RESUMO
HLA-A*11:152 differs from A*11:01:01 by a single nucleotide at position 266 in Exon 2.
Assuntos
Alelos , Loci Gênicos , Antígeno HLA-A11/genética , Células-Tronco Hematopoéticas/imunologia , Polimorfismo de Nucleotídeo Único , Substituição de Aminoácidos , Povo Asiático , Sequência de Bases , Éxons , Expressão Gênica , Antígeno HLA-A11/imunologia , Transplante de Células-Tronco Hematopoéticas , Células-Tronco Hematopoéticas/citologia , Teste de Histocompatibilidade , Humanos , Dados de Sequência Molecular , Alinhamento de Sequência , Análise de Sequência de DNA , Doadores não RelacionadosRESUMO
We demonstrate a robust and versatile solution for locking the continuous-wave dye laser for applications in laser cooling of molecules which need linewidth-narrowed and frequency-stabilized lasers. The dye laser is first stabilized with respect to a reference cavity by Pound-Drever-Hall (PDH) technique which results in a single frequency with the linewidth 200 kHz and short-term stabilization, by stabilizing the length of the reference cavity to a stabilized helium-neon laser we simultaneously transfer the ± 2 MHz absolute frequency stability of the helium-neon laser to the dye laser with long-term stabilization. This allows the dye laser to be frequency chirped with the maximum 60 GHz scan range while its frequency remains locked. It also offers the advantages of locking at arbitrary dye laser frequencies, having a larger locking capture range and frequency scanning range to be implemented via software. This laser has been developed for the purpose of laser cooling a molecular magnesium fluoride beam.
Assuntos
Temperatura Baixa , Lasers de Corante , Fenômenos Ópticos , Eletricidade , Fatores de TempoRESUMO
We theoretically investigated the improvement on the production rate of the decelerated bromine (Br) atoms near zero speed by photodissociating laser aligned Br2 precursors. Adiabatic alignment of Br2 precursors exposed to long laser pulses with duration on the order of nanoseconds was investigated by solving the time-dependent Schrödinger equation. The dynamical fragmentation of adiabatically aligned Br2 precursors was simulated and velocity distribution of the Br atoms produced was analyzed. Our study shows that the larger the degree of the precursor alignment, ⟨cos(2) θ⟩, the higher the production rate of the decelerated Br atoms near zero speed. For Br2 molecules with an initial rotational temperature of ~1 K, a ⟨cos(2) θ⟩ value of ~0.88 can result in an improvement factor of over ~20 on the production rate of the decelerated Br atoms near zero speed, requiring a laser intensity of only ~1 × 10(12) W/cm(2) for alignment.
RESUMO
HLA-A*02:441 differs from HLA-A*02:01:01:01 by one nucleotide exchange at position 91(T>C) with an amino acid exchange.
Assuntos
Alelos , Povo Asiático/genética , Bases de Dados de Ácidos Nucleicos , Antígenos HLA-A/genética , Sequência de Bases , China , Humanos , Dados de Sequência MolecularRESUMO
Overexpression of interleukin (IL-)17 has recently been shown to be associated with a number of pathological conditions. Because IL-17 is found at high levels in the synovial fluid surrounding cartilage in patients with inflammatory arthritis, the present study determined the direct effect of IL-17 on articular cartilage. As shown herein, IL-17 was a direct and potent inducer of matrix breakdown and an inhibitor of matrix synthesis in articular cartilage explants. These effects were mediated in part by leukemia inhibitory factor (LIF), but did not depend on interleukin-1 activity. The mechanism whereby IL-17 induced matrix breakdown in cartilage tissue appeared to be due to stimulation of activity of aggrecanase(s), not matrix metalloproteinase(s). However, IL-17 upregulated expression of matrix metalloproteinase(s) in chondrocytes cultured in monolayer. In vivo, IL-17 induced a phenotype similar to inflammatory arthritis when injected into the intra-articular space of mouse knee joints. Furthermore, a related protein, IL-17E, was found to have catabolic activity on human articular cartilage. This study characterizes the mechanism whereby IL-17 acts directly on cartilage matrix turnover. Such findings have important implications for the treatment of degenerative joint diseases such as arthritis.
