoses.
    The New England journal of medicine, 1998, Jan-22, Volume: 338, Issue:4

    Topics: Amyloid; Amyloidosis; Coloring Agents; Humans; Potassium Permanganate; Staining and Labeling

1998
A simple histological method differentiating AL-type from AA-type amyloidosis.
    Nephron, 1998, Volume: 78, Issue:2

    Topics: Adult; Aged; Aged, 80 and over; Amyloid; Amyloidosis; Benzothiazoles; Female; Fluorescent Antibody Technique, Indirect; Histocytochemistry; Histological Techniques; Humans; Kidney; Male; Middle Aged; Potassium Permanganate; Serum Amyloid A Protein; Thiazoles

1998
Potassium permanganate resistant amyloid in fine-needle aspirate of the liver.
    Diagnostic cytopathology, 1994, Volume: 10, Issue:4

    A case of primary amyloidosis, initially detected by fine-needle aspiration of the liver, is reported here. Amorphous acellular metachromatic material was seen extracellularly in between the hepatocytic cords compressing them. This material showed typical apple-green birefringence under crossed bipolars after alkaline Congo-red staining proved its amyloid nature. It was resistant to potassium permanganate pretreatment, indicating it to be of the AL type.

    Topics: Amyloid; Amyloidosis; Biopsy, Needle; Humans; Liver; Liver Diseases; Male; Middle Aged; Potassium Permanganate

1994
Immunohistochemical classification of 140 autopsy cases with systemic amyloidosis.
    Pathology international, 1994, Volume: 44, Issue:5

    One hundred and forty autopsy cases of systemic amyloidosis were examined using the potassium permanganate method for distinction of amyloid A protein from other amyloid proteins and an immunohistochemical technique. Of those cases, amyloid proteins were identified in 121 cases. There were 68 cases of amyloid A-related (AA) amyloidosis and these were the most common type among the cases (56.2%). There were 39 cases of immunoglobulin light chain-related (AL) amyloidosis (32.2%), six cases of beta 2-microglobulin-related (A beta 2M) amyloidosis (5%), and five cases of transthyretin-related (ATTR) amyloidosis (4.1%). Minute areas of amyloid deposits in four cases with AA were resistant to potassium permanganate pretreatment. In A beta 2M amyloidosis amyloid deposits were either resistant or sensitive to potassium permanganate pretreatment, from case to case. The coexistence of two different amyloid proteins was seen in three cases: one case had ATTR and A kappa types, and two cases had A beta 2M and AA types. Some discrepancies were seen between the immunohistochemical typing and clinical classification of amyloidosis referred to in the Annual of the Pathological Autopsy Cases in Japan, for example, one case of AA type in myeloma-associated amyloidosis and one case of AL type in secondary amyloidosis. From the present results, the importance of the immunohistochemical method in classifying amyloidosis is stressed.

    Topics: Adult; Aged; Aged, 80 and over; Amyloid; Amyloidosis; beta 2-Microglobulin; Female; Humans; Immunohistochemistry; Male; Middle Aged; Potassium Permanganate; Prealbumin; Serum Amyloid A Protein

1994
[Systemic amyloidosis: clinico-pathologic study of 69 cases].
    Revista clinica espanola, 1992, Volume: 191, Issue:4

    A series of 69 cases of systemic amyloidosis is discussed (12 primaries; 7 due to myeloma; 44 reactive; 5 due to familiar mediterranean fever and 1 portuguese familiar polyneuropathy) in which their clinical aspects, topographical distribution of the deposit and histochemical characteristics are studied using the potassium permanganate technique. According to sings and symptoms of presentation and topography there is a remarkable overlapping in the five types of amyloidosis. Only macroglossia was more frequent in primary amyloidosis (p less than 0.001). However the potassium permanganate technique can help in the classification. Considering the first clinical diagnosis. 83% of primary amyloidosis and 100% of amyloidosis due to myeloma, were resistant to permanganate. 84% of reactive amyloidosis and 100% of familiar mediterranean fever, were sensitive. The only case of portuguese familiar polyneuropathy showed resistance.

