Speech coding at 4800 bps for mobile satellite communications

A speech compression project has recently been completed to develop a speech coding algorithm suitable for operation in a mobile satellite environment aimed at providing telephone quality natural speech at 4.8 kbps. The work has resulted in two alternative techniques which achieve reasonably good communications quality at 4.8 kbps while tolerating vehicle noise and rather severe channel impairments. The algorithms are embodied in a compact self-contained prototype consisting of two AT and T 32-bit floating-point DSP32 digital signal processors (DSP). A Motorola 68HC11 microcomputer chip serves as the board controller and interface handler. On a wirewrapped card, the prototype's circuit footprint amounts to only 200 sq cm, and consumes about 9 watts of power

The epidermal growth factor receptor (EGFR) is proteolytically modified by the Matriptase–Prostasin serine protease cascade in cultured epithelial cells

AbstractProstasin is expressed at the apical surface of normal epithelial cells and suppresses in vitro invasion of cancer cells. Prostasin re-expression in the PC-3 prostate carcinoma cells down-regulated the epidermal growth factor receptor (EGFR) protein expression and EGF-induced phosphorylation of the extracellular signal-regulated kinases (Erk1/2). We report here that prostasin and its activating enzyme matriptase are capable of inducing proteolytic cleavages in the EGFR extracellular domain (ECD) when co-expressed in the FT-293 cells, generating two amino-terminally truncated fragments EGFR135 and EGFR110, at 135 and 110 kDa. Prostasin's role in EGFR cleavage is dependent on the serine active-site but not the GPI-anchor. The modifications of EGFR were confirmed to be on the primary structure by deglycosylation. EGFR135 and EGFR110 are not responsive to EGF stimulation, indicating loss of the ligand-binding domains. EGFR110 is constitutively phosphorylated and in its presence Erk1/2 phosphorylation is increased in the absence of EGF. The protease-induced EGFR cleavages are not dependent on EGFR phosphorylation. The EGFR ECD proteolytic modification by matriptase–prostasin is also observed in the BEAS-2B normal lung epithelial cells, the BPH-1 benign prostate hyperplasia and the MDA-MB-231 breast cancer cell lines; and represents a novel mechanism for epithelial cells to modulate EGF-EGFR signaling

Identification of protein-RNA interaction sites using the information of spatial adjacent residues

<p>Abstract</p> <p>Background</p> <p>Protein-RNA interactions play an important role in numbers of fundamental cellular processes such as RNA splicing, transport and translation, protein synthesis and certain RNA-mediated enzymatic processes. The more knowledge of Protein-RNA recognition can not only help to understand the regulatory mechanism, the site-directed mutagenesis and regulation of RNA–protein complexes in biological systems, but also have a vitally effecting for rational drug design.</p> <p>Results</p> <p>Based on the information of spatial adjacent residues, novel feature extraction methods were proposed to predict protein-RNA interaction sites with SVM-KNN classifier. The total accuracies of spatial adjacent residue profile feature and spatial adjacent residues weighted accessibility solvent area feature are 78%, 67.07% respectively in 5-fold cross-validation test, which are 1.4%, 3.79% higher than that of sequence neighbour residue profile feature and sequence neighbour residue accessibility solvent area feature.</p> <p>Conclusions</p> <p>The results indicate that the performance of feature extraction method using the spatial adjacent information is superior to the sequence neighbour information approach. The performance of SVM-KNN classifier is little better than that of SVM. The feature extraction method of spatial adjacent information with SVM-KNN is very effective for identifying protein-RNA interaction sites and may at least play a complimentary role to the existing methods.</p

Progressive decay of Ca2+ homeostasis in the development of diabetic cardiomyopathy

BACKGROUND: Cardiac dysfunction in diabetic cardiomyopathy may be associated with abnormal Ca(2+) homeostasis. This study investigated the effects of alterations in Ca(2+) homeostasis and sarcoplasmic reticulum Ca(2+)-associated proteins on cardiac function in the development of diabetic cardiomyopathy. METHODS: Sprague–Dawley rats were divided into 4 groups (n = 12, each): a control group, and streptozotocin-induced rat models of diabetes groups, examined after 4, 8, or 12 weeks. Evaluations on cardiac structure and function were performed by echocardiography and hemodynamic examinations, respectively. Cardiomyocytes were isolated and spontaneous Ca(2+) spark images were formed by introducing fluorescent dye Fluo-4 and obtained with confocal scanning microscopy. Expressions of Ca(2+)-associated proteins were assessed by Western blotting. RESULTS: Echocardiography and hemodynamic measurements revealed that cardiac dysfunction is associated with the progression of diabetes, which also correlated with a gradual but significant decline in Ca(2+) spark frequency (in the 4-, 8- and 12-week diabetic groups). However, Ca(2+) spark decay time constants increased significantly, relative to the control group. Expressions of ryanodine receptor 2 (RyR2), sarcoplasmic reticulum Ca(2+)-2ATPase (SERCA) and Na(+)/Ca(2+) exchanger (NCX1) were decreased, together with quantitative alterations in Ca(2+)regulatory proteins, FKBP12.6 and phospholamban progressively and respectively in the diabetic rats. CONCLUSIONS: Ca(2+) sparks exhibited a time-dependent decay with progression of diabetic cardiomyopathy, which may partly contribute to cardiac dysfunction. This abnormality may be attributable to alterations in the expressions of some Ca(2+)-associated proteins