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1.
J Opt Soc Am A Opt Image Sci Vis ; 38(8): 1237-1247, 2021 Aug 01.
Artículo en Inglés | MEDLINE | ID: mdl-34613319

RESUMEN

This work reports the 3D reconstruction of a particle from a set of three simulated interferometric images of this particle (from three perpendicular angles of view). The reconstruction of each view from its corresponding interferometric pattern uses the error-reduction (ER) algorithm. The 3D reconstruction enables an estimation of the volume of the particle. The method is tested on a dendrite-like particle. An experimental demonstration of the technique is done using a digital micromirror device (DMD) that generates the interferometric images of "programmable" rough particles.

2.
Rev Sci Instrum ; 90(5): 053109, 2019 May.
Artículo en Inglés | MEDLINE | ID: mdl-31153261

RESUMEN

The characterization of ice crystals has important applications in airborne research and civil aviation. Interferometric out-of-focus imaging is a promising technique. We investigate in this study the impact of the 3D shape reconstruction of the particles from a pair of interferometric images on the estimation of the ice particle's volume. An interferometric image gives indeed the 2D autocorrelation of the particle's shape. As different shapes can exhibit a similar 2D autocorrelation, particles of different shapes can have similar interferometric images. In this study, the volume of ice particles is estimated from a pair of interferometric images (with two perpendicular angles of view). The relative error in the particle's volume estimation is shown to be around ΔV V≈30% depending on the choice of the initial 3D particle's shape. It appears that the choice of the shape of the particle for both angles of view has a lower impact on the estimation of the particle's volume than the other sources of errors due to image acquisitions themselves.

3.
Mol Cell Biol ; 16(9): 4710-6, 1996 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-8756628

RESUMEN

Interleukin-9 (IL-9), a T-cell-derived cytokine, interacts with a specific receptor associated with the IL-2 receptor gamma chain. In this report, we analyze the functional domains of the human IL-9 receptor transfected into mouse lymphoid cell lines. Three different functions were examined: growth stimulation in factor-dependent pro-B Ba/F3 cells, protection against dexamethasone-induced apoptosis, and Ly-6A2 induction in BW5147 lymphoma cells. The results indicated that a single tyrosine, at position 116 in the cytoplasmic domain, was required for all three activities. In addition, we observed that human IL-9 reduced the proliferation rate of transfected BW5147 cells, an effect also dependent on the same tyrosine. This amino acid was necessary for IL-9-mediated tyrosine phosphorylation of the receptor and for STAT activation but not for IRS-2/4PS activation or for JAK1 phosphorylation, which depended on a domain closer to the plasma membrane. We also showed that JAK1 was constitutively associated with the IL-9 receptor. Activated STAT complexes induced by IL-9 were found to contain STAT1, STAT3, and STAT5 transcription factors. Moreover, sequence homologies between human IL-9 receptor tyrosine 116 and tyrosines (of other receptors activating STAT3 and STAT5 were observed. Taken together, these data indicate that a single tyrosine of the IL-9 receptor, required for activation of three different STAT proteins, is necessary for distinct activities of this cytokine, including proliferative responses.


Asunto(s)
Apoptosis/fisiología , Proteínas de Unión al ADN/metabolismo , Proteínas de la Leche , Receptores de Interleucina/química , Transactivadores/metabolismo , Tirosina/química , Secuencia de Aminoácidos , Animales , Antígenos Ly/biosíntesis , Antígenos Ly/genética , Secuencia de Bases , División Celular/fisiología , Humanos , Interleucina-9/farmacología , Interleucina-9/fisiología , Janus Quinasa 1 , Janus Quinasa 3 , Linfoma/patología , Sarcoma de Mastocitos/patología , Ratones , Datos de Secuencia Molecular , Fosforilación , Procesamiento Proteico-Postraduccional , Proteínas Tirosina Quinasas/metabolismo , Receptores de Eritropoyetina/química , Receptores de Interleucina/fisiología , Receptores de Interleucina-2/química , Receptores de Interleucina-9 , Proteínas Recombinantes/metabolismo , Factor de Transcripción STAT1 , Factor de Transcripción STAT3 , Factor de Transcripción STAT5 , Homología de Secuencia de Aminoácido , Transducción de Señal , Relación Estructura-Actividad , Transfección , Células Tumorales Cultivadas
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