    Topics: Adolescent; Adult; Aged; Aged, 80 and over; Amyloidosis; Female; Histocytochemistry; Humans; Male; Middle Aged; Potassium Permanganate

1992
The pattern of amyloidosis in a Malaysian patient population.
    Histopathology, 1991, Volume: 18, Issue:2

    Congo red screening of 27,052 routine biopsy specimens from 22,827 patients over a 5 1/2-year period in the Department of Pathology, University of Malaya detected 186 cases of amyloidosis. The categories of amyloidosis encountered and their prevalences in relation to each other were: systemic AL (5.9%); systemic AA (3.2%); isolated atrial (14%); primary localized cutaneous (7.5%); other primary localized deposits (3.2%); localized intratumour (58%); and dystrophic (8.6%). A third of patients with systemic AL amyloidosis had coexistent immunocyte abnormality. The commonest underlying pathology for systemic AA amyloidosis was leprosy. Notable among the types of localized amyloidosis revealed by this study were isolated atrial amyloidosis, which appeared to complicate chronic rheumatic heart disease, and intratumour amyloidosis complicating nasopharyngeal carcinoma. Other tumours in which amyloid deposits were observed included basal cell carcinoma, islet cell tumour and medullary carcinoma of the thyroid. Dystrophic amyloidosis was observed in fibrotic tissues, such as damaged cardiac valves and osteoarthritic joints. Heredofamilial amyloidosis, senile systemic amyloidosis and degenerative cerebral amyloidosis were notably absent from this study.

    Topics: Adolescent; Adult; Aged; Aged, 80 and over; Amyloid; Amyloidosis; Cardiomyopathies; Child; Humans; Immunoglobulin kappa-Chains; Immunoglobulin lambda-Chains; Immunohistochemistry; Malaysia; Microscopy, Electron; Middle Aged; Neoplasms; Potassium Permanganate; Prevalence; Skin Diseases

1991
Morphological and immunohistochemical findings in dialysis-related amyloidosis. An analysis of 16 cases.
    Applied pathology, 1989, Volume: 7, Issue:6

    The morphologic features of amyloidosis associated with long-term hemodialysis for chronic renal failure were studied in a series of 16 patients in all of whom immunohistochemical evidence of beta 2-microglobulin-related amyloidosis was obtained. Osteoarticular involvement was present in 15 cases, as demonstrated in synovial biopsies, articular fluid sediments, three surgically obtained femoral heads, and 1 autopsied case. Amyloid was found in synovial membrane, articular cartilage and capsule. Osseous lesions due to amyloid infiltration were found in 2 cases with spontaneous fracture of the femoral neck. Thirteen patients had also amyloid in tissues obtained from carpal tunnel. Systemic involvement was demonstrated in 8 patients by means of rectal biopsies, abdominal fat aspiration biopsies, surgical specimens and autopsy. Deposition in the muscular layer of the gastrointestinal tract was found in 3 cases. Nodular subendothelial deposits in vessels of multiple sites seem to be characteristic of this type of amyloidosis. Immunohistochemical reactions for beta 2-microglobulin and P component were strongly positive in amyloid deposits of all cases. According to our results, abdominal fat aspiration biopsy has little value for screening purposes, whereas the study of articular fluid sediment is highly sensitive as a diagnostic method in patients with articular effusions.

    Topics: Acute Kidney Injury; Adult; Aged; Amyloidosis; beta 2-Microglobulin; Female; Humans; Immunohistochemistry; Male; Middle Aged; Potassium Permanganate; Renal Dialysis

1989
[Methods for verifying forms of amyloidosis by a pathologist].
    Arkhiv patologii, 1989, Volume: 51, Issue:1

    Potassium permanganate reaction, immunohistochemical assay using immune sera, and autoclave method combined with alkaline guanidine one are considered to be the most effective methods among those designed for verifying forms (primary, secondary, hereditary, senile systemic) of systemic amyloidosis.

    Topics: Amyloidosis; Diagnosis, Differential; Guanidine; Guanidines; Humans; Immunohistochemistry; Potassium Permanganate

1989
Morphologic differences in the pattern of liver infiltration between systemic AL and AA amyloidosis.
    Human pathology, 1988, Volume: 19, Issue:6

    Biopsy and necropsy tissue from 31 unselected patients with systemic amyloidosis, in which there was histologic evidence of liver involvement, were reviewed with reference to the location and pattern of amyloid deposition in the liver. Amyloidosis was classified into AA and AL types on the basis of immunohistochemistry and permanganate reaction of the amyloid deposits. Nineteen were categorized as AA (secondary) and 12 as AL (primary) amyloidosis. Deposition of AA amyloid was limited to the walls of vessels in the portal tract, constituting a "vascular" pattern. In AL amyloidosis, the deposits exhibited a "sinusoidal" pattern in that they were seen along hepatic sinusoids as well as in vessel walls. This difference was statistically significant (P less than .001). The histologic pattern of liver infiltration offers a valuable clue in the classification of systemic amyloidosis and provides information that may be useful in the selection of patients for therapy.

