Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Demonstration of protein AA in subcutaneous fat tissue obtained by fine needle biopsy. 10 69

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).
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PMID:The potassium permanganate method. A reliable method for differentiating amyloid AA from other forms of amyloid in routine laboratory practice. 49 95

A 67-year-old man was hospitalized with a diagnosis of nephrotic syndrome. Physical findings at admission were generalized edema and macroglossia. Urinalysis showed massive proteinuria, + +occult blood, and granular and broad casts. Ig A lambda monoclonal gammopathy was noted in the serum. There was no evidence of myeloma in the bone marrow aspirate, scintigram or X-ray of the bone. A biopsy specimen of the kidney showed massive deposits of structureless material in the glomeruli. Marked cell infiltration was also observed in the interstitium. Multinucleated giant cells were occasionally seen in the Bowman's capsules and the interstitium. There were reactive changes in the Bowman's capsule adjacent to the giant cell. The deposits were proved to be amyloid by positive staining with Congo red and apple-green birefringence by polarized light. In addition, microfibrills seen on electron microscopy displayed deposits. Amyloid depositions were observed in other tissues such as gingiva, skin and tongue. Staining of amyloid with Congo red was resistant to potassium permanganate, and amyloid was positively stained with lambda-light chain of immunoglobulin. These findings indicated that the patient had primary amyloidosis. Infiltration of the multinucleated giant cell has been reported only in patients with familial amyloidosis and secondary amyloidosis associated with rheumatoid arthritis. To our knowledge the present case is a first report of the giant cell infiltration in a Bowman's capsule in primary amyloidosis.
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PMID:[A case of primary amyloidosis associated with giant cell infiltration within a Bowman's capsule]. 147 13

Primary (idiopathic) or multiple myeloma-associated amyloidosis is characterized by the deposition in tissue of monoclonal light chains or light-chain fragments (AL amyloidosis). In contrast to other types of amyloidosis, information regarding the pathogenesis of light-chain-related amyloid has heretofore been limited due to the lack of a suitable in vivo model. The authors report the successful experimental induction of human AL amyloid deposits. The repeated injection into mice of Bence Jones proteins obtained from two patients with AL amyloidosis produced the histopathologic lesions characteristic of this disease. Partial dehydration of animals before protein injection resulted in the acceleration of amyloid formation. The human proteins were deposited as amyloid within the mouse renal blood vessel walls and parenchymal tissue, as well as in other organs. The deposits were Congo red-positive, exhibited green birefringence, and had a fibrillar ultrastructure. As evidenced immunohistochemically, the experimentally induced amyloid deposits consisted of the injected human light chains, and in addition, contained mouse amyloid P component (AP); mouse immunoglobulin (Ig) or inflammatory-associated amyloid A protein was not detected. Extraction and characterization of the amyloid deposits found within the mouse kidney revealed the presence of a predominantly intact human light polypeptide chain. Mice injected in identical manner with a non-amyloid-associated Bence Jones protein had no or only rare amyloid deposits. The experimental mouse model provides a means to ascertain the amyloidogenic potential of human monoclonal light chains and to study further the pathogenesis of AL amyloidosis.
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PMID:Induction in mice of human light-chain-associated amyloidosis. 154 44

All forms of MIDD are related to the presence of an expanded clone of B-cell origin that is producing an Ig product, usually, but not exclusively an L-chain, which is predisposed to deposit in tissues, with or without some degree of processing. The nature of the processing is currently unclear, although limited proteolysis is likely to play a major role in most, but not all, patients. Diagnosis is made by the identification, using immunohistochemical techniques, of the monoclonal Ig nature of the deposited material, which may be fibrillar and Congo red-positive (AL and AH), or more amorphous and Congo red-negative (LCDD and LCHDD). Present modalities of therapy are similar or identical to those employed in multiple myeloma, attempting to eliminate the monoclonal cell population responsible for the production of the precursor of the deposited protein. A variety of ancillary therapeutic measures may be employed to treat problems associated with the failure of specific organs produced by the deposition. The details of how the uniformly soluble precursor molecule is converted to an essentially insoluble aggregate that compromises the function of the tissue in which it is formed are not yet known. It is still not possible to construct a potential "unified field theory" governing the deposition of intact Igs or their fragments. It is likely, as appears to be the case in other forms of amyloid unrelated to Ig, that many proteins contain, within their sequence, peptides that are capable of forming insoluble beta sheet-like structures. When these peptides are isolated from their surrounding molecular environment--either by proteolysis in the test tube, by a mutational change that predisposes them to limited proteolysis; or by a point mutation, deletion, or some other structural modification (as glycosylation), which alters their molecular context without proteolysis--and are present in sufficient concentration, they become less soluble under physiologic conditions. It is likely that the site of deposition depends upon the site of synthesis, but to a lesser extent than the protease profile and the physicochemical make-up of the affected tissues. Better understanding of the latter factors is necessary for the development of better modes of treatment.
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PMID:Mechanisms of disease: monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease. 158 76

