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Renal amyloidosis. Histological differentiation based on chemical types compared to Reimann's classification.

13 cases of renal amyloidosis were reclassified on the basis of the chemical types of the major amyloid fibril proteins. The classification (primary, secondary) depending on the absence or presence of a coexisting disease was found not to correlate with the classification based on the chemical types (AL, AA). It is concluded that in association with a disease capable of inducing amyloidosis amyloid of type AA does not necessarily appear. The deposited amyloid may be of AL type. No difference of decisive importance between the AL and the AA type was observed concerning the tissue distribution of the amyloid within the kidney. With respect to the cause of death, however, a significant difference was found between the chemical types. In amyloidosis of AA type, the cause of death was always renal insufficiency, whereas in the cases of AL type cardiac or hepatic insufficiency led to death. Differentiation of the types of amyloid proteins has gained practical importance, as it offers the possibility of selective therapeutic approaches. Their routine differentiation is possible with the potassium permanganate method.

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Characterization of an amyloid fibril protein from localized amyloidosis of the skin as lambda immunoglobulin light chains of variable subgroup I (A lambda I).

Amyloid fibrils obtained from a case (Hud) of localized, tumorous amyloidosis of the skin were investigated by immunological and biochemical methods including amino acid sequence studies. Evidence was obtained that a lambda immunoglobulin light chain protein, A lambda I, and differently sized N terminal fragments (mol. wt 14,000 and 10,000) of the same protein comprised a major component of the fibrils. The chemical nature of this protein suggested that this case of cutaneous amyloidosis belonged to the idiopathic form of amyloidosis, probably as a special type of systemic, idiopathic amyloid disease.

Amino Acid Sequence↗

Nonobstructive gastroparesis in amyloidosis improved with metoclopramide.

Patients with systemic amyloidosis often have symptoms related to impaired gastrointestinal motility. Delayed gastric emptying may result from autonomic nerve and/or smooth-muscle infiltration with amyloid. In two patients with gastroparesis secondary to amyloidosis, metoclopramide hydrochloride therapy quantitatively enhanced gastric emptying. We suggest that metoclopramide treatment may be useful in the supportive therapy of patients with delayed gastric emptying due to amyloidosis.

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Exclusively vascular systemic amyloidosis with visceral ischemia.

A patient with multiple myeloma had systemic amyloidosis exclusively confined to the vascular system. These vascular deposits had the typical tinctorial and ultrastructural characteristics of amyloid. At first, the patient clinically had ischemic heart disease, and at postmortem examination was seen to have had acute and chronic ischemic injury of the heart and kidneys due to vascular narrowing by massive amyloid deposits. Exclusively vascular systemic amyloidosis represents a morphologically and clinically distinctive, but uncommon, variant of amyloidosis.

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[Macrophage migration inhibition test in mice with experimental amyloidosis].

The migration inhibition factor (MIF) has been detected in sera of both amyloid patients and mice with casein-induced amyloidosis. This factor inhibits the migration of intact mouse splenocytes and peritoneal macrophages of the guinea pig. The same activity is also displayed by sera of guinea pig. The same activity is also displayed by sera of patients with chronic active hepatitis, liver cirrhosis and systemic lupus erythematosus. Spontaneous migration of splenocytes was studied in the course of casein-induced amyloidosis in mice. In the early stages of antigenic stimulation there was an increase in the cell migration activity, corresponding with the morphological picture of pyroninophilic and plasma cell proliferation. In the course of further antigenic stimulation the migration activity gradually decreases as the lymphoid tissue gets replaced by amyloid mass. MIF production during amyloidosis is discussed.

Amyloidosis↗

[Amyloidosis. I. Recent findings concerning amyloid substance].

