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Myosin VI (MVI) is the only known myosin walking towards minus end of actin filaments. Here, MVI, but not myosins IB or IIB, was detected in chromaffin granules isolated from bovine medulla and found to be tightly associated with the granule apical surface. MVI also localized to secretory granules within rat pheochromocytoma PC12 cells as well as to the Golgi apparatus, endoplasmic reticulum and clathrin-coated pits. Notably, it was also found in the nucleus. RT-PCR revealed that MVI splice variants with a large insert (LI), characteristic of polarized cells, were barely detectable in PC12 cells, whereas variants with a small insert (SI) were the major isoforms. The presented data indicate that MVI in adrenal medulla cells is engaged in secretory vesicle trafficking within the cytoplasm and possibly also involved in transport within the nucleus.
The adrenal glands from 15 guinea pigs aged 90 days were used in the study. Paraffin slices were stained with Mayer haematoxylin and eosin with Masson method and silvered. The histochemical reactions were carried out for catecholamines and the biochemical determinations of catecholamines. Ultrastructural observations were also performed. In the adrenal medulla of sexually mature guinea pigs numerous epinephrocites and no noreoinefrocites were observed when histochemical methods were used. The small and large ganglion cells accompanying the supporting and neurolemmal cells formed typical gangliar weaving (medullary ganglia). Apart from epinephrocytes, small and large ganglion cells and supporting and neurolemmal cells, small intensively fluorescent (SIF) cells were also detected. Biochemical investigation revealed that the mean content of adrenaline calculated for a pair of adrenal glands was 98.87% of the pool of catecholamines, whereas the mean content of noradrenaline was 1.00%, and of dopamine 0.13%.
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In addition to the central nervous system, glutamate receptors have been recently identified in a number of peripheral tissues, including adrenals. Pharmacological evidence indicates that adrenal glutamate receptors may be involved in stress response, particularly in catecholamine release. However, possible stress-induced changes at the level of local receptors themselves have not been evaluated yet. This study was aimed to investigate gene expression of N-methyl-D-aspartate (NMDA) receptor subunits (NR1, NR2A, NR2B) in rat adrenal gland under basal and stress conditions, using RT-PCR. NR1 mRNA was found to be present in the adrenal gland, while mRNAs coding for NR2-type subunits failed to be detected in adrenal tissue. The distribution of NR1 mRNA in rat adrenals showed higher concentrations in the adrenal medulla (228%) compared to those in the cortex. Single stress stimulus (immobilization) induced a significant increase of NR1 gene expression in both medullar (by 25%) and cortical (by 66%) regions of the adrenal gland at 24 h, while no changes were observed at 3 h after the stress exposure. It is possible that delayed rise in adrenal NR1 gene expression following stress exposure represents one of the factors by which stress exerts long-term effects on adrenal function at the molecular level.
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