Nervous regulation: beta-2-adrenergic signaling in immune homeostasis, cancer immunotherapy, and autoimmune diseases.

Beta-2-adrenergic receptor (ß2-AR) mediates neural signaling from the sympathetic nervous system (SNS) to the immune system to modulate immunogenic and immunosuppressive responses for maintaining immune homeostasis. ß2-AR regulates various cellular activities on the innate and adaptive immune cells through differential signaling to modulate activation, proliferation, differentiation, and cytokine production. This signaling pathway has been found to be critical for regulating anti-tumor immune responses and autoimmune responses. Recently, ß2-AR has also been implicated in the mobilization of immune cells in peripheral blood and ex-vivo expansion of cytotoxic T cells from donor blood that has clinical implications for improving cancer immunotherapy. This review attempts to provide a comprehensive overview of the established and emerging roles of ß2-AR signaling in immune homeostasis, cancer immunotherapy, and autoimmune diseases.

Optimization of western blotting for the detection of proteins of different molecular weight.

Protein samples electroblotted onto nitrocellulose membranes and quenched with a mixture of blocking agents produced a strong signal for cystic fibrosis transmembrane-conductance regulator (CFTR), a high-molecular-weight protein, in western blotting. Optimized conditions for CFTR were then extended to medium- and low-molecular-weight proteins (LAMP1 and Rab11a, respectively) to determine the effects of methanol concentration (0-20%) in Towbin's transfer buffer (TTB). Methanol in TTB appears to have little to no effect on CFTR signal. However, for medium-sized (LAMP1) and small (Rab11a) proteins, a lower concentration of methanol (10%) was sufficient to produce a maximal signal. Therefore, methanol, a toxic solvent, can be removed from or reduced in TTB without compromising signal strength. Here, we show modifications that may be useful in detecting and/or improving the signal of low-abundance proteins.