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Biomedical subjects

B G Fishkin

Publications and source records attributed to B G Fishkin.

9 recordsLinked to original sources
PubMed1987

Toward meaningful blood usage review: comprehensive monitoring of physician practice.

During a one-year period, all blood transfusions at an acute care Veterans Administration hospital were concurrently reviewed. Inappropriate transfusion episodes represented less than 2% of the total according to clinical criteria established for purposes of screening cases. The percentage of episodes reviewed that did not meet the screening criteria decreased progressively (3.6% to 0.3%) during the study period. Episodes in which red blood cells (RBC) or fresh frozen plasma (FFP) alone and RBC and FFP together were transfused comprised almost all of the cases that were unjustified by peer review. The findings indicated that, although comprehensive review may document the overall appropriateness of clinical transfusion practice, more detailed profiling of clinical circumstances of each episode is necessary to provide convincing arguments for major revisions in hemotherapy practice.

Blood Transfusion↗
PubMed1979

Lymphoplasmacytic myeloma: an immunological, immunohistochemical and electron microscopic study.

An unusual case of a light chain plasma cell myeloma is described. The disease was initially characterized by a diffuse lymphoplasmacytic bone marrow involvement, but subsequently developed widespread extramedullary metastases with anaplastic tumors in the skin which histologically resembled a "histiocytic lymphoma." Electron microscopic examination, in vitro protein synthesis of bone marrow lymphoidal cells, chemical and immunochemical studies of serum and urine proteins, and intracellular immunoglobulin study by the immunoperoxidase technique on the skin biopsy and postmortem tumor tissue demonstrated evidence for lambda light chain synthesis and secretion. These findings provide further support to the notion that the wide spectrum of diverse morphologic patterns seen in lymphoplasmacytic disorders originates from the same progenitor B-lymphoid cell. Distinguishing anaplastic variant of plasma cell myeloma from other undifferentiated neoplasms offers a challenge.

Bone Marrow↗
PubMed1976

Cervical lymph node metastasis as the first manifestation of localized extramedullary plasmacytoma.

Two patients who had cervical lymph node metastases as the first symptom of a localized soft tissue extramedullary plasmacytoma of the epiglottis and nasopharynx, respectively, are described. Classical multiple myeloma was excluded by bone marrow biopsies and x-ray studies of the skeleton. In both patients, the primary tumor was diagnosed 2 years after excision of the cervical lymph node. One patient had a IgD, lambda myeloma protein in the serum and excreted lambda Bence-Jones protein into the urine. No M-component was found in the other patient. Both are living with a long survival of 8 and 4 years respectively. The presence of a cervical lymph node plasmacytoma should suggest an upper respiratory tract or oropharynx plasmacytoma rather than a primary lymph node plasmacytoma.

Aged↗
PubMed1976

Human myeloma IgA half-molecules.

A lambda, IgAl myeloma protein that formed two chain half-molecules was obtained from a patient who had typical multiple myeloma. His serum contained 1.3 g/100 ml of an IgA paraprotein of gamma-1 electrophoretic mobility, his urine predominantly lambda Bence Jones protein, and only small amounts of IgA paraprotein. Analytical ultracentrifugation of the isolated serum IgA protein showed 7.0S and 4.5S protein peaks but no IgA polymers. When the 7.0S and 4.5S protein peaks were tested with an antiserum specific for alpha chain, both fractions were antigenically deficient compared to control IgA myeloma proteins but showed a line of identity to their F(ab')2 fragments. The serum and 7.0S protein fraction showed double precipitin lines in IgA radial immunodiffusion plates and in immunoelectrophoretic analysis, one line being formed by the myeloma protein and the other by residual normal IgA. The myeloma protein did not form a precipitin line with antisera specific for the IgA Fc fragment. Sodium dodecylsulfate-urea-polyacrylamide gel electrophoresis demonstrated that both the 7.0S and 4.5S fractions of the myeloma protein consisted of covalently linked heavy and light chains, 4.5S fraction being apparently the half-molecule of the 7.0S protein. The heavy chain had a mol wt of 46,500 daltons compared to 55,000 daltons for normal alpha chains. Reduction and alkylation in aqueous solutions resulted in dissociation of the 7.0S myeloma protein fractions into smaller units, probably half-molecules, suggesting that the noncovalent interactions between the alpha chains were substantially weakened or absent, presumably as a result of a deletion in the Fc portion of the alpha chain. The catabolic rates of the radio-labeled 7.0S and 4.5S protein in rhesus monkeys were similar to those of control IgA myeloma proteins; the excretion of protein-bound radioactivity of the IgA half-molecules into the urine was no greater than that of the 7.0S or of control IgA myeloma proteins. It is suggested that the myeloma IgA half-molecule is probably derived from an IgAl mutant that is carried in the human genome and that it is unlikely a representative of a rare IgA subclass or an IgA l allotypic variant.

Chromatography, Gel↗
PubMed1968

Catabolism of human gammaG-immunoglobulins of different heavy chain subclasses. I. Catabolism of gammaG-myeloma proteins in man.

The rates of catabolism of human gammaG-immunoglobulins of subclasses gammaG(1), gammaG(2), gammaG(3), and gammaG(4) were studied by determining the rates of elimination from the circulation of pairs of (131)I-and (125)I-labeled gammaG-myeloma proteins in 57 patients suffering from cancer other than multiple myeloma. On the average, gammaG(1)-, gammaG(2)-, and gammaG(4)-myeloma proteins were catabolized at a rate similar to that of normal gammaG-immunoglobulin, whereas gammaG(3)-myeloma proteins were catabolized more rapidly than normal gammaG-immunoglobulin. The average half-lives for the myeloma proteins were 12.3 days for normal gammaG, 11.6 days for gammaG(1), 12.4 days for gammaG(2), 8.2 days for gammaG(3), and 11.3 days for gammaG(4). However, significant differences in catabolic rates were observed when individual myeloma proteins of a single subclass were compared. These individual variations were present within all four heavy chain subclasses. The extent of differences ranged from 10 to 47%. The catabolic rate of normal gammaG was in an intermediate range when compared with myeloma proteins of relatively long and short half-lives. The rate of catabolism of an individual myeloma protein did not correlate with its light chain type, Gm factor, carbohydrate content, or electrophoretic mobility. These findings indicate that the structure(s) related to the catabolism of gammaG-immunoglobulins are complex and differ from one immunoglobulin molecule to another.

Animals↗