Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 4 de 4
Filtrar
Mais filtros

Base de dados
Tipo de documento
Assunto da revista
País de afiliação
Intervalo de ano de publicação
1.
Folia Morphol (Warsz) ; 76(1): 74-81, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-27665952

RESUMO

BACKGROUND: Additional extrinsic muscles of the tongue are reported in literature and one of them is the myloglossus muscle (MGM). Since MGM is nowadays considered as anatomical variant, the aim of this study is to clarify some open questions by evaluating and describing the myloglossal anatomy (including both MGM and its ligamentous counterpart) during human cadaver dissections. MATERIALS AND METHODS: Twenty-one regions (including masticator space, sublingual space and adjacent areas) were dissected and the presence and appearance of myloglossus were considered, together with its proximal and distal insertions, vascularisation and innervation. RESULTS: The myloglossus was present in 61.9% of cases with muscular, ligamentous or mixed appearance and either bony or muscular insertion. Facial artery provided myloglossal vascularisation in the 84.62% and lingual artery in the 15.38%; innervation was granted by the trigeminal system (buccal nerve and mylohyoid nerve), sometimes (46.15%) with hypoglossal component. CONCLUSIONS: These data suggest us to not consider myloglossus as a rare anatomical variant.


Assuntos
Língua/anatomia & histologia , Língua/irrigação sanguínea , Língua/inervação , Cadáver , Feminino , Humanos , Masculino
2.
Folia Morphol (Warsz) ; 75(1): 112-116, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-26365851

RESUMO

The digastric muscle is an important surgical landmark. Several anatomical variants of the digastric muscle are reported in literature and, in particular, the presence of accessory anterior bellies of the muscle is not uncommon. Here, an unreported symmetrical variant of the digastric muscle was found during a dissection of the suprahyoid region. The dissection showed digastric muscles with an accessory anterior belly, which originated from the anterior belly of muscles in proximity and anteriorly to the intermediate tendon. The accessory bellies were fused together on the midline and were attached with a unique tendon to the inner surface of the mental symphysis. These muscles completely filled the submental triangle. This unreported anatomical variant could be considered an additional contribution to description of the anatomical variants of the digastric muscle, with several implications in head and neck pathology, diagnosis and surgery.


Assuntos
Músculos do Pescoço , Variação Anatômica , Dissecação , Cabeça , Tendões
3.
J Phys Chem B ; 110(11): 5409-15, 2006 Mar 23.
Artigo em Inglês | MEDLINE | ID: mdl-16539476

RESUMO

The room temperature cation occupancy in LiMgVO(4) and LiZnVO(4) crystallographic sites is obtained by means of the combined use of X-ray powder diffraction (XRPD), (7)Li and (51)V magic angle spinning nuclear magnetic resonance (MAS NMR), and micro-Raman measurements. In the LiMgVO(4) Cmcm orthorhombic structure, the 4c (C(2)(v) symmetry) tetrahedral vanadium site is fully ordered; on the contrary, the Li 4c tetrahedral site and the 4b (C(2)(h) symmetry) Mg octahedral site display about 22% of reciprocal cationic exchange. Higher cationic disorder is observed in LiZnVO(4): the three cations can distribute on the three tetrahedral and distinct sites of the R-3 structure. XRPD and MAS NMR analysis results highly agree for what concerns vanadium ion distribution on the three cationic sites (about 25, 26, and 47%). From the full profile fitting of XRPD patterns with the Rietveld method, it is also obtained that Li(+) displays a slightly preferred occupation of the T1 position (approximately 55%) and Zn(2+) of the T2 position (approximately 46%). The vibrational spectra of the two compounds are characterized by different peak positions and broadening of the Raman modes, reflecting the cation distribution and the local vibrational unit distortion. A comparison is also made with recent Raman results on Li(3)VO(4). High temperature XRPD measurements rule out possible structural transitions up to 673 K for both compounds.

4.
Cell Calcium ; 57(2): 57-68, 2015 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-25573187

RESUMO

Saccharomyces cerevisiae cells respond to hypotonic stress (HTS) by a cytosolic calcium rise, either generated by an influx of calcium from extracellular medium, when calcium is available, or by a release from intracellular stores in scarcity of extracellular calcium. Calcium release from intracellular compartments is peculiarly inhibited by external calcium in a calcineurin-independent and Cch1-, but not Mid1-, driven manner. HTS-induced calcium release is also negatively regulated by the ER protein Cls2 and involves a poorly characterized protein, FLC2/YAL053W gene product, previously proposed to be required for FAD transport in the ER, albeit, due to its molecular features, it was also previously classified as an ion transporter. A computational analysis revealed that this gene and its three homologs in S. cerevisiae, together with previously identified Schizosaccharomyces pombe pkd2 and Neurospora crassa calcium-related spray protein, belong to a fungal branch of TRP-like ion transporters related to human mucolipin and polycystin 2 calcium transporters. Moreover, disruption of FLC2 gene confers severe sensitivity to Calcofluor white and hyper-activation of the cell wall integrity MAPK cascade, suggesting a role in cell wall maintenance as previously suggested for the fission yeast homolog. Perturbation in cytosolic resting calcium concentration and hyper-activation of calcineurin in exponentially growing cells suggest a role for this transporter in calcium homeostasis in yeast.


Assuntos
Canais de Cálcio/metabolismo , Sinalização do Cálcio , Retículo Endoplasmático/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/metabolismo , Calcineurina/metabolismo , Cálcio/metabolismo , Canais de Cálcio/genética , Proteínas de Ligação ao Cálcio/metabolismo , Glicoproteínas de Membrana/genética , Glicoproteínas de Membrana/metabolismo , Proteínas Quinases Ativadas por Mitógeno/metabolismo , Mutação , Pressão Osmótica , Proteínas de Saccharomyces cerevisiae/genética , Canais de Cátion TRPC/genética , Canais de Cátion TRPC/metabolismo
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA