On the online pharmacy, the majority of patients had commercial insurance (71%) followed by Medicaid (12%). Limitations Data from Dermatology.com are limited. Conclusions Lower-cost medications from the online pharmacy site may improve adherence and outcomes in older adults and decrease total cost associated with AK treatment. However, the online pharmacy is underutilized by this population. J Drugs Dermatol. 2020;19(4) doi10.36849/JDD.2020.4690.Background Green route biosynthesis of silver nanoparticles using Trichoderma viride (T. viride) filtrate (TVFSNPs) can serve as an alternative to antibiotics and as an effective drug delivery to combat cancer and act as an immune-stimulator. Objectives To biosynthesize silver nanoparticles (SNPs) with T. viride filtrate using green route and to characterize and determine the cytotoxic and immunomodulatory potential of nanoparticles. Material and methods Trichoderma viride filtrate was used for biosynthesizing SNPs. The biosynthesized SNPs were characterized using UV-visible spectroscopy, Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM) and energy dispersive X-ray (EDX). The cytotoxic properties against Hep‑2C and rotavirus and the immunomodulatory potential were evaluated. Results Trichoderma viride filtrate was able to bio-reduce AgNO3 to SNPs. The surface plasmon resonance peak was at 450 nm. The presence of aldehydes, amino acids, ethers, esters, carboxylic acids, hydroxyl groups, and phenol among others indicates the capping and stabilization of proteins in the nanoparticles. The nanoparticles were spherical with a size of 0.1-10.0 nm. The EDX analysis revealed a strong signal of silver (Ag). The TVFSNPs had a cytotoxic effect on Hep2C and rotavirus in a dose-dependent manner and increased the production of immunoglobulin (Ig) A (IgA) and IgM. Conclusions Trichoderma viride filtrate contained some biochemicals that can bio-reduce silver nitrate (AgNO3) for SNPs biosynthesis. The anticancer and immunostimulatory potential justifies the biomedical application and biotechnological relevance of T. viride.Aims Plectin, a universally expressed multi-functional cytolinker protein, is crucial for intermediate filament networking, including crosstalk with actomyosin and microtubules. In addition to its involvement in a number of diseases affecting skin, skeletal muscle, heart, and other stress-exposed tissues, indications for a neuropathological role of plectin have emerged. Having identified P1c as the major isoform expressed in neural tissues in previous studies, our aim for the present work was to investigate whether, and by which mechanism(s), the targeted deletion of this isoform affects neuritogenesis and proper nerve cell functioning. Methods For ex vivo phenotyping, we used dorsal root ganglion and hippocampal neurons derived from isoform P1c-deficient and plectin-null mice, complemented by in vitro experiments using purified proteins and cell fractions. VM-26 To assess the physiological significance of the phenotypic alterations observed in P1c-deficient neurons, P1c-deficient and wild-type littermate mice were subjected to standard behavioural tests. Results We demonstrate that P1c affects axonal microtubule dynamics by isoform-specific interaction with tubulin. P1c deficiency in neurons leads to altered dynamics of microtubules and excessive association with tau protein, affecting neuritogenesis, neurite branching, growth cone morphology, and translocation and directionality of movement of vesicles and mitochondria. On the organismal level, we found P1c deficiency manifesting as impaired pain sensitivity, diminished learning capabilities and reduced long-term memory of mice. Conclusions Revealing a regulatory role of plectin scaffolds in microtubule-dependent nerve cell functions, our results have potential implications for cytoskeleton-related neuropathies.Introduction One of the major neuropathological features of Alzheimer’s disease (AD) is the accumulation of amyloid-β (Aβ) protein in the brain. Evidence suggests that the low-density lipoprotein receptor-associated protein (RAP) binds strongly to Aβ and enhances its cellular uptake and that decreased RAP expression correlates with increased Aβ production in animal models of AD. Methods The current study examined whether RAP levels change in AD human brain tissue and whether they are related to the amount of AD pathology. RAP and NeuN levels were determined by Western blot, while low-density lipoprotein receptor-related protein 1 (LRP1), tau and Aβ levels were determined by ELISA in the temporal cortex of 17 AD and 16 control cases. Results An increase in total Aβ and insoluble and soluble tau protein was observed in AD brain tissue. In contrast, RAP levels were significantly decreased in AD brain tissue compared to controls. Correlation analysis revealed that levels of RAP correlated with both total Aβ and soluble and insoluble tau levels. Neither LRP1 nor NeuN levels were significantly altered in AD brain tissue homogenates and did not correlate with Aβ or tau protein levels. Conclusion Reduction in RAP may contribute to the accumulation and aggregation of Aβ in the AD brain.Human carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) are a family of receptors that mediate intercellular interactions. Pathogenic bacteria have ligands that bind CEACAMs on human cells. Neisseria gonorrhoeae (Gc) encodes numerous unique outer membrane opacity-associated (Opa) proteins that are ligands for one or more CEACAMs. CEACAMs that are expressed on epithelial cells facilitate Gc colonization, while those expressed on neutrophils affect phagocytosis and consequent intracellular survival of Gc. Since Opa protein expression is phase-variable, variations in receptor tropism affect how individual bacteria within a population interact with host cells. Here we report the development of a rapid, quantitative method for collecting and analyzing fluorescence intensity data from thousands of cells in a population using imaging flow cytometry to detect N-CEACAM bound to the surface of Opa-expressing Gc. We use this method to confirm previous findings regarding Opa-CEACAM interactions and to examine the receptor-ligand interactions of Gc expressing other Opa proteins, as well as for other N-CEACAM proteins.