The considerable progress made recently in the study of amyloid substance have led to the identification of numerous organised protein components in typical microfibrillar structures. In spite of the biochemical heterogeneity of fibril proteins, it is still possible to find similar chemicophysical and tintorial features in the various types of amyloid, probably due, at least in part, to the common Beta type molecular configuration, a structure proper to fibril proteins. In so-called primary amyloidosis and in that associated with myelomatous diseases, the principal protein component consists of AL protein, correlated with the light immunoglobulin chains, with which analogies have been observed both in the amino acid sequence and in antigenic characteristics. In secondary amyloidosis, AA protein, which is unrelated to immunoglobulins or other known human proteins, is prevalent. AA protein probably derives from a serum globulin, SAA, whose blood levels increase during numerous pathological processes, particularly in those of neoplastic or inflammatory type. The origin of serum protein, which might be either a normal tissue component released under stimulus or a reagent of the acute phase synthesised ex novo, and its function, which is probably of immunomodulator or more specifically immunosuppressive type, are still to be defined. In all forms of amyloidosis studied, a common observation is the presence of AP protein, organised in pentagonal structures. This protein would appear to derive from a serum component defined as SAP, with a marked affinity for amyloid fibrils. Also identifiable are other forms of amyloid such as APUD-amyloid, which probably derives from polypeptide hormones, and AS amyloid, which is present in some organs of elderly patients and is biochemically identifiable at cardiac level with A(SCA) protein. Still awaiting definition in amyloid tumours or amyloidomas is the precise chemical composition of deposited proteins.

Amyloid↗

Radiation therapy in amyloidosis of the eyelid and conjunctiva: a case report.

Many questions about amyloidosis are still unanswered. Etiology and pathogenesis remain unclear. Diagnosis is difficult to prove without a biopsy. Several approaches have been tried, but no effective cure has been documented. Russian authors report the use of cobalt therapy for a patient with local laryngeal amyloidosis. This paper presents a case report of a patient with local amyloidosis of the conjunctiva. Superficial radiation therapy was used, and resulted in some shrinkage of the lesions. Surgical excision was later utilized to remove the remaining amyloid deposits.

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[(Intrahepatic cholestasis with jaundice due to amyloidosis of the liver) ].

Two cases of severe intrahepatic cholestasis due to amyloidosis of the liver seen within 9 months are described and compared with the pertinent literature. In both, the diagnosis was established by needle biopsy of the liver, and the amyloidosis associated with a myeloma. The methods available for reaching a definite diagnosis are discussed, and the possible diagnostic importance of percutaneous transhepatic cholangiography, as performed in one of the two patients, is stressed. Amyloidosis of the liver complicated by jaundice is possibly not such a rare disease; it has a very poor prognosis, and the patients do not survive more than a few months.

Adult↗

Secondary amyloidosis complicating rheumatoid arthritis; report of a case in an eight-year-old girl.

Secondary amyloidosis can complicate any long-standing suppurative infection, such as tuberculosis, osteomyelitis and disorders of connective tissue, i.e., the so-called "collagen diseases". Rheumatoid arthritis is known to be a notable precursor of amyloidosis. The fact that a long-standing process is often necessary to produce the changes in the ground substance, makes Juvenile Rheumatoid Arthritis (J R A) an interesting challenge to that hypothesis. The decreasing incidence of secondary amyloidosis, complicating rheumatoid arthritis, is attributed to better management of patients and the use of more effective anti-inflammatory therapy.

Amyloidosis↗

[Amyloidosis of the intestinal tract (author's transl)].

Amyloidosis may afflict different organs of the body and thus cause a variety of clinical symptoms. Amyloidosis of the gastro-intestinal tract can mimic several gastric and intestinal disorders, as for instance disturbances of motility, vascular processes and tumors. The amyloid infiltrates the tissue affected, replaces it and thus cause insufficient organ function. The disease usually progresses slowly, in some cases however, acutely life threatening situations may occur. Biopsy of the rectal mucosa will allow to establish the diagnosis; generalized amyloidosis was present in about 80% of the cases analysed. A medical management has to be done.

Amyloidosis↗

[Reproduction of amyloidosis in mice by contact sensitization with dinitrochlorobenzene].

Induction of murine amyloidosis by contact sensitization with hapten--dinitrochlorobenzene is described. Three to five applications of 15--25% dinitrochlorobenzene solution in acetone during two weeks are necessary for this. Within 3 weeks after the 1st application amyloidosis develops involving consecutively the spleen, liver, kidney and heart. Such consequence of the organ involvement and tinctorial pecularities are typical of murine amyloidosis.

Amyloidosis↗

[Whipple's disease--a rare cause of secondary amyloidosis].