Assuntos
Cartilagem Articular/efeitos dos fármacos , Interleucina-17/farmacologia , Animais , Western Blotting , Cartilagem Articular/citologia , Cartilagem Articular/metabolismo , Bovinos , Condrócitos/efeitos dos fármacos , Condrócitos/metabolismo , Técnicas de Cultura , Citocinas/farmacologia , Endopeptidases/metabolismo , Feminino , Injeções Intra-Articulares , Metaloproteinases da Matriz/metabolismo , Camundongos , Camundongos Endogâmicos C57BL , Óxido Nítrico/fisiologia , Patela/metabolismo , Proteoglicanas/efeitos dos fármacos , Proteoglicanas/metabolismo , Suínos , Regulação para CimaRESUMO
The proinflammatory cytokine interleukin 17 (IL-17) is the founding member of a family of secreted proteins that elicit potent cellular responses. We report a novel human IL-17 homolog, IL-17F, and show that it is expressed by activated T cells, can stimulate production of other cytokines such as IL-6, IL-8 and granulocyte colony-stimulating factor, and can regulate cartilage matrix turnover. Unexpectedly, the crystal structure of IL-17F reveals that IL-17 family members adopt a monomer fold typical of cystine knot growth factors, despite lacking the disulfide responsible for defining the canonical "knot" structure. IL-17F dimerizes in a parallel manner like neurotrophins, and features an unusually large cavity on its surface. Remarkably, this cavity is located in precisely the same position where nerve growth factor binds its high affinity receptor, TrkA, suggesting further parallels between IL-17s and neurotrophins with respect to receptor recognition.
Assuntos
Interleucina-17/química , Receptores de Interleucina/metabolismo , Proteínas Recombinantes/metabolismo , Sequência de Aminoácidos , Cartilagem/metabolismo , Cristalografia por Raios X , Cistina/química , Dimerização , Humanos , Interleucina-17/genética , Interleucina-17/metabolismo , Modelos Moleculares , Dados de Sequência Molecular , Família Multigênica , Estrutura Terciária de Proteína , RNA Mensageiro/isolamento & purificação , Receptores de Interleucina-17 , Proteínas Recombinantes/química , Homologia de Sequência de Aminoácidos , Linfócitos T/metabolismo , Distribuição TecidualRESUMO
PYRIN domains were identified recently as putative protein-protein interaction domains at the N-termini of several proteins thought to function in apoptotic and inflammatory signaling pathways. The approximately 95 residue PYRIN domains have no statistically significant sequence homology to proteins with known three-dimensional structure. Using secondary structure prediction and potential-based fold recognition methods, however, the PYRIN domain is predicted to be a member of the six-helix bundle death domain-fold superfamily that includes death domains (DDs), death effector domains (DEDs), and caspase recruitment domains (CARDs). Members of the death domain-fold superfamily are well established mediators of protein-protein interactions found in many proteins involved in apoptosis and inflammation, indicating further that the PYRIN domains serve a similar function. An homology model of the PYRIN domain of CARD7/DEFCAP/NAC/NALP1, a member of the Apaf-1/Ced-4 family of proteins, was constructed using the three-dimensional structures of the FADD and p75 neurotrophin receptor DDs, and of the Apaf-1 and caspase-9 CARDs, as templates. Validation of the model using a variety of computational techniques indicates that the fold prediction is consistent with the sequence. Comparison of a circular dichroism spectrum of the PYRIN domain of CARD7/DEFCAP/NAC/NALP1 with spectra of several proteins known to adopt the death domain-fold provides experimental support for the structure prediction.