Articles by Chen Chun Chiang in JoVE
Entrenamiento de la resistencia Adaptado mejora la fuerza en ocho semanas en personas con esclerosis múltiple Jennifer L. Keller1, Nora Fritz1,2, Chen Chun Chiang1, Allen Jiang1, Tziporah Thompson3, Nicole Cornet1, Scott D. Newsome4, Peter A. Calabresi4, Kathleen Zackowski1,2,4 1Motion Analysis Laboratory, Kennedy Krieger Institute, 2Physical Medicine & Rehabilitation, Johns Hopkins University School of Medicine, 3Johns Hopkins University School of Medicine, 4Department of Neurology, Johns Hopkins University School of Medicine Debilidad de cadera es un síntoma común que afecta a la capacidad de caminar en las personas con esclerosis múltiple. Fortalecimiento muscular aislada es un método útil para apuntar debilidades específicas. Este protocolo describe un programa de entrenamiento de resistencia progresiva utilizando bandas de ejercicio para aumentar la fuerza muscular de la cadera.
Other articles by Chen Chun Chiang on PubMed
Modeling Rhl Quorum-sensing Regulation on Rhamnolipid Production by Pseudomonas Aeruginosa Biotechnology Progress. Sep-Oct, 2004 | Pubmed ID: 15458313 The effect of autoinducer PAI2 on rhamnolipid (RL) production by Pseudomonas aeruginosa was evaluated using an rhlI null mutant of PAO1 added with PAI2 at various concentrations. A model has also been developed to describe the production kinetics regulated by the rhl quorum-sensing system in three steps: First, PAI2 combines with RhlR protein. Second, the activated complex RhlR:PAI2 triggers the transcription (and expression) of the rhlAB operon that encodes for rhamnosyltransferase. Finally, the enzyme catalyzes the RL synthesis. The model describes fairly well the experimental results/profiles from three different studies (this and two others reported in the literature). The overall picture predicted by the model is as follows: The induced enzyme synthesis proceeds at the highest rate following PAI2 addition. The rate decreases with time as the autoinducer is degraded. The enzyme concentration nonetheless continues to increase until reaching the plateau at the exhaustion of autoinducer. Higher added PAI2 concentrations thus give not only higher initial enzyme synthesis rates but also longer induced synthesis. As the enzyme concentration increases with time, the RL production rate also increases, resulting in an accelerated rise in RL concentrations initially. The increase in RL concentrations becomes linear at the exhaustion of PAI2. The best-fit model parameters obtained also provided important insights. To complex half of the intracellular RhlR proteins would require 1.61 microM PAI2, about half of the PAI2 concentration obtained in the stationary-phase culture of wild-type PAO1. On the other hand, to activate the rhamnosyltransferase synthesis at half of its maximum rate would require the binding of 39% of RhlR with PAI2. The maximum RL production rate of the culture was found to be 0.042 g/L.h, and the fully induced culture would require at least 1.61 h to synthesize the enzyme to the necessary level for producing RL at half of the maximum rate.
Degradation and Synthesis Kinetics of Quorum-sensing Autoinducer in Pseudomonas Aeruginosa Cultivation Journal of Biotechnology. Apr, 2005 | Pubmed ID: 15831242 The quorum-sensing (las and rhl) systems play critical roles in the pathogenicity of Pseudomonas aeruginosa and its synthesis of the important biosurfactants, rhamnolipids. In this work, P. aeruginosa PAO1 and its rhlI and rhlR null mutants were used to study the degradation and synthesis kinetics of the rhl system's autoinducer PAI2 (N-butanoyl-homoserine lactone). The two mutants, lacking the ability of synthesizing PAI2 or RhlR protein, produced insignificant amounts of rhamnolipids while having similar growth profiles as the wild-type culture. The regulatory RhlR:PAI2 complex is thus essential to rhamnolipid synthesis. In batch culture of the wild-type PAO1, the autoinducer PAI2 concentration increased along cell growth, especially during the transition from exponential-growth phase to stationary phase, and began to decrease after entering the stationary phase. The decrease in the stationary phase resulted from a faster PAI2 degradation than its synthesis. The degradation kinetics was studied using PAI2-containing supernatants (from centrifuged broth of wild-type culture) with and without the rhlI(-) mutant cells incapable of PAI2 synthesis. Being insignificant in the cell-free systems, PAI2 degradation was found predominantly cell-associated and could be described empirically by the first-order, exponential decay kinetics with the best-fit degradation constant (k(d)) of 0.195 h(-1). When similarly modeled with a first-order kinetics, PAI2 synthesis in stationary-phase wild-type culture was derived to have a synthesis constant (k(s)) of 0.189 h(-1). The PAI2 concentration in batch cultivation of the rhlR(-) mutant also showed an increase-then-decrease profile. However, the maximum PAI2 concentration was about one third of that from the wild-type culture. The constitutive rate of PAI2 synthesis was therefore significantly lower than the rate attainable with active auto-induction by RhlR-PAI2 complex.