    Topics: Amyloid; Amyloidosis; Congo Red; Hepatic Artery; Humans; Liver; Potassium Permanganate; Staining and Labeling

1988
[Discriminative value of potassium permanganate staining in systemic amyloidosis].
    Revista clinica espanola, 1987, Volume: 180, Issue:3

    Topics: Amyloidosis; Humans; Potassium Permanganate; Staining and Labeling

1987
Demonstration and classification of amyloidosis in needle biopsies of the kidneys, with special reference to amyloidosis of the AA-type.
    Acta pathologica, microbiologica, et immunologica Scandinavica. Section A, Pathology, 1987, Volume: 95, Issue:6

    To examine whether sequence-specific antibodies directed against serum amyloid A were useful in the demonstration and classification of amyloidosis, needle biopsy specimens from the kidneys of 152 cases with renal disorders were investigated using the avidin-biotin-peroxidase complex technique of immunohistochemistry. A distinct immunoreactivity of protein AA was seen in biopsies from all 42 individuals who were clinically classified as having the AA-type of amyloidosis. The stained areas coincided with deposits stained by Congo red. Four of these cases demonstrated immunoreactivity of both protein AA and light immunoglobulin chains and all biopsies except one showed immunoreactivity for the amyloid P-component. After treatment with potassium permanganate, the amyloid deposits in the biopsies of all 42 cases lost their affinity for Congo red. Ten patients with clinical and laboratory findings compatible with the AL-type of amyloidosis were also investigated. All their biopsies demonstrated Congophilic amyloid deposits but none of them showed any immunoreactivity of protein AA. Amyloid deposits of lambda light immunoglobulin chains-but not kappa-were demonstrated in biopsies from four patients. The amyloid P-component was found in biopsies from six individuals and positive Congo red staining after treatment with potassium permanganate was seen in biopsies from four of the cases. Biopsies of 100 patients suffering from non-amyloid renal disorders were also examined. None of them displayed any immunoreactive deposits of protein AA. The investigation shows that amyloid deposits of the AA-type can be identified in needle biopsies when sequence-specific antibodies against serum amyloid A are used in the avidin-biotin-peroxidase complex technique. Both the diagnostic sensitivity (42 of 42) and specificity (110 of 110) of the assay were optimal (1.0). The method was found to be superior to other investigated techniques and useful for classifying amyloidosis in formalin-fixed renal biopsies.

    Topics: Amyloidosis; Biopsy, Needle; Humans; Immunoglobulin kappa-Chains; Immunoglobulin lambda-Chains; Kidney; Potassium Permanganate; Serum Amyloid A Protein; Serum Amyloid P-Component

1987
An investigation of the protein components of amyloid using immunoperoxidase and permanganate methods on tissue sections.
    Pathology, 1986, Volume: 18, Issue:1

    Amyloid deposits in tissue from 8 patients with generalized primary amyloidosis, 11 patients with generalized secondary amyloidosis, 11 nasopharyngeal carcinomas, 11 basal cell carcinomas, 4 islet cell tumours, 4 medullary carcinomas of the thyroid and 9 cases of lichen amyloidosis were studied using the indirect immunoperoxidase and peroxidase-antiperoxidase methods with specific antisera against Amyloid A (AA) protein and human immunoglobulin lambda and kappa light chains. The permanganate method of Wright was also applied to tissue sections. Positive staining for AA protein was observed only in secondary amyloidosis. There was excellent correlation between AA positivity and permanganate sensitivity. Positivity for immunoglobulin light chains was not observed in secondary amyloidosis but was noted in 5 (63%) cases of primary amyloidosis and 18-27% of intratumour amyloidosis. Lichen amyloidosis did not stain for AA protein or light chains. It is shown that assessment of the permanganate reaction and AA positivity of amyloid deposits can reliably differentiate secondary from primary amyloidosis and may contribute significantly to selection of patients for appropriate therapy.

    Topics: Amyloid; Amyloidosis; Humans; Immunoenzyme Techniques; Immunoglobulin Light Chains; Potassium Permanganate; Serum Amyloid A Protein; Staining and Labeling

1986
Pathologic fractures associated with idiopathic amyloidosis of bone in chronic hemodialysis patients.
    Nephron, 1986, Volume: 43, Issue:1

    Amyloid bone lesions were found in 2 chronic hemodialysis patients presenting with pathologic hip fractures. These amyloid deposits were noted as lytic defects on plain skeletal radiographs. No evidence for disseminated amyloidosis was discovered on physical examination, skin biopsy, or bone marrow biopsy. Myeloma, other plasma cell dyscrasia, and preceding chronic inflammatory states were not found in either patient. The amyloid deposits had staining characteristics suggestive of secondary amyloid based on the potassium permanganate reaction. Isolated amyloid bone deposits should be included in the differential diagnosis of lytic bone lesions or pathologic fractures in chronic dialysis patients.

    Topics: Aged; Amyloidosis; Bone Diseases; Femoral Neck Fractures; Fractures, Spontaneous; Humans; Kidney Failure, Chronic; Male; Middle Aged; Potassium Permanganate; Renal Dialysis

1986
[Systemic amyloidosis in Hodgkin's disease: presentation of 2 cases].
    Revista clinica espanola, 1986, Volume: 179, Issue:7

    Topics: Adult; Amyloidosis; Antineoplastic Combined Chemotherapy Protocols; Combined Modality Therapy; Congo Red; Hodgkin Disease; Humans; Male; Middle Aged; Potassium Permanganate

1986
Secondary (AA) amyloidosis in cystic fibrosis. A report of three cases.
    American journal of clinical pathology, 1986, Volume: 85, Issue:4

    The authors report the pathologic features of three cases of amyloidosis associated with cystic fibrosis. Renal biopsy led to the diagnosis (case 1) or suspicion (case 2) of amyloidosis in patients who were 23 and 21 years old, respectively. The third patient died at age 22 years, and amyloidosis was not discovered until autopsy. Immunohistochemical staining and potassium-permanganate pretreatment of histologic sections in all three cases provided evidence that the amyloid seen in these patients is of the secondary (AA) type. Congo red staining in each case and electron microscopy in case 1 confirmed the initial diagnosis of amyloidosis. A markedly elevated serum amyloid A protein (160 micrograms/mL; normal less than 1 microgram/mL) in case 1 indicated the presence of large quantities of the precursor protein from which the AA fibrils of secondary amyloid are derived. The kidneys, spleen, and liver contained amyloid deposits in autopsy material from all three cases. Involvement of other organs by amyloid was variable. Review of autopsy material in Boston from 23 additional cystic fibrosis patients with long-term survival did not reveal any evidence of amyloidosis. It appears that secondary amyloidosis is emerging as a significant, although rare, complication of cystic fibrosis as greater numbers of these patients survive into adulthood.

    Topics: Adult; Amyloidosis; Biopsy; Congo Red; Cystic Fibrosis; Histocytochemistry; Humans; Kidney; Microscopy, Electron; Potassium Permanganate

1986
[Usefulness of potassium permanganate staining in the classification of systemic amyloidoses].
    Medicina clinica, 1985, Mar-02, Volume: 84, Issue:8

    Topics: Adolescent; Adult; Aged; Amyloid; Amyloidosis; Child; Congo Red; Female; Humans; Male; Middle Aged; Potassium Permanganate; Serum Amyloid A Protein; Staining and Labeling

1985
Classification of amyloidosis: immunohistochemistry versus the potassium permanganate method in differentiating AA from AL amyloidosis.
    Applied pathology, 1985, Volume: 3, Issue:1-2

    As systemic AA and Al amyloidosis differ considerably with regard to prognosis and therapeutic approach, it is of importance to make an accurate histochemical classification with regard to the amyloid protein involved. In the present study the results of the potassium permanganate (KMnO4) method, an indirect histochemical procedure based on differences in cross-beta-potential of different amyloid fibril proteins, were compared with the results of an immunohistochemical method utilizing anti-AA and anti-AP antibodies. Renal biopsy sections of patients with systemic amyloidosis related to inflammatory conditions, systemic amyloidosis associated with plasma cell dyscrasia, idiopathic systemic amyloidosis, and nonamyloidotic controls were studied. Positive reaction of anti-AA was observed on all KMnO4-sensitive amyloid deposits, whereas the KMnO4-resistant amyloid deposits remained unstained, provided that highly purified anti-AA antiserum was used. Anti-AP produced not only comparable staining of both KMnO4-sensitive and -resistant amyloid deposits, but also of glomerular basement membranes and elastin layers of blood vessels in amyloid and control biopsies. The intensity of anti-AP reactivity was comparable with the reaction of anti-AA on KMnO4-sensitive amyloid deposits. The present results confirm the specificity of the KMnO4 method, which is a simple method available to every laboratory, in differentiating between AA and AL amyloidosis. Furthermore, the results indicate that, at least in renal biopsy specimens, anti-AP may serve as a general marker for AA and AL amyloid deposition; this finding is in contrast to the results of a recently published report.