Primary localized amyloidosis was found in a family. A 66-year-old woman had suffered from hoarseness for 18 years. A biopsy specimen from the larynx showed amyloid deposits in the submucosal connective tissue. Her 40-year-old daughter noticed a subcutaneous nodule on her philtrum. Histologic examination showed the deposition of amyloid in the middle and lower dermis, which also encased the blood vessels and epidermal appendages. In both cases the amyloid deposits were positively stained with Congo red and the staining was resistant to potassium permanganate treatment. These amyloid deposits were strongly positive against the anti-amyloid antibody of the lambda light chain. These results indicate that the amyloid substance is derived from protein AL. There was no clinical or laboratory evidence of systemic amyloidosis or multiple myeloma in either patient.
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PMID:Primary localized amyloidosis in one family. 193 75

Histopathological and immunohistochemical studies were performed on 10 autopsy cases of generalized amyloidosis. The results showed that there were 3 cases of secondary amyloidosis (AA protein), 4 cases of primary amyloidosis (AL protein) and 3 cases of amyloidosis associated with multiple myeloma (AL protein); no familial amyloidosis (AF protein) was identified. Amyloid substances detected in all of the cases were similar in appearance morphologically, and differentiation of different types of amyloid proteins could not be depended on whether the disease is primary in nature or there is amyloid deposition in various organs or tissues. Anyhow, the differentiation could be made by pre-treatment with KMnO4 in Congo red stain or by immunoperoxidase stain, and the latter one is considered to be more reliable in identifying amyloid protein types.
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PMID:[Histopathological and immunohistochemical studies of generalized amyloidosis]. 206 74

Monoclonal immunoglobulin deposition occurs in tissues as Congo Red binding fibrils in light chain amyloidosis, as less structured deposits in light chain deposition disease, and as similar but distinct deposits in light and heavy chain deposition disease. The nonamyloid forms were found in 13 patients who had evidence of plasmacytic dyscrasia by the immunohistochemical detection of immunoglobulin light chains of kappa or lambda class (with or without staining for a single heavy chain isotype) and by the absence of amyloid P component in tissue sections that did not show the birefringence characteristic of amyloid after Congo Red staining. All but two of the patients presented with proteinuria with or without azotemia. Clinical syndromes involving other organ systems were less common but occasionally severe. Four patients had overt multiple myeloma. Three others had hypercalcemia and mild bone marrow plasmacytosis but no lytic lesions. Analyses of immunoglobulin synthesis in bone marrow cells from seven patients showed excess light chains in all and incomplete light chains or heavy chain fragments in six, regardless of whether an intact monoclonal protein or related subunit was in the serum or urine. The fibrillar (amyloidotic) and nonfibrillar forms of monoclonal immunoglobulin deposition occur either in overt multiple myeloma or in the course of less neoplastically aggressive plasmacytic dyscrasias. Bone marrow cells from patients with either type produce immunoglobulin fragments that are related to those deposited in the affected tissues.
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PMID:Monoclonal immunoglobulin deposition disease: light chain and light and heavy chain deposition diseases and their relation to light chain amyloidosis. Clinical features, immunopathology, and molecular analysis. 210 17

A 48-year-old Japanese woman died of multiple myeloma (lambda light-chain type) with chronic renal failure. Histological examination revealed deposition of a homogeneous substance and crystals in the kidneys and thyroid gland. The homogeneous substance was stained with Congo red after permanganate treatment but did not stain with antibody to amyloid A protein, and it was recognized as AL-type amyloid. Crystals were not stained with Congo red, but crystals were stained with antibody to the lambda light chain. Since AL-type amyloid is considered to be derived from a myeloma light chain, the present case showed two different types of deposition, both of which were derived from the same myeloma protein.
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PMID:Crystalline light-chain deposition and amyloidosis in the thyroid gland and kidneys of a patient with myeloma. 210 50

We report a 49-year-old woman who developed lobular glomerulonephritis with prevalent deposition of material positive for IgG, C1q and lambda light chain, but which was not stained by Congo red. Glomeruli revealed massive electron-dense deposits with a microlamellar structure in the mesangial matrix and peripheral capillary loops. Clinically, the patient had nephrotic syndrome, microhematuria and hypertension. No Bence-Jones protein or cryoglobulin was found in the urine or serum. Anti-DNA antibody was positive, but systemic lupus erythematosus (SLE) was ruled out by repeated serological examinations. Immunoelectrophoresis of blood and urine revealed increased IgG-lambda paraprotein, but no free light chains were found. We reviewed 54 cases reported in the literature, which showed organized crystalline structures on ultrastructural examination, but were unassociated with amyloidosis, SLE, cryoglobulinemia or multiple myeloma. The present patient is the first reported to have exhibited a combination of glomerulonephritis with organized deposits, monoclonal IgG lambda paraproteinemia, and the presence of anti-DNA antibody.
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PMID:Microlamellar structures in lobular glomerulonephritis associated with monoclonal IgG lambda paraproteinemia. A case report and review of the literature. 212 87


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