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L Tóth

Publications and source records attributed to L Tóth.

At least 127 records · Page 7Linked to original sources
PubMed1978

[Morphological base of Renshaw inhibition studied by light and electron microscopic histochemistry. Topograhic analysis of AChE-positive Renshaw elements].

Light- and electron microscopic structure of Renshaw elements--morphologic representatives of the recurrent spinal inhibition--was investigated by histochemical localization of AChE. Renshaw elements are spindle-shaped segments of the dendrites of the Renshaw cells and endings of the axoncollaterals of AChE-positive motoneurons are situated on them. Examination of serial sections of the L5-segment of the cat spinal cord revealed that the majority of Renshaw elements and the dendrit-arborization of interneurons of 3. type described by MATSUSHITA are lokalized in the same region. The fact that Renshaw elements in greatest amount could be found in that region of the anterior horn, where the Renshaw inhibition can be electrophysiologically elicited, seems to evidence they role in the latter.

Acetylcholinesterase↗
PubMed1977

[Complications of kidney transplants].

Increasingly more publications are reported on reassuring results after kidney transplantation. After some initial difficulties promising results were achieved on three patients who now live with a transplanted kidney. The importance of improving diagnostic possibilities and the reduction of damages caused by immunosuppressive drugs is stressed and the possibility of altering if necessary the combination of drugs is suggested.

Host vs Graft Reaction↗
PubMed1976

[The localization of the acetylcholinesterase in the area postrema and area subpostrema of the rat. Light and electron microscopical investigations (author's transl)].

In perfusion fixed material was studied the localization of acetylcholinesterase in the region of rat Area postrema on frozen slides and chopped tissue light and electron microscopically. In the light microscope there was a week reaction in the parenchyma cells of the Area postrema and the capillary endothelium and some nerve fibres of the Area subpostrema. Electron microscopically was demonstrated the AChE in the perinuclear cisterna, in the cisternae of the rough endoplasmatic reticulum and the neurotubuli of the axons and dendrites in the Area postrema. It was also evidenced the AChE-reaction in the pinocytic vesicles of the capillary endothelium, the axons, dendrites and some other structural elements of the neuropil in the Area subpostrema. The results were discussed from the standpoint of the functional morphology.

Acetylcholinesterase↗
PubMed1975

Electron cytochemistry of acetylcholinesterase in the neuromuscular junction during ontogenesis.

Electron histochemical studies were performed on neuromuscular junctions of the diaphragm in early postnatal states of development in rat by means of the acetylthiocholine technique. Presynaptic AChE appears to be derived from perikaryal sources, carried along by means of axonal transport mechanisms. Postsynaptic AChE is synthesized in the sarcotubular system of the underlying muscle fiber and within the perinuclear and endoplasmic reticulum of fundamental cells. Distribution of AChE synthesizing loci parallels with that of acetylcholine sensitive areas.

Acetylcholinesterase↗
PubMed1975

Histochemical localization of capillary enzyme activities in brain smears.

Since the regulation of the vascular permeability in the CNS is dependent partly on the enzymes associated with the wall of brain capillaries, the histochemical demonstration of these enzymes may furnish further data on the function of the blood brain barrier (BBB), a new methodological approach, using brain smears was developed for the histochemical demonstration of several enzymes participating in the function of the BBB. The method presented renders possible also the subsequent demonstration of monoamines and the activity of different enzymes in the same tissue preparation. The usefulness of this simple technique in the study of brain capillary functions is discussed.

Acetylcholinesterase↗