RESUMO
The safety of the endoscopic technique for carpal tunnel release remains a major concern. Serious complications such as division nerves, tendons or vessels may occur. In this study the topography of the carpal tunnel was studied in fresh cadaver hands after the introduction of the blade assembly of a one portal system. By using a plastination method, it was possible to study the in situ relationships in detail by serial cross sections. Furthermore a modified Spalteholz method allowed the position of the blade to be viewed in whole specimens.
Assuntos
Artroscópios , Síndrome do Túnel Carpal/patologia , Articulação do Punho/anatomia & histologia , Idoso , Anatomia Transversal , Cadáver , Síndrome do Túnel Carpal/cirurgia , Feminino , Humanos , Masculino , Complicações Pós-Operatórias/prevenção & controle , Articulação do Punho/cirurgiaRESUMO
The ORF YOL018c (TLG2) of Saccharomyces cerevisiae encodes a protein that belongs to the syntaxin protein family. The proteins of this family, t-SNAREs, are present on target organelles and are thought to participate in the specific interaction between vesicles and acceptor membranes in intracellular membrane trafficking. TLG2 is not an essential gene, and its deletion does not cause defects in the secretory pathway. However, its deletion in cells lacking the vacuolar ATPase subunit Vma2p leads to loss of viability, suggesting that Tlg2p is involved in endocytosis. In tlg2Delta cells, internalization was normal for two endocytic markers, the pheromone alpha-factor and the plasma membrane uracil permease. In contrast, degradation of alpha-factor and uracil permease was delayed in tlg2Delta cells. Internalization of positively charged Nanogold shows that the endocytic pathway is perturbed in the mutant, which accumulates Nanogold in primary endocytic vesicles and shows a greatly reduced complement of early endosomes. These results strongly suggest that Tlg2p is a t-SNARE involved in early endosome biogenesis.
Assuntos
Endocitose/fisiologia , Fatores de Troca do Nucleotídeo Guanina , Proteínas de Membrana/química , Proteínas de Membrana/metabolismo , Proteínas de Transporte de Nucleotídeos , Organelas/fisiologia , Proteínas de Saccharomyces cerevisiae , Saccharomyces cerevisiae/fisiologia , ATPases Vacuolares Próton-Translocadoras , Sequência de Aminoácidos , Cromossomos Fúngicos , Clonagem Molecular , Proteínas Fúngicas/biossíntese , Proteínas Fúngicas/genética , Deleção de Genes , Cinética , Fator de Acasalamento , Proteínas de Membrana/genética , Proteínas de Membrana Transportadoras/genética , Proteínas de Membrana Transportadoras/metabolismo , Dados de Sequência Molecular , Fases de Leitura Aberta , Organelas/ultraestrutura , Peptídeos/genética , Peptídeos/metabolismo , ATPases Translocadoras de Prótons/genética , ATPases Translocadoras de Prótons/metabolismo , Proteínas Qa-SNARE , Proteínas Recombinantes de Fusão/biossíntese , Saccharomyces cerevisiae/genética , Alinhamento de Sequência , Homologia de Sequência de AminoácidosRESUMO
end4-1 was isolated as a temperature-sensitive endocytosis mutant. We cloned and sequenced END4 and found that it is identical to SLA2/MOP2. This gene is required for growth at high temperature, viability in the absence of Abp1p, polarization of the cortical actin cytoskeleton, and endocytosis. We used a mutational analysis of END4 to correlate in vivo functions with regions of End4p and we found that two regions of End4p participate in endocytosis but that the talin-like domain of End4p is dispensable. The N-terminal domain of End4p is required for growth at high temperature, endocytosis, and actin organization. A central coiled-coil domain of End4p is necessary for formation of a soluble sedimentable complex. Furthermore, this domain has an endocytic function that is redundant with the function(s) of ABP1 and SRV2. The endocytic function of Abp1p depends on its SH3 domain. In addition we have isolated a recessive negative allele of SRV2 that is defective for endocytosis. Combined biochemical, functional, and genetic analysis lead us to propose that End4p may mediate endocytosis through interaction with other actin-associated proteins, perhaps Rvs167p, a protein essential for endocytosis.