    Topics: Amyloid; Amyloidosis; Antibody Specificity; Congo Red; Enzyme-Linked Immunosorbent Assay; Female; Histocytochemistry; Humans; Immunoenzyme Techniques; Male; Potassium Permanganate; Serum Amyloid A Protein

1985
[Use of the potassium permanganate technique in the differential diagnosis of amyloidoses].
    Medicina clinica, 1985, Mar-02, Volume: 84, Issue:8

    Topics: Amyloidosis; Diagnosis, Differential; Humans; Potassium Permanganate

1985
A new method to classify amyloid fibril proteins.
    Acta neuropathologica, 1985, Volume: 67, Issue:3-4

    The permanganate method, the immunoperoxidase method, and a newly developed autoclave method were used to distinguish different types of amyloid fibril proteins in formalin-fixed, paraffin-embedded tissue sections. All tissues from permanganate-sensitive cases (AA type) lost the affinity of Congo red and green birefringence under polarized light after incubation with special autoclave treatment. AL type systemic amyloidosis and amyloid plaques of CJD and GSS were permanganate-resistant, but decreased markedly the affinity of Congo red after prolonged autoclaving. On the other hand, prealbumin type systemic amyloidosis and senile plaques of SDAT were resistant to both permanganate oxidation and prolonged autoclaving. Thus, amyloid plaques of CJD and GSS are identical to AL type in systemic amyloidosis, and senile plaques are similar to the prealbumin type. However, anti-prealbumin antiserum did not stain senile plaque amyloid. The anti-human P component stained positively systemic amyloids and cerebral amyloid plaques of SSE, but failed to stain senile plaques of SDAT. Therefore, the amyloid fibril protein of senile plaques is apparently different from other types of amyloid depositions. Amyloid plaques of SSE are different from senile plaques not only with regard to fibril proteins, but also to globular protein in the amyloid.

    Topics: Adolescent; Adult; Aged; Amyloid; Amyloidosis; Brain; Female; Histocytochemistry; Humans; Immunochemistry; Male; Methods; Middle Aged; Potassium Permanganate

1985
Amyloid deposits in bioprosthetic cardiac valves after long-term implantation in man. A new localization of amyloidosis.
    The American journal of pathology, 1984, Volume: 114, Issue:3

    Congo red staining with microscopic examination under polarized light was performed in 30 porcine bioprosthetic cardiac valves and one autologous fascia lata valve explanted from 31 patients in order to detect the presence of amyloid. Microdeposits of amyloid were present in the sewing ring of the fascia lata valve and in 10 porcine bioprostheses, and this finding was confirmed by transmission electron microscopy in 3 porcine bioprostheses. All amyloid-laden porcine valves had been implanted for at least 33 months before removal, and all except two showed dysfunction and/or severe degeneration of cuspal tissue. Statistical analyses failed to establish any correlation between the presence of amyloid and patient-related factors. In a majority of porcine bioprostheses amyloid was permanganate-sensitive and tryptophan-positive. The pathogenesis of this new form of heart valve amyloidosis might consist in penetration of human macrophages in deteriorated bioprosthetic cusps and their interaction with blood-borne amyloid precursors.

    Topics: Adolescent; Adult; Aged; Amyloid; Amyloidosis; Aortic Valve; Child; Female; Heart Valve Diseases; Heart Valve Prosthesis; Histocytochemistry; Humans; Long-Term Care; Male; Middle Aged; Mitral Valve; Potassium Permanganate; Tryptophan

1984
Characterization of spontaneous amyloidosis of Syrian hamsters using the potassium permanganate method.
    Laboratory animal science, 1984, Volume: 34, Issue:4

    Amyloid from 16 Syrian hamsters with spontaneous age-related systemic amyloidosis retained affinity for Congo red dye after treatment with potassium permanganate. Serum electrophoresis showed a slight rise in gamma globulins without a monoclonal spike. Bence-Jones proteins were not present in the urine. There was no histological evidence of plasmacytosis. Amyloidosis could not be associated with chronic inflammation. The lack of apparent etiology of this amyloid and its resistance to potassium permanganate treatment suggests that it is a primary non-AA amyloid. This finding varies with a report suggesting that the spontaneous amyloidosis of aged Syrian hamsters is associated with the AA fibril.

