Methyl-sulfonyl-methane (MSM)-induced acute angle closure.

Purpose: To report the first case of presumed bilateral acute angle closure (AAC) secondary to ingestion of the dietary supplement, methyl-sulfonyl-methane (MSM).

Patient: A 35-year-old woman presented with bilateral AAC 1 week after starting multiple dietary supplements, one of which contained MSM. Ultrasound biomicroscopy demonstrated bilateral anterior rotation of the iris-lens diaphragm, ciliary body edema, and choroidal effusion.

Phenotypic assays for β-amyloid in mouse embryonic stem cell-derived neurons.

Given the complex nature of Alzheimer's disease (AD), a cell-based model that recapitulates the physiological properties of the target neuronal population would be extremely valuable for discovering improved drug candidates and chemical probes to uncover disease mechanisms. We established phenotypic neuronal assays for the biogenesis and synaptic action of amyloid β peptide (Aβ) based on embryonic stem cell-derived neurons (ESNs). ESNs enriched with pyramidal neurons were robust, scalable, and amenable to a small-molecule screening assay, overcoming the apparent limitations of neuronal models derived from human pluripotent cells.

Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing.

The beta-site APP cleaving enzyme-1 (BACE1) mediates the first cleavage of the beta-amyloid precursor protein (APP) to yield the amyloid beta-peptide (Abeta), a key pathogenic agent in Alzheimer's disease (AD). Using a proteomic approach based on in-cell chemical cross-linking and tandem affinity purification (TAP), we herein identify sorting nexin 6 (SNX6) as a BACE1-associated protein. SNX6, a PX domain protein, is a putative component of retromer, a multiprotein cargo complex that mediates the retrograde trafficking of the cation-independent mannose-6-phosphate receptor (CI-MPR) and sortilin.

Two tarantula peptides inhibit activation of multiple sodium channels.

Two peptides, ProTx-I and ProTx-II, from the venom of the tarantula Thrixopelma pruriens, have been isolated and characterized. These peptides were purified on the basis of their ability to reversibly inhibit the tetrodotoxin-resistant Na channel, Na(V) 1.8, and are shown to belong to the inhibitory cystine knot (ICK) family of peptide toxins interacting with voltage-gated ion channels.