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Found: 5 471
Page 190 of 548-
[On the behavior of the pineal gland under conditions of stress].
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Cytological evidence for catecholamine-containing sensory cells bordering the ventricle of the toad hypothalamus.
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[Histophysiology of the endocrine system after disturbance of nervous regulation mechanisms].
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[Ultrastructure of the neurohypophysis of dogs in reflexogenic hypertension].
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The effect of transient cerebral ischemia on the vascular permeability to protein tracers.
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[Liquor contacting neurons in the nucleus lateralis tuberis of fishes].
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Ultrastructure of neurons in the nucleus basalis of Meynert in squirrel monkey.
The nucleus basalis of Meynert in the squirrel monkey exhibits numerous labeled neurons following the retrograde transport of horseradish peroxidase from occipital cortical injection sites. The typically large, often clustered, labeled cells are seen most frequently in association with the fibrous bordering structures of the substantia innominata and in the internal and external laminae of the globus pallidus. Ultrastructurally the copious cytoplasm of nucleus basalis neurons abounds with organelles. Large, vacuolated lipofuscin granules proliferate as a function of age and are not evident in younger monkeys. Approximately 4% of the somal surface is occupied by symmetrical synapses with either flat or pleomorphic vesicles. The remainder is covered mostly by neuroglial processes. Somatic spines bearing synapses are occasionally observed. In the neuropil surrounding nucleus basalis somata, the synapses onto dendrites and spines are mostly asymmetrical with large, round vesicles. Labeled nucleus basalis cells in the substantia innominata immediately lateral to the optic tract are larger and rounder than cells in the internal and external pallidal laminae. However, no remarkable ultrastructural differences were observed between nucleus basalis somata in the substantia innominata and external pallidal lamina, or between horseradish peroxidase-labeled and unlabeled large cells.
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Sonication-enhanced histochemistry of wheat germ agglutinin binding to intracellular sites of rat layer V cortical neurons and spinal motoneurons.
Cellular surface carbohydrates have been studied extensively in relation to cell interactions. However, the presence of intracellular carbohydrates not associated with cell surface membranes has not been well-defined histochemically. We describe a technique for the ultrastructural localization of intracytoplasmic carbohydrates using a wheat germ agglutinin peroxidase conjugate. The ultrastructural aspects of wheat germ agglutinin (WGA) binding to intracellular structures of rat somatomotor cortex layer V neurons and spinal cord motoneurons were examined using sonication to enhance penetration of the lectin-peroxidase conjugate. In addition to the membrane-associated structures previously described by others, WGA binding was observed on neuronal nuclear chromatin, nuclear pores, ribosomes, microtubules, vesicular organelles, and to synaptic complexes, primarily in the presynaptic bouton. The results support data indicating that complex carbohydrates may be important in neuronal molecular processing.
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Fluorescence and electron microscopic study of the tree shrew pineal organ.
The fine structure of the pineal gland and the pineal innervation in the tree shrew were studied by electron microscopy and glyoxylic acid-induced fluorescence microscopy respectively. The parenchymal cells consist of pinealocytes, glial cells and pigment-containing cells. The pinealocytes are characterized by the presence of granular vesicles, synaptic ribbons, electron-dense bodies and small profiles of rER with dilated cisternae. Glial cells contain light cytoplasmic bodies, lipofuscin granules, bundles of microfilaments, and elongate profiles of rER with flattened cisternae which are often stacked together with light cytoplasmic bodies; the pigment-containing cells are unique in possessing giant pigment granules in the cytoplasm. The pinealocyte/glial cell/pigment cell in tree shrew pineals may be the same cell line of parenchymal cells at different ontogenetic stages. Pigment-containing cells contain pigment granules as a prominent cytoplasmic inclusion, suggesting they are senscent in secretory function. Both pinealocytes and glial cells contain structures suggesting secretory function such as well-developed Golgi complex and granular vesicles. The antigonadotrophic substances may be stored in granular vesicles. The present ultrastructural study supports the conclusion that tree shrew pineal organ is an endocrine gland which is heavily innervated by adrenergic nerves and possibly by cholinergic nerves.
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Localization of calmodulin in rat cerebellum by immunoelectron microscopy.
Calmodulin, a multifunctional Ca(++)-binding protein, is present in all eucaryotic cells. We have investigated the distribution of this protein in the rat cerebellum by immunoelectron microscopy using a Fab-peroxidase conjugate technique. In Purkinje and granular cell bodies, calmodulin reaction product was found localized both on free ribosomes and on those attached to rough endoplasmic reticulum (RER) and the nuclear envelope. No calmoduline was observed in the cisternae of RER or the Golgi apparactus. Calmodulin did not appear to be concentrated in the soluble fraction of the cell under the conditions used. Rather, peroxidase reaction product could be seen associated with membranes of the Golgi apparatus the smooth endoplasmic reticulum (SER), and the plasma membrane of both cell bodies and neuronal processes. In the neuronal dendrites, calmodulin appeared to be concentrated on membranes of the SER, small vesicles, and mitochondria. Also, granular calmodulin was observed in the amorphous material. In the synaptic junction, a large amount of calmodulin was seen attached to the inner surface of the postsynaptic membrane, whereas very little was observed in the presynaptic membrane or vesicles. These observations suggest that calmodulin is synthesized on ribosomes and discharged into the cytosol, and that it then becomes associated with a variety of intracellular membranes. Calmodulin also seems to be transported via neuronal processes to the postsynaptic membrane. Calmodulin localization at the postsynaptic membrane suggests that this protein may mediate calcium effects at the synaptic junction and, thus, may play a role in the regulation of neurotransmission.