Correction of a genetic deficiency in pantothenate kinase 1 using phosphopantothenate replacement therapy.

Coenzyme A (CoA) is a ubiquitous cofactor involved in numerous essential biochemical transformations, and along with its thioesters is a key regulator of intermediary metabolism. Pantothenate (vitamin B5) phosphorylation by pantothenate kinase (PanK) is thought to control the rate of CoA production. Pantothenate kinase associated neurodegeneration is a hereditary disease that arises from mutations that inactivate the human PANK2 gene.

Physiological roles of the pantothenate kinases.

CoA (coenzyme A) is an essential cofactor that is involved in many metabolic processes. CoA is derived from pantothenate in five biosynthetic reactions. The CoA biosynthetic pathway is regulated by PanKs (pantothenate kinases) and four active isoforms are expressed in mammals.

Objective measures of the effects of the "Read Without Glasses Method".

Purpose: The Read Without Glasses Method is a home-based vision training program designed to "avoid, eliminate, or reduce the need for bifocals" in presbyopic patients with 6 minutes of daily vision exercises. The purpose of this study was to objectively measure changes in accommodation and near unaided visual acuity (VA) in emmetropic presbyopes using this program.

Methods: Eight emmetropic presbyopes between 50 and 65 years of age participated in 2 pretreatment and 2 post-treatment visits.

Cytokine secretion requires phosphatidylcholine synthesis.

Choline cytidylyltransferase (CCT) is the rate-limiting enzyme in the phosphatidylcholine biosynthetic pathway. Here, we demonstrate that CCT alpha-mediated phosphatidylcholine synthesis is required to maintain normal Golgi structure and function as well as cytokine secretion from the Golgi complex. CCT alpha is localized to the trans-Golgi region and its expression is increased in lipopolysaccharide (LPS)-stimulated wild-type macrophages.

Role of amino acid residues in transmembrane segments IS6 and IIS6 of the Na+ channel alpha subunit in voltage-dependent gating and drug block.

Alanine-scanning mutagenesis of transmembrane segments IS6 and IIS6 of the rat brain Na(v)1.2 channel alpha subunit identified mutations N418A in IS6 and L975A in IIS6 as causing strong positive shifts in the voltage dependence of activation. In contrast, mutations V424A in IS6 and L983A in IIS6 caused strong negative shifts.