Mexican migrant workers: Are they the image of a global village?

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Activity And Localization Of Maltodextrin Binding Site Mutants Of Glycogen Synthase In Saccharomyces Cerevisiae

Mentor: Wayne A. WilsonGlycogen is a glucose polymer formed by the enzyme glycogen synthase and is used in many organisms to store chemical energy. Saccharomyces cerevisiae (baker’s yeast) was used to study the activity and localization of glycogen synthase. Genes GSY1 and GSY2 encode glycogen synthase. GSY2 is responsible for the formation of Gsy2p, whose action accounts for ~90% of glycogen synthase activity; the remainder of total glycogen synthase activity stems from Gsy1p. Because glycogen synthase binds to glycogen, it can be used to determine glycogen localization. Glycogen synthase can appear in distinct patterns throughout the cell. Gsy2p has been shown to be regulated by phosphorylation. Phosphorylation of Gsy2p leads to inactivation of the enzyme, a decrease in glycogen storage, and a more localized pattern of glycogen synthase. Conversely, lowering the phosphorylation state of Gsy2p results in increased glycogen production and delocalization of glycogen synthase throughout the cell. Glucose-6-P (glucose-6-phosphate) activates glycogen synthase regardless of its phosphorylation state. We obtained a set of plasmids from a collaborator, encoding Gsy2p mutated at sites believed to be involved with maltodextrin binding. Maltodextrin is a chain of 20 or fewer dextrose molecules with α (1→4) glycosidic bonds. A protein sequence involved in maltodextrin binding likely would also bind to glycogen. Our task was to discover the localization pattern shown by the maltodextrin binding site mutants of glycogen synthase using a GFP tag on GSY2. The goal of this study was to determine the 16 effects of Gsy2p maltodextrin binding mutants on glycogen synthase activity, localization, and glycogen accumulation

Prevalence of the E321G MYH1 variant for immune-mediated myositis and nonexertional rhabdomyolysis in performance subgroups of American Quarter Horses.

BackgroundImmune-mediated myositis (IMM) in American Quarter Horses (QHs) causes acute muscle atrophy and lymphocytic infiltration of myofibers. Recently, an E321G mutation in a highly conserved region of the myosin heavy chain 1 (MYH1) gene was associated with susceptibility to IMM and nonexertional rhabdomyolysis.ObjectivesTo estimate prevalence of the E321G MYH1 variant in the QH breed and performance subgroups.AnimalsThree-hundred seven elite performance QHs and 146 random registered QH controls.MethodsProspective genetic survey. Elite QHs from barrel racing, cutting, halter, racing, reining, Western Pleasure, and working cow disciplines and randomly selected registered QHs were genotyped for the E321G MYH1 variant and allele frequencies were calculated.ResultsThe E321G MYH1 variant allele frequency was 0.034 ± 0.011 in the general QH population (6.8% of individuals in the breed) and the highest among the reining (0.135 ± 0.040; 24.3% of reiners), working cow (0.085 ± 0.031), and halter (0.080 ± 0.027) performance subgroups. The E321G MYH1 variant was present in cutting (0.044 ± 0.022) and Western Pleasure (0.021 ± 0.015) QHs at lower frequency and was not observed in barrel racing or racing QHs.Conclusions and clinical importanceKnowing that reining and working cow QHs have the highest prevalence of the E321G MYH1 variant and that the variant is more prevalent than the alleles for hereditary equine regional dermal asthenia and hyperkalemic periodic paralysis in the general QH population will guide the use of genetic testing for diagnostic and breeding purposes

The North American Spa Industry: An Examination of Emergent Trends

The spa industry is rapidly growing, both in North America and around the globe. However, hospitality and tourism professionals seem to be surprised and unprepared of the impressive evolution. The authors report of the North American spa industry’s current practices and emergent trends that are likely to prove significant for spa stakeholders and educators in this growing field of inquiry

Occupational vision care program: Eyecare for the coal mining industry

Occupational vision care program: Eyecare for the coal mining industr