Novel light delivery method for performing transbronchial photodynamic therapy ablation to treat peripheral lung cancer: A pilot study.

Background: Photodynamic therapy involves using a photosensitizer with l illumination and is recommended for treating early, centrally located lung cancers, but it is not a standard treatment for peripheral lung tumor.. We previously proposed a novel light delivery method, in which lipiodol is perfused into the bronchial tree to increase the scope of illumination via the fiber effect.

From cellular to molecular mechanobiology.

Mechanobiology at the cellular level is concerned with what phenotypes that cells exhibit to maintain homeostasis in their normal physiological mechanical environment, as well as what phenotypical changes that cells have to make when their environment is altered. Mechanobiology at the molecular level aims to understand the molecular underpinning of how cells sense, respond to, and adapt to mechanical cues in their environment. In this Perspective, we use our work inspired by and in collaboration with Professor Shu Chien as an example with which we connect the mechanobiology between the cellular and molecular levels.

Risk of Leukemia after Dengue Virus Infection: A Population-Based Cohort Study.

Background: Infections account for about 15% of human cancers globally. Although abnormal hematologic profiles and bone marrow suppression are common in patients with dengue, whether dengue is associated with a higher risk of leukemia has not been investigated.

Methods: We conducted a nationwide population-based cohort study by analyzing the National Health Insurance Research Databases in Taiwan.

Regulation of actin catch-slip bonds with a RhoA-formin module.

The dynamic turnover of the actin cytoskeleton is regulated cooperatively by force and biochemical signaling. We previously demonstrated that actin depolymerization under force is governed by catch-slip bonds mediated by force-induced K113:E195 salt-bridges. Yet, the biochemical regulation as well as the functional significance of actin catch bonds has not been elucidated.

Actin depolymerization under force is governed by lysine 113:glutamic acid 195-mediated catch-slip bonds.

As a key element in the cytoskeleton, actin filaments are highly dynamic structures that constantly sustain forces. However, the fundamental question of how force regulates actin dynamics is unclear. Using atomic force microscopy force-clamp experiments, we show that tensile force regulates G-actin/G-actin and G-actin/F-actin dissociation kinetics by prolonging bond lifetimes (catch bonds) at a low force range and by shortening bond lifetimes (slip bonds) beyond a threshold.

Structural basis and kinetics of force-induced conformational changes of an αA domain-containing integrin.

Background: Integrin α(L)β₂ (lymphocyte function-associated antigen, LFA-1) bears force upon binding to its ligand intercellular adhesion molecule 1 (ICAM-1) when a leukocyte adheres to vascular endothelium or an antigen presenting cell (APC) during immune responses. The ligand binding propensity of LFA-1 is related to its conformations, which can be regulated by force. Three conformations of the LFA-1 αA domain, determined by the position of its α₇-helix, have been suggested to correspond to three different affinity states for ligand binding.