Two cases of Whipple's disease with secondary amyloidosis are described. One patient had a nephrotic syndrome, the other malabsorption. The chronic inflammatory stimulus of Whipple's disease is discussed as a trigger for the development of secondary amyloidosis. The clinical symptoms of seronegative arthritis, weight loss, chronic diarrhea, intermittent fever and lymphadenopathy may be the clue to the diagnosis of Whipple's disease. Peroral intestinal biopsy is the diagnostic procedure of choice. Adequate antibiotic treatment with a regimen of penicillin and trimethoprim-sulfamethoxazole is indicated and prevents the development of secondary amyloidosis.

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[Methotrexate treatment of amyloidosis secondary to rheumatoid arthritis].

Amyloidosis secondary to rheumatoid arthritis is a complication with a poor prognosis and as yet an undefined medical therapy. In the last decades the use of different cytostatics has been advocated to avoid renal function deterioration. The clinical characteristics and course in eight patients with amyloidosis secondary to rheumatoid arthritis are here reported after therapy with low dosage methotrexate. In twelve patients who followed a 12-month therapy a clinical improvement was observed, with a marked decrease in proteinuria; in one of them proteinuria disappeared. These results suggest that methotrexate at low doses might be an alternative in the early treatment of amyloidosis secondary to rheumatoid arthritis in patients with preserved renal function.

Amyloidosis↗

[Amyloidosis of the gallbladder. An unusual localization].

We report a rare case of amyloidosis of the gallbladder in a 60-year-old man. This amyloidosis was associated with hepatic amyloidosis and pancreatic adenocarcinoma. To our knowledge, this is the second case reported in the literature and the first associated with neoplastic pathology.

Adenocarcinoma↗

[Behçet's disease and renal amyloidosis].

We report the case of an 29-year-old male Turkish patient suffering from generalized Behçet's disease. After an evolution of twelve years, he suddenly presented a nephrotic syndrome, a terminal renal insufficiency and thrombosis of the renal veins as well as the inferior vena cava. A percutaneous renal biopsy showed amyloidosis of the AA type, characteristic of secondary amyloidosis. Attempts to install an arterio venous shunt of the arm and to set up a peritoneal dialysis catheter were complicated by septic thrombosis. The patient died of renal failure. The association of renal amyloidosis and Behçet's disease is rare. It is, as far as we know, the first case reported in Switzerland.

Acute Kidney Injury↗

The SJL/J mouse: a new model for spontaneous age-associated amyloidosis. I. Morphologic and immunochemical aspects.

A high incidence of spontaneous amyloidosis is described in SJL/J mice. Amyloid was detected as early as 30 weeks of age and the incidence rose to 90 per cent by 60 weeks of age. Amyloid deposits were most prominent in the perifollicular zones of the spleen and the lobular areas of the liver. Ultrastructural analysis revealed rigid, nonbranching fibrils indistinguishable from those observed in casein-induced murine amyloidosis. On the other hand, immunochemical studies indicated that amyloid deposits in SJL/J mice differ from those found in casein-treated CBA mice with respect to size, amino acid content, and antigenic properties. Since the SJL/J mouse also develops spontaneous reticulum cell tumors and serum M components, it appears to be a useful model for study of the pathogenesis of amyloidosis and its relationship to aging, neoplasia, and certain B-cell dyscrasias.

Age Factors↗

[Localized amyloidosis in the area of the head-neck. A retrospective study].

Localized amyloidosis is a benign rare process in the head and neck. From 1972 to 1992, 12 patients with amyloid deposits of the head and neck were treated at the ENT Department of the University of Erlangen-Nürnberg. Negative congo red staining of rectal biopsy specimens established that the amyloidosis was not systemic. Localized amyloidosis appeared as a diffuse grey-to-yellow mass in the nose (n = 1) or larynx (n = 11). In 10 of the 12 cases excision of amyloid was possible with preservation of adjacent functional structures. Two patients refused surgery and underwent only symptomatic treatment with clinical followup investigations. Amyloid deposits completely excised did not recur during a mean postoperative period of 10 years. When not operated, the amyloid tumors showed a slowly progressive growth pattern.

Adolescent↗

[Localized amyloidosis of the ENT area].

Although amyloidosis is in general a systemic disorder, it may occur as an isolated lesion, especially in the head and neck. The actual classification of amyloidosis is dependent on the biochemical nature of its protein deposits. In the present report, the symptoms and diagnosis of localized amyloidosis are discussed with special regard to histological findings.

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