    Topics: Amyloid; Amyloidosis; Animals; Cricetinae; Female; Kidney; Male; Mesocricetus; Potassium Permanganate; Rodent Diseases; Serum Amyloid A Protein

1984
Hepatic amyloidosis. An unusual cause of ascites and portal hypertension.
    Archives of internal medicine, 1984, Volume: 144, Issue:11

    I treated a patient who had amyloidosis with predominantly hepatic involvement and portal hypertension. The main clinical features were hepatomegaly, gross ascites, proteinuria, and elevated alkaline phosphatase levels. Despite permanganate-sensitive AA protein being present in the biopsy specimen, none of the recognized disease entities associated with secondary amyloidosis were found. A review of the literature and the mechanism of portal hypertension in amyloidosis is given. It is suggested that elevated portal pressures may be of greater importance in the pathogenesis of ascites in amyloidosis than has been appreciated.

    Topics: Aged; Amyloidosis; Ascites; Female; Fixatives; Hepatomegaly; Humans; Hypertension, Portal; Liver; Potassium Permanganate; Serum Amyloid A Protein

1984
Differentiation of amyloid fibril proteins in tissue sections. Two simple and reliable histological methods applied to fifty-one cases of systemic amyloidosis.
    Acta pathologica japonica, 1982, Volume: 32, Issue:5

    The potassium permanganate method and the unlabeled immunoperoxidase (PAP) method were applied for distinguishing different types of amyloid fibril proteins in conventionally fixed, paraffin-embedded tissue sections obtained from fifty-one autopsied cases of systemic amyloidosis and three control cases of well-analysed fibril proteins. All of the eighteen cases "sensitive" to permanganate treatment, whose amyloid deposits lost completely their affinity to Congo red and birefringence under polarized light, were shown to have AA antigenic determinants by the PAP method. Meanwhile, all of the remaining thirty-three "resistant" cases, where Congo red affinity and birefringence were retained at various degree even only in minimal areas, were negative for AA antigenicity. This indicated the feasibility of potassium permanganate method for the identification of AA protein based on this criterion of "sensitivity". Twenty-eight cases were classified as AA, A lambda, A kappa or AA+[A kappa] the remaining twenty-three cases were unclassified, and there were some discrepancies between the preliminary clinicopathological classification and the protein nature of the amyloid. It is important to differentiate the types of amyloid fibril protein of individual patients because the expedience of selective therapeutic approaches had been suggested. The two methods applied herein are handy and useful for this purpose.

    Topics: Adult; Aged; Amyloid; Amyloidosis; Child; Female; Histocytochemistry; Humans; Immunoenzyme Techniques; Male; Middle Aged; Multiple Myeloma; Potassium Permanganate; Staining and Labeling; Waldenstrom Macroglobulinemia

1982
[Potassium permanganate reaction in amyloidosis].
    Nihon Naika Gakkai zasshi. The Journal of the Japanese Society of Internal Medicine, 1982, Jun-10, Volume: 71, Issue:6

    Topics: Aged; Amyloid; Amyloidosis; Diagnosis, Differential; Female; Histocytochemistry; Humans; Male; Middle Aged; Potassium Permanganate; Staining and Labeling

1982
Permanganate oxidation of senile cerebral amyloid and its relationship to AA protein.
    Acta neuropathologica, 1982, Volume: 58, Issue:4

    Immunoreactivity for AA protein was rarely detected in briefly fixed amyloid of senile plaques and dyshoric angiopathy, but was not observed in Congophilic angiopathy. Plaque and dyshoric amyloid exhibited variable sensitivity to permanganate oxidation; Congophilic angiopathy was resistant to oxidation. In contrast to systemic amyloid composed of AA protein, the rare immunoreactivity of senile cerebral amyloid was lost with prolonged fixation. This study demonstrates that the fibrillar protein of senile cerebral amyloid differs from that of systemic amyloid of AA type.

