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Biomedical subjects

D Schünke

Publications and source records attributed to D Schünke.

4 recordsLinked to original sources
PubMed1983

Cytochemical demonstration of negative surface charges in central myelin.

Homogenates of central myelin were treated with ferritin derivatives having different isoelectric points. It was found that considerable amounts of cationic ferritin (pI 8.5-9.5) had access to the extracellular space, but that anionic ferritin (pI 4.0) and native ferritin (pI 4.5) did not. The electrostatic nature of the binding of cationic ferritin was demonstrated by treating the homogenates with poly-L-lysine and 1 M NaCl:both reagents led to a complete displacement of the bound cationic ferritin. Neither extensive trypsination nor neuraminidase treatment showed a significant effect on the intralamellar distribution of the bound cationic ferritin molecules. This suggests that the net negative charge on the extracellular myelin face stems primarily from acidic lipid groups in the membrane.

Animals↗
PubMed1980

Interlamellar tight junctions of central myelin. II. A freeze fracture and cytochemical study on their arrangement and composition.

The interlamellar tight junctions (ITJ) of central myelin (white matter from the parietal lobe and the medulla oblongata of the rat) were analyzed electron microscopically, making use of a wide range of different preparatory techniques. Freeze-fracture observations indicate that the ITJ are composed of rows of particulate subunits in glutaraldehyde-fixed or formaldehyde-fixed material, and in the unfixed state. The particulate subunits of the ITJ are preferentially associated with the protoplasmic (P) face in the aldehyde-fixed state, and no shift in the binding characteristics of the particles was observed after omission of aldehyde fixation. Tracer studies in conjunction with the dissociated appearance of the junctional globules suggest that the ITJ represent a leaky type of zonula occludens. It is assumed that the ITJ particles represent an "integral-type protein" that preferentially serves as a mechanical device maintaining the structural integrity of the central myelin sheath. By means of cytochemical experiments, the proteinaceous character of the ITJ subunits is established. An attempt is made, based on results from lipid extraction and protein digestion, to define certain cytochemical parameters of the ITJ proteins and to compare them with the current collection of chemically identified proteins of central myelin.

Animals↗
PubMed1978

The oligodendrocytic junctional complex.

The junctional complex of oligodendrocytes was studied by means of different electron microscopical techniques. This complex is composed of the following junctional membrane formations: 1) tight junctional domains in the oligodendrocytic membrane near the some of the cells, 2) fasciae occludentes or focal tight junctions on the outer oligodendrocytic loop of myelin and on the outermost myelin membrane, 3) gap junctions of considerable size variations, either on membranes near the soma or on peripheral oligodendrocytic processes, and 4) non-paranodal transverse bands. The different types of oligodendrocytic junctions are discussed in terms of their functional implications.

Animals↗