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Biomedical subjects

M A Scheinberg

Publications and source records attributed to M A Scheinberg.

At least 55 records · Page 3Linked to original sources
PubMed1979

Subsets of T lymphocytes and lymphocyte cooperation. Modulation of the immunocellular response.

Recent advances in the characterization of T cell subsets suggests that the various subsets of T cells described in mice also occur in man. These various subsets of T cells can be detected by the use of appropriated antisera, co-cultivation of purified lymphoid cell preparations and differential sensitivity to radiation. Clinical applications from these new observations are now underway and it is hopeful that they should help to achieve a better understanding of the mechanisms responsible for autoimmunity, neoplasias and the various primary and secondary immunologic deficiencies.

Animals↗
PubMed1979

Serum amyloid protein SAA, C-reactive protein and lysozyme in leprosy.

Serum amyloid protein (SAA) appears to be the precursor of amyloid protein AA, the non-immunoglobulin fibril protein of secondary amyloidosis. Since amyloidosis is known to occur in high frequency associated with lepromatous leprosy (LL), we have examined the SAA levels in untreated LL patients and compared them to the levels observed in patients with tuberculoid leprosy (TT) and a large number observed in healthy controls. We found that SAA is markedly elevated in LL when compared to TT and controls. No clear correlation could be established with C-reactive protein, a well-documented acute phase reactant, or serum lysozyme levels that reflect the presence of monocyte activity. This study showed that SAA levels in leprosy do not appear to be a reflection of inflammatory activity or monocyte turnover. Whether amyloidosis will be more prevalent in patients who have higher SAA levels remains to be determined.

Amyloid↗
PubMed1978

Monocyte function in patients with solid neoplasms during immunotherapy with Corynebacterium parvum.

The present studies were performed in order to evaluate monocyte function in patients with solid neoplasms before and after administration of C. parvum. The results demonstrate that monocytes from cancer patients display increased numbers of C3 and Fc receptor sites after administration of C. parvum. It is concluded that characterization of monocyte receptor activity may be helpful in monitoring the effects of immunotherapy in the immune system.

Chemotaxis, Leukocyte↗
PubMed1978

Decreased lymphocyte response to PHA, Con-A, and calcium ionophore (A23187) in patients with RA and SLE, and reversal with levamisole in rheumatoid arthritis.

The mechanism of poor lymphocyte transformation to mitogens was studied in selected patients with rheumatoid arthritis and systemic lupus erythematosus. Low lymphocyte response to PHA and Con-A in media containing autologous and homologous sera was usually associated with poor response to the calcium ionophore A23187, which induces blastogenesis by a different mechanism. The low lymphocyte response to mitogens in patients with rheumatoid arthritis could be restored by in vivo treatment with the anthelmintic drug, levamisole. The present findings suggest that intrinsic defects are responsible for the decreased cellular response in patients with rheumatoid arthritis and systemic lupus erythematosus.

Adolescent↗
PubMed1978

Suppression of C3 rosette formation by serum from patients with systemic lupus erythematosus. A corollary of disease activity.

Many sera from patients with systemic lupus erythematosus (SLE) inhibit C3 rosette formation of normal human lymphocytes. Fractionation of SLE sera by Sephadex G-200 gel chromatography showed that the inhibition was present in low molecular weight serum fractions. A correlation was noted between inhibition of C3 rosette formation and disease activity. Inhibition of C3 rosette formation may be helpful and simple way to monitor clinical activity and complement activation in patients with SLE.

Adult↗
PubMed1978

New concepts in the pathogenesis of primary and secondary amyloid disease.

Despite the marked progress obtained in the structural and amino acid sequencing data of amyloid proteins our understanding of the cellular mechanisms causing the deposition of amyloid fibrils is still poor. Some of the questions about the cellular events leading to the synthesis of amyloid fibrils can be approached by evaluating the immune reactivity of animals that develop amyloid after repeated daily casein injections. Recent studies carried out in a mouse model indicate that macrophage activation associated with T-cell suppression and followed by B-cell proliferation appear to be responsible for the immunopathological abnormalities in both primary and secondary amyloid disease.

Amyloidosis↗
PubMed1977

Kinetics of serum amyloid protein A in casein-induced murine amyloidosis.

Serum amyloid protein A (SAA), the precursor of secondary amyloid protein, is elevated in chronic diseases which are associated with an increased incidence of amyloid. However, SAA is also elevated in acute bacterial and viral infections and somes forms of cancer. The murine model of casein-induced amyloidosis was studied to determine the relationship between SAA production and amyloid deposition. SAA levels measured by radioimmunoassay were found to be as high as 200 times the normal level in CBA/J mice receiving daily parenteral casein. After a single injection of casein the SAA level was elevated by 3h and peaked by 12-18 h. Similar levels were found in casein-treated A/J mice, a strain less susceptible to the induction of amyloid. Parenterally administered bovine serum albumin, which has low potential for amyloid induction, gave SAA levels in CBA/J and A/J mice comparable to casein treatment. These data show that, while SAA levels are elevated during chronic antigenic stimulation, there are other factors involved in amyloid formation. These factors may include alterations in the degradation of SAA by the reticuloendothelial system caused by substances such as casein. Nude (athymic) mice were shown to attain high levels of SAA after receiving casein parenterally. Therefore, thymus-derived lymphocytes are not necessary for the synthesis of SAA.

Amyloid↗