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Biomedical subjects

M Pras

Publications and source records attributed to M Pras.

At least 145 records · Page 8Linked to original sources
PubMed1985

The prevention of amyloidosis in familial Mediterranean fever with colchicine.

Colchicine has been used since 1972 to prevent the acute attacks of familial Mediterranean fever. The present study shows that colchicine is also effective in the prevention of amyloidosis. If initiated in patients without evidence of renal disease there is no appearance of proteinuria and no progression to renal insufficiency over long follow-up periods. Moreover, it ameliorates the course of the disease in patients with amyloid nephropathy and normal renal function. It does not alter the course of the disease if initiated after renal function is even mildly impaired. These findings suggest that colchicine prevents the new deposition of amyloid.

Adult↗
PubMed1984

Degradation of amyloid A and serum amyloid A by red blood cell haemolysate in patients with familial mediterranean fever.

Enzymatic activity for the degradation of serum amyloid A (SAA) and amyloid A (AA) was detected in erythrolysates of normal subjects and patients with familial mediterranean fever. A significant difference between the activity of normal subjects and patients was not found. Serum inhibited the SAA (but not the AA) haemolysate proteolytic activity. Interindividual variation in the susceptibility of SAA to degradation by RBC haemolysates was shown. The original digestible fraction of SAA became gradually resistant to proteolytic cleavage over a 9 month period while the susceptibility of AA to degradation remained unchanged in this time period. These findings suggest that enzymatic degradation of SAA depends on the source of SAA, as well as inhibitory activity in serum.

Amyloid↗
PubMed1983

Characterization of amyloid deposits and P component from a patient with factor X deficiency reveals proteins derived from a lambda VI light chain.

Amyloid fibrils were isolated from a spleen obtained at surgery from a 58-year-old white man with primary amyloidosis presenting with factor X deficiency and responding dramatically to splenectomy. Gel filtration on Ultragel ACA 54 in 5 M guanidine 1 M acetic acid yielded components with molecular weights between 17,000 and 13,000. Two of them (17K and 15K) were studied in detail. Antigenic and amino acid sequence analysis showed that these proteins were related to lambda VI immunoglobulin light chain. The predominant protein subunits of the amyloid fibril of the deposits (17K) was processed at the carboxy terminus in the same section of the constant region as the only other lambda VI amyloid protein previously reported. Amino terminal sequence of the 15K protein revealed not only degradation at the C terminal, but also minor degradation at the amino terminal (three residues difference from the 17K species). P component was also isolated from the spleen and characterized. This represents the first antigenic and sequence analysis of tissue amyloid proteins and P component from a patient presenting with factor X deficiency and another example of amyloid proteins derived from the newly discovered amyloidogenic lambda VI light chain subgroup.

Amino Acids↗
PubMed1983

Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin.

The complete amino acid sequence of three related amyloid proteins (Mr 14,000, 10,000, and 5,000) derived from tissues of a Jewish patient who suffered from a variant of familial polyneuropathic amyloidosis was determined. The protein, which contains 127 residues, is identical to a human serum prealbumin subunit. Only one amino acid substitution, glycine for threonine, was detected at position 49, where enzymatic cleavage occurred, yielding Mr 5,000 and 10,000 fragments which represent the amino terminus (residues 1-48) and carboxyl terminus (residues 49-127) of the molecule, respectively. Thus, a prealbumin variant and its fragments constitute the amyloid fibrils in a heredofamilial amyloidosis syndrome of dominant inheritance.

Amino Acid Sequence↗
PubMed1983

The immune system in familial Mediterranean fever.

Familial Mediterranean fever (FMF) is a genetic disorder with an obscure aetiology. In attempts to investigate a possible immunoregulatory imbalance involved in this disease we tested 24 FMF patients for suppressor T cell activity and for chemotaxis of mononuclear cells. The suppressor T cell activity and chemotaxis were decreased in untreated FMF patients as compared to colchicine treated patients or normal controls. Amyloid FMF patients manifested significantly increased chemotactic activity, while the suppressor T cell activity was normal. This finding may extend our knowledge concerning the immune mechanism involved in FMF.

Adolescent↗
PubMed1982

Amyloidosis associated with renal cell carcinoma of the AA type.

Amyloid fibrils were found at postmortem examination in a 70 year old woman with generalized amyloidosis associated with renal carcinoma (hypernephroma). Clinically, her amyloid disease presented as nephrotic syndrome. It was demonstrated by electrophoretic and amino acid sequence analysis studies that the amyloid fibrils contained AA protein identical to that found in amyloidosis associated with chronic inflammatory and infectious diseases as well as in the genetic form of familial Mediterranean fever.

Adenocarcinoma↗
PubMed1982

Demonstration of AA-protein in formalin-fixed, paraffin-embedded tissues.

AA-protein was identified by SDS-acrylamide electrophoresis in amyloid fibrils fixed in formalin after isolation from fresh-frozen tissues obtained from patients with familial Mediterranean fever (FMF) amyloidosis and idiopathic AA-amyloidosis and, following deparaffination, rehydration and homogenization of embedded formalin-fixed tissues of old autopsy cases of the hereditary amyloidosis of FMF and amyloidosis acquired in association with tuberculosis, bronchiectasis, and rheumatoid arthritis. That AA-protein is unaltered by formalin was firmly established by agar gel diffusion using specific rabbit anti-AA serum. By contrast, AL proteins could not be demonstrated either in formalin-fixed amyloid fibrils derived from fresh-frozen tissues of a patient with presumably AL-amyloidosis dominated by cardiomegaly and one with AL-kappa amyloidosis or in blocks of cases of familial neuropathic amyloidosis, multiple myeloma, and idiopathic amyloidosis with cardiopathy. AA-protein is not denatured by formalin and retains its typical electrophoretic, chromatographic, and immunologic characteristics even 30 years after fixation and paraffin-embedding.