    Topics: Aged; Alzheimer Disease; Amyloid; Amyloidosis; Brain; Carcinoma; Dementia; Humans; Immunoenzyme Techniques; Middle Aged; Oxidation-Reduction; Potassium Permanganate; Serum Amyloid A Protein; Thyroid Neoplasms

1982
Difference in potassium permanganate sensitivity between primary and secondary amyloidosis.
    The Malaysian journal of pathology, 1981, Volume: 4

    Topics: Amyloidosis; Humans; Potassium Permanganate

1981
The potassium permanganate method. A reliable method for differentiating amyloid AA from other forms of amyloid in routine laboratory practice.
    The American journal of pathology, 1979, Volume: 97, Issue:1

    Alterations in affinity of amyloid for Congo red after incubation of tissue sections with potassium permanganate, as described by Wright el al, were studied. The affinity of amyloid for Congo red after incubation with potassium permanganate did not change in patients with myeloma-associated amyloidosis, familial amyloidotic polyneuropathy, medullary carcinoma of the thyroid, pancreatic island amyloid, and cerebral amyloidosis. Affinity for Congo red was lost after incubation with potassium permanganate in tissue sections from patients with secondary amyloidosis and amyloidosis complicating familial Mediterranean fever (consisting of amyloid AA). Patients with primary amyloidosis could be divided into two groups, one with potassium-permanganate--sensitive and one with potassium-permanganate--resistant amyloid deposits. These two groups correlated with the clinical classification in typical organ distribution (presenting with nephropathy) and atypical organ distribution (presenting with cardiomyopathy, nephropathy, and glossopathy) and the expected presence of amyloid AA or amyloid AL. Potassium permanganate sensitivity seems to be restricted to amyloid AA. The potassium permanganate method can be important in dividing the major forms of generalized amyloidosis in AA amyloid and non-AA amyloid. This can be used for differentiating early stages of the disease and cases otherwise difficult to classify. It is important to define patient groups properly, especially in evaluating the effect of therapeutic measures. (Am J Pathol 97:43--58, 1979).

    Topics: Amyloid; Amyloidosis; Blood Vessels; Congo Red; Diagnosis, Differential; Histocytochemistry; Humans; Kidney; Myocardium; Neurons; Potassium Permanganate; Serum Amyloid A Protein; Thyroid Gland; Tissue Distribution

1979
Potassium permanganate reaction in amyloidosis. A histologic method to assist in differentiating forms of this disease.
    Laboratory investigation; a journal of technical methods and pathology, 1977, Volume: 36, Issue:3

    A simple and reproducible histochemical method for distinguishing different chemical types of amyloid is described. The method is based on the affinity of amyloid for Congo red dye after exposure to potassium permangenate and dilute sulfuric acid. The permanganate method represents a modification of the Romhanyi trypsin technique. It yields comparable results while obviating some of the technical difficulties associated with the latter method. The permanganate reaction was applied to a series of amyloid samples of known amino acid composition, to amyloid samples fixed in a variety of different preservatives, and to tissues obtained at autopsy from 67 amyloidosis patients whose disease had been previously subclassified on the basis of clinical presentation and autopsy observations. This method distinguished amyloid protein AA from other varieties of amyloid and proved effective when applied to amyloid samples preserved in any of several commonly used fixatives. This simple histochemical method proved useful in subclassifying amyloid type in the patient series particularly when used in conjunction with the available clinical history and the organ distribution of amyloid accumulation.

    Topics: Amyloidosis; Cardiomyopathies; Congo Red; Histocytochemistry; Humans; Liver; Lung; Male; Middle Aged; Multiple Myeloma; Potassium Permanganate; Spleen; Tendons; Trypsin

1977
[Fluorescence optical demonstration of amyloid by means of thioflavin S].
    Zentralblatt fur allgemeine Pathologie u. pathologische Anatomie, 1970, Volume: 113, Issue:4

    Topics: Aldehydes; Alloxan; Amino Acids; Amyloid; Amyloidosis; Benzoates; Chemical Phenomena; Chemistry; Flavins; Fluorescent Dyes; Formates; Humans; Hyaluronoglucosaminidase; Hydrochloric Acid; Imides; Indicators and Reagents; Microscopy, Fluorescence; Neuraminic Acids; Oxidation-Reduction; Peptide Hydrolases; Perchlorates; Periodic Acid; Potassium Permanganate; Ribonucleases; Spleen; Sulfhydryl Compounds; Trichloroacetic Acid

1970