Ultrastructure of the myelinated and unmyelinated nerve fibers of the tongue mucosa of albinus rat (Wistar) with aging / Ultraestructura de las Fibras Nerviosas Mielínicas y Amielínicas de la Mucosa Lingual de ratas Albinas (Wistar) Envejecidas

El objetivo de esta investigación fue estudiar las fibras sensitivas mielinizadas y amielínicas localizadas en la lámina propia subepitelial de la mucosa lingual de ratas. Se usó el método de impregnación argéntica, microscopía MET y mediciones morfométricas. Los resultados revelaron que los fascículos de fibras subepiteliales de las regiones anterior, media y posterior de la lengua provenían de su capa muscular profunda. Los grupos de fibras fueron localizados dentro del tejido conectivo de la lámina propia. Estas fibras nerviosas se ramificaron varias veces y en el tejido conectivo de las papilas formaron terminaciones simples o ramificados. Las papilas fungiformes y valadas contenían numerosas terminaciones nerviosas. La ultraestructura demostró en el axoplasma la presencia de neurofilamentos, mitocondrias y microtúbulos; aunque los registros morfométricos de las fibras mielinizadas mostraron que alrededor del 44 por ciento tenían un diámetro entre 3 y 4 µm, el valor promedio fue de 4.5 µm. El diámetro mayor fue de 12 µm y el menor de 1.4 um. Los rangos de menores diámetros fueron de 1 a 3 µm, siendo el promedio de 2.33 µm. En relación al espesor de las vainas de mielina, los valores obtenidos fueron de 0.2 a 0.8 um siendo el valor promedio de alrededor de 0,5 µm, en el 90 por ciento de ellas. En las fibras amielínicas los mayores diámetros (62 por ciento) variaron entre 0.25 y 0.75 µm. El valor promedio fue de 0.6 µm, siendo el valor máximo 3.17 µm y el mínimo 0.2 µm. El menor diámetro fue obtenido en 44 por ciento de las fibras amielínicas y los rangos variaron entre 0.2 y 0.4 µm. El valor máximo obtenido fue de 1 µm y el mínimo 0.12 µm.

The purpose of this paper was to study the sensory myelinated and unmyelinated nerve fibers found in the subepithelial lamina propria of tongue mucosa of aging rats. It was used the silver impregnation, transmission electron microscopy methods and morphometric measurements. The results revealed that subepithelial nerve fiber bundles of the anterior, medium and posterior regions of tongue were arise from deep muscular layer of tongue. The nerve fiber bundles were verified inside of the connective tissue of lamina propria. These nerve fibers branched several times and into the connective tissue papillae they form a single or ramified sensory nerve endings. The fungiform and vallate papillae contain numerous nerve terminals. The fine structure demonstrated that in the axoplasm were noted the presence of neurofilaments, mitochondria and microtubules. Although the morphometric data of myelinated fibers showed that about 44% having larger diameter between 3 to 4 µm and the mean value was 4.5 µm. The largest diameter was 12 µm and the smaller was 1.4 um. The smallest diameter ranges from 1 to 3 µm, being that the mean value was 2.33 µm. Concerning to the thickness of myelin sheets were revealed the values ranging from 0.2 to 0.8 µm being that the 90% present the values around 0.5 µm. The unmyelinated fibers showed the largest diameter (62%) varying from 0.25 to 0.75 µm. The mean value was 0.6 µm being the maximum value was 3.17 µm and the minimum was 0.2 µm. The smallest diameter was obtained in 44% of unmyelinated fibers which the diameter ranges from 0.2 to 0.4 µm.Then maximum value obtained was 1 µm and the minimum was 0.12 µm.

Selective regulation of G protein-coupled receptor-mediated signaling by G protein-coupled receptor kinase 2 in FRTL-5 cells: analysis of thyrotropin, alpha(1B)-adrenergic, and A(1) adenosine receptor-mediated responses.

G protein-coupled receptor kinases (GRKs) play a key role in the process of receptor homologous desensitization. In the present study, we address the question of whether a variety of receptors coupled to different G protein subtypes and naturally expressed on the same cell are selectively regulated by GRK2. The signaling stimulated by thyrotropin (TSH), alpha(1B)-adrenergic, and A(1) adenosine receptors was studied in FRTL-5 cells permanently transfected to overexpress GRK2 and GRK2-K220R, a kinase dead GRK dominant negative mutant. In FRTL-5 overexpressing GRK2, TSH-induced cyclic AMP response was attenuated, indicating that TSH receptor is desensitized by this kinase. Consistently, FRTL-5 cells overexpressing GRK2-K220R show increased TSH-induced cyclic AMP response, demonstrating that this receptor is under tonic control by GRK. Unlike TSH receptor, alpha(1B)-adrenergic receptor response was unaffected in FRTL-5 overexpressing GRK2 and GRK2-K220R. When A(1) adenosine receptors were stimulated, G(ialpha)-mediated cyclic AMP inhibition was totally unaffected by overexpression of either GRK2 or GRK2-K220R. By contrast, G(betagamma)-mediated response (activation of mitogen-activated protein kinases) was efficiently desensitized by GRK2 but was unaffected by GRK2-K220R overexpression. The present study documents that overexpression of GRK2 results in a selective regulation of different G protein-coupled receptors expressed on the same cell and that this kinase can regulate preferentially only one of the different pathways activated by the same receptor. The preferential regulation of the A(1) adenosine receptor-stimulated mitogen-activated protein kinases by GRK2 indicates that this kinase can have additional regulatory effects on G(betagamma)-stimulated pathways, possibly through direct binding and regulation of the receptor-G(betagamma) complex.

Human plasma kallikrein. Preliminary studies on hydrolysis of proteins and peptides.

Acid-activated human plasma kallikrein (HuPK) was purified from human Cohn fraction IV by affinity chromatography, using a ligand soybean trypsin inhibitor and aminobenzamidine. The purified enzyme does not inactivate bradykinin and lysyl-bradykinin by cleavage of their peptide bonds. Methionyl-lysyl-bradykinin is converted to the more potent peptide, bradykinin, by incubation with plasma kallikrein. The enzyme does not show aminopeptidase activity when assayed with amino-acyl-naphthylamides. Arginine-rich polypeptides and proteins, such as polyarginine, salmine, and histones were cleaved by the enzyme. HuPK does not show any detectable caseinolytic activity. A kinin is released from a non-homologous plasma (horse) by this kallikrein. The enzyme is not affected by calcium or EDTA, and it is strongly inhibited by copper ion.