Amyloid↗
PubMed1982

Idiopathic AL-kiv amyloidosis presenting as giant hepatomegaly.

The 11/2-yr course of idiopathic systemic amyloidosis in a 63-yr-old woman was characterized by inanition, subcutaneous ecchymoses and giant hepatomegaly, the liver weighing 8.5 kg at autopsy. Skeletal survey and bone marrow aspirate were normal. The major components of isolated amyloid fibrils were 16,000- and 23,000-dalton proteins. The 16,000-dalton component was shown by amino acid sequencing to be a fragment of the kappa (k)iv light chain, the first such case. These clinicochemical correlations suggest that isolated massive hepatomegaly may prove to be a hallmark of idiopathic amyloid light chain-related protein k amyloidosis.

Adult↗
PubMed1982

Serum amyloid A (SAA) in viral infection: rubella, measles and subacute sclerosing panencephalitis (SSPE).

Serum amyloid A (SAA) levels were determined in the serial serum samples of eight rubella, 10 measles and seven subacute sclerosing panencephalitis (SSPE) patients. An early rise in SAA levels was detected in the acute phase in rubella and measles, followed by a prompt decrease in the convalescent phase. In a number of measles and rubella patients from whom early serum samples were available, the rise of SAA levels could be demonstrated before specific viral antibodies could be detected by complement fixation (CF) (measles) and haemagglutination inhibition (HI) (rubella). In only one rubella and one measles patient was no rise of SAA level detected. In SSPE only a moderate increase in SAA levels was noted except in one patient during a temporary deterioration, at which time the SAA level was very high; it returned to close to normal shortly thereafter. The possibility that SAA levels might be of value in monitoring the severity of infections, the recovery process and effects of anti-viral agents is discussed.

Adult↗
PubMed1981

A variant of prealbumin from amyloid fibrils in familial polyneuropathy of Jewish origin.

Amyloid fibrils were isolated from spleen and thyroid obtained at autopsy from one patient (S.K.O.) of Jewish origin with familial amyloidotic polyneuropathy. Gel filtration on Sephadex G100 after solubilization in 5 M guanidine HCl yielded three major components with 14,000, 9,000, and 5,000 mol wt, respectively. The two larger components shared antigenic determinants with human prealbumin. Amino acid analysis and amino terminal sequence studies revealed the 14,000-mol wt protein to be an intact prealbumin subunit. The 9,000-mol wt fragment obtained in highest yield encompassed the region from position 49-127 and the 5,000 mol wt fraction encompassed the amino terminal of prealbumin (position 1-48). An amino acid substitution (Gly/Thr) was detected at position 49, where enzymatic cleavage occurred. Thus, several prealbumin-derived fragments, predominantly the carboxyl end, constitute the amyloid fibrils in a heredofamilial amyloidosis syndrome of dominant inheritance.

Adult↗
PubMed1981

[Periodic arthralgia: teratogenicity of colchicine and its influence on pregnancy and sterility (author's transl)].

Pregnancy appears to exert a beneficial effect on periodic arthralgia, the frequency of episodes being reduced by a half. Sterility, probably of anavulatory rather than mechanical origin, occurs in one third of cases. Its frequency could be diminished by colchicine, which by its anti-inflammatory action can prevent the development of mechanical sequelae. Though colchicine appears to lack teratogenetic activity, it should be discontinued three months before pregnancy.

Adolescent↗
PubMed1980

AA protein in a case of "primary" or "idiopathic" amyloidosis.

Amyloidosis constitutes a group of diseases in which extracellular fibrils with a characteristic appearance are deposited in a variety of tissues. Several different proteins have been identified as the major subunits of the fibrils. In the primary and myeloma-associated type, the amyloid fibrils consist of immunoglobulin light chain fragments, whereas in the secondary type and the amyloid associated with familial Mediterranean fever the major component is the AA protein. In this report a 21 year old man of Yemenite extraction with no underlying disease and no family history of amyloidosis was found to have amyloid deposits composed of AA protein. Although clinically this might be classified as primary amyloidosis, the absence of light chain fragments makes that diagnosis unlikely. Therefore, it is suggested that whenever possible the clinical classification be supplemented by a description of the biochemical nature of the fibrils.

Adult↗
PubMed1980

An adult form of juvenile rheumatoid arthritis.

The conditions of five adults were eventually diagnosed as juvenile rheumatoid arthritis (Still's disease). Prolonged hospitalization, repetitive roentogenographic examinations, biopsies, laparotomies, and therapeutic trials with toxic agents preceded the establishment of the final diagnosis. Common early findings in all cases were prolonged "septic fever," polyarthralgia, and an elevated ESR. Three patients had a rash, four had splenomegaly, three had a vague history of a similar disease, and four had leukocytosis. Some of the patients were older than others described in the literature. Two received immunosuppressive agents and did relatively well. In view of our experience and the few reports in the literature, we concluded that juvenile rheumatoid arthritis in adults has to be seriously considered in the presence of prolonged septic fever, polyarthralgia, rash, and splenomegaly, before harmful drugs are given or risky procedures are performed.

Adult↗