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Biomedical subjects

B GOLDBERG

Publications and source records attributed to B GOLDBERG.

At least 37 records · Page 2Linked to original sources
PubMed1962

Postnatal psychological causes of mental retardation.

The psychological factors present in 715 suspected retarded children were studied. Social, cultural and educational deprivation accounted for 57 cases. Personality and emotional conflicts were primary etiological factors in 15 children. Functional childhood psychosis was found in 18. A group of 89 children had no obvious definitive cause for retardation, although epilepsy, mixed eye and hand dominance, visual perceptive disorders, or poor muscle tone was present in some. In the remaining 523 children, primary brain damage was evident. A sample of 142 of these brain-damaged children revealed that 38 had neurotic symptoms, 23 were antisocial, 11 were psychotic, 28 had restless, disturbed activity, and 42 had intellectual lowering only. The authors suggest that both psychological and organic factors must be taken into consideration in order that complete diagnostic and therapeutic effectiveness be achieved.

Antisocial Personality Disorder↗
PubMed1962

Immune cytolysis: electron microscopic localization of cellular antigens with ferritin-antibody conjugates.

Immune gamma globulin has been coupled to ferritin by the diisocyanate method of Singer. The final product ("ferroglobulin") had approximately 13 per cent of its gamma globulin coupled to ferritin, and roughly half of its ferritin coupled to gamma globulin. The uncoupled gamma globulin could be removed by ultracentrifugal sedimentation of the free ferritin and the ferritin-antibody conjugates. The characteristics of the native antibody were retained by the ferritin-antibody conjugates, for they could be precipitated by anti-gamma globulin antisera, and when used as antibodies, they reacted specifically with soluble and cellular antigens. Ferroglobulin preparations made from rabbit antisera against whole ascites tumor cells were incubated with the cells, and the location of ferritin determined by electron microscopy of thin-sectioned material. It was found that the immune ferroglobulins localized specifically on antigens of the cell membrane. Some of the ferritin label entered the cells by pinocytosis, but the ferritin-antibody units did not appear able to pass directly through the cell membrane into the cytoplasmic matrix. When cells were incubated with ferritin-labeled antibody and complement, antibody could be located in the cytoplasmic matrix, and it therefore appeared that complement action was required before antibody could pass directly through the cell membrane. This finding was consistent with previous observations that the plasma membrane of an antibody-complement treated cell becomes permeable to large molecules. In broken cell preparations incubated with ferroglobulin, antibody combined with amorphous material and with structures derived from cell membranes and from smooth membranes of the endoplasmic reticulum. The data favor the concept that antigens contained within the membranous structures are most important in the formation of cytotoxic antibodies. The reported experiments support the view that cytotoxic antibodies fix primarily to surface antigens of the cell membrane. The subsequent action of complement establishes the permeability defect that induces the osmotic lysis of the cell and permits antibody to pass into the cell where it may act in a similar fashion on intracellular organelles.

Animals↗
PubMed1960

Immune cytolysis. 1. The release of ribonucleoprotein particles. 2. Membrane-bounded structures arising during cell fragmentation.

It has been shown that Krebs ascites tumor cells incubated in vitro with immune gamma globulin and complement lose the bulk of their cytoplasmic RNA to the suspending medium, although the cell membrane remains visibly intact. The present experiments show that about four-fifths of the lost RNA is sedimented by centrifugation of the cell-free medium at 105,000 g. Electron microscopic and chemical analyses of the pellets show them to consist of 150 A ribonucleoprotein particles. It is concluded that most of the RNA passes from the cells in this form. Antibody-complement action causes osmotic swelling of the tumor cells and they become quite fragile. Fragmentation of such preparations yields large numbers of membrane-bounded spheres which may be separated from the heavier nuclei by differential centrifugation. Electron microscopic study of the spheres provides evidence that they can arise from segments of the cell surface as well as from mitochondria and the endoplasmic reticulum.

Animals↗
PubMed1959

Effect of antibody and complement on permeability control in ascites tumor cells and erythrocytes.

Rabbit antibody + complement alters the permeability properties of mouse Krebs ascites tumor cells and erythrocytes. When antibody + C' acts on ascites tumor cells in a low protein medium, intracellular K(+) is lost from the cells at a rate far greater than the normal leak rate. At the same time the cells lose amino acids and ribonucleotides and become fully permeable to the Na(+) of the medium. When antibody + C' acts in a low protein medium, the cells swell extensively and lose most of their macromolecules to the medium (hemoglobin from erythrocytes, protein and RNA from the ascites tumor cells). If the antibody + C' acts in a medium containing protein in sufficient concentration to balance the colloid osmotic pressure of the cells, the swelling is prevented; no macromolecules are then lost from the cells, but the loss of K(+) and entrance of Na(+) are not altered, and the loss of amino acids and ribonucleotides is only slightly affected. It therefore appears that the action of antibody + C' is to produce functional "holes" in the animal cell membrane which permit the equilibration of cations and small molecules between cell and medium. This leads to an increase in the osmotic pressure of the cell and a rapid influx of water. The cell membrane and its "holes" are thereby stretched, permitting macromolecules to escape from the cell.

Animals↗
PubMed1959

The cytotoxic action of immune gamma globulin and complement on Krebs ascites tumor cells. I. Ultrastructural studies.

Electron microscopic studies of Krebs ascites tumor cells treated in vitro with rabbit immune gamma globulin revealed a distinctive alteration in the structure of the cellular surface membrane. The subsequent addition of complement to this system severely damaged the cytoplasmic matrix, mitochondria, and endoplasmic reticulum. This sequence of events provides a structural basis for the cytotoxic action of antibody and complement.

Agammaglobulinemia↗
PubMed1959

The cytotoxic action of immune gamma globulin and complement on Krebs ascites tumor cells. II. Chemical studies.

The in vitro exposure of Krebs ascites tumor cells to the action of rabbit immune gamma globulin alone does not result in any changes in the cell concentration of amino acids, ribonucleotides, RNA, DNA, or protein, nor in the rate of entry of potassium into the cell. The exposure of the cells to antibody + complement results in the following changes within a few minutes:- (a) Loss of about two-thirds of the free amino acids and ribonucleotides. (b) Loss of about 90 per cent of the intracellular potassium. (c) Loss of about three-quarters of the cell RNA to the medium, part appearing as TCA-soluble and the rest as TCA-insoluble products. There were no changes detectable in DNA. (d) A small increase in total free amino acid of the cell suspension. (e) Loss of from 30 to 60 per cent of the cell protein. The loss of these substances is believed to occur through a cell membrane which is still intact, as judged by phase and electron microscopy, and still able to discriminate to a small degree against passage of larger molecules.

Agammaglobulinemia↗