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Biomedical subjects

D A Fischman

Publications and source records attributed to D A Fischman.

101 records · Page 6Linked to original sources
PubMed1970

Membrane modifications in nutritionally induced filamentous Escherichia coli B.

Nutritionally induced filamentous cell forms of Escherichia coli B were examined for their morphological and biochemical lesions. The filamentous forms showed no significant alteration in total DNA concentration, RNA synthesis, ability to form beta-galactosidase in response to isopropylthiogalactoside, or insensitivity to actinomycin D as compared to the normal cell form. The filamentous cells showed a marked decrease in the ability to incorporate N-acetylglucosamine-UL-(14)C into a phenol-soluble glycoprotein fraction relative to the normal cell form or relative to strain E-26 of E. coli grown in the filament-inducing medium. The filaments yielded an envelope-specific phenol-soluble protein fraction markedly reduced in or lacking three proteins as determined by acrylamide gel electrophoresis. Amino acid analysis, and chemical and enzymatic treatments of the envelope-specific phenol-soluble proteins showed striking differences between the fractions obtained from normal and filamentous cells. Electron microscope studies of divalent cation-induced aggregates of the envelope proteins showed different aggregation patterns dependent upon the cell form yielding the protein fraction.

Amino Acids↗
PubMed1969

Formation of neuromuscular junctions in embryonic cell cultures.

The formation of nerve-muscle junctions in monolayer cultures of embryonic muscle and spinal cord cells is described. Muscle-forming cells (myoblasts) from leg muscles of 12-day chick embryos were separated with trypsin and cultured on a collagen substrate for two days. Suspensions of ventral spinal cord cells from six-day chick embryos were then plated over the differentiating muscle cells. The cultures were subsequently examined by electron microscopy and in silver-stained light microscopic preparations. After 10-12 days in culture, irregular thickenings were observed along the nerve cell processes in contact with the muscle fibers which by that time had undergone advanced differentiation (myogenesis). By electron microscopy it was demonstrated that many of the nerve-muscle contacts had the characteristics of a synapse. Some aspects of the fine structure of these junctions are described. The possibilities raised by these findings with respect to innervation mechanisms and specificities in nerve-muscle interactions are briefly discussed.

Animals↗
PubMed1967

Hexagonal pattern in cell walls of Escherichia coli B.

Cell walls, isolated from Escherichia coli B, as examined by electron microscopy and optical diffraction contain a hexagonal lattice structure, the (1,0) planes of which are separated by 140 +/- 8 angstroms. Unless the walls are briefly heated (10 minutes, 90 degrees C) early in the isolation, the hexagonal array cannot always be observed. Enzymatic digestion with pancreatin and amylase improves visualization of the lattice; subsequent treatment with pepsin and sodium dodecylsulfate removes the hexagonal pattern. Protein or lipoprotein globular units within the wall may thus be arranged in a hexagonal array uponthe mucopeptide layer.

Amylases↗
PubMed1967

An electron microscope study of myofibril formation in embryonic chick skeletal muscle.

The formation of myofibrils in the developing leg muscle of the 12-day chick embryo was studied by electron microscopy. Myofilaments of two varieties, thick (160-170 A in diameter) and thin (60-70 A in diameter), which have been designated myosin and actin filaments, respectively, on the basis of their similarity to natural and synthetic myosin and actin filaments, appear in the cytoplasm of developing muscle cells. There is a greater than 7:1 ratio of thin to thick filaments in these young myofibers. The free myofilaments become aligned in the long axis of the cells, predominantly in subsarcolemmal locations, and aggregate into hexagonally packed arrays of filaments. The presence of Z band material or M band cross-bridges do not appear to be essential for the formation or spacing of these aggregates of filaments. Formation of the Z band lattices occurs coincidentally with the back-to-back apposition of thin filaments. An hypothesis concerning myofibril growth, based on the self-assembly characteristics of the filaments, is presented.

Animals↗
PubMed1967

The fine structure of embryonic chick skeletal muscle cells differentiated in vitro.

Dissociated myoblasts from 12-day chick embryos were cultured in monolayer, and the differentiation of skeletal muscle cells was studied by electron microscopy. The results have revealed a striking ultrastructural similarity between the in vivo and the in vitro developing muscle, particularly with respect to the myofibrils and sarcoplasmic reticulum. This study demonstrates that all the characteristic organelles of mature skeletal muscle can develop in vitro in the absence of nerves.

Animals↗
PubMed1967

Nickel substitution for calcium in excitation-contraction coupling of skeletal muscle.

In 1962 Frank (22) reported that the addition of any one of a number of divalent cations, including Ni, to a Ca-free Ringer solution prevented the rapid loss of contractility seen in the absence of external Ca. To investigate further the Ni-Ca substitution, studies were made of (45)Ca and (63)Ni exchange during contraction and at rest using frog striated muscle. In contrast to (45)Ca, it was found that there is no increase of (63)Ni uptake associated with a K contracture of the sartorius muscle. The rates of loss of (63)Ni and (45)Ca from resting toe muscles previously bathed in the respective radioisotopes are not significantly different. Resting and action potentials, after 1 hr in a Ringer solution with Ni replacing Ca, closely resemble these potentials in normal Ca-Ringer's solution. Studies on the syneresis of isolated myofibrils indicate that Ni cannot replace Ca in activating this reaction. It is suggested that Ca is required for at least two steps in E-C coupling: one is the spread of excitation at the sarcolemma and transverse tubular system; the second is the activation of actomyosin ATPase. Conceivably Ni can substitute for Ca in the former but not in the latter.

Action Potentials↗
PubMed1967

Enzyme-induced formation of spheres from cells and envelopes of Escherichia coli.

Normal and filamentous whole cells and isolated envelopes of Escherichia coli B were exposed to various enzymatic treatments to remove surface layers and to characterize the component(s) conferring rigidity in this organism. Modification of cell rigidity was determined by sphere formation in both whole cells and isolated envelopes. Enzymes capable of converting trypsinized normal or untreated filamentous whole cells and untreated envelopes to spheres included: lysozyme plus ethylenediaminetetraacetic acid, clostridial phospholipase C, and phospholipase D from cabbage. These data suggest that there are at least two components essential for maintenance of cell rigidity in E. coli B. The first is the peptidoglycan (mucopeptide), which is susceptible to lysozyme. The second is a phospholipid which is either covalently linked to the mucopeptide or in close association with it. This phospholipase C-sensitive component is protected more completely in normal than in filamentous whole cells by a protein layer which is easily modified by trypsin treatment to allow enzymatically induced sphere formation to occur.

Cell Wall↗