Joyas valencianas : [ monumentos y edificios notables.: Año 1924

Microfilme.. Valencia: BV, ca. 1990.

Margaret Bush Wilson

Margaret Bush Wilson was a woman of highly exceptional stature. Bush accomplished much in her life; the most prominent being the first female on the N.A.A.C.P. national board of Directors. Much of her career consisted of civil rights and urban development. Before Mrs. Bush focused on her civil rights path, she was valedictorian of her graduating high school class. After completing her high school career, she began to study abroad, traveling to over six countries. These included: England, France, Ceylon, Japan, the Hawaiian Islands and her most extraordinary visit to India. Here Margaret met and spoke with Mahatma Gandhi which fueled her passion of the civil rights movement in the United States. Mrs. Bush pursued a law degree at Lincoln University Law School after completing her Bachelor’s at Talladega University. On top of her extraordinary accomplishments, Margaret Bush possessed the unique quality of appearing 10 years younger than her real age, reflecting her strong spirit and compassion towards humanity.

Yvonne D. Stark - Wilson

Yvonne Wilson is a woman of achievement, accomplishment, and ambition. It all started when she enrolled in Lincoln University; the only public institution for higher education in Missouri that admitted African Americans. She later went on to become a teacher, principal and systems director in the Kansas City School District. Mrs. Wilson was involved in many civic/social activities including the Metropolitan Community Colleges and the Bruce Watkins Cultural Heritage Center. She had many accomplishments including her positions as the President of Lincoln University Board of Curators and the first African American President of the Missouri Association of Elementary School Principals. Finally, one of her top accomplishments was being appointed to the Missouri House of Representatives.

Wendell Berry's Critique of E. O. Wilson on Science

Drawing on the work of Wendell Berry, among others, allows us to see through claims that science has on limits (scientism). Berry shows what follies scientism generates and provides his own guidelines to what the limits of science are or ought to be.

1924 Lincoln University Yearbook

Yearbook of Lincoln Institute and its later name Lincoln University (Jefferson City, Mo.) for the academic year 1923-1924.

Public Religion and Secularization in England : Defending Bryan Wilson

Peer reviewed

Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis

The delivery of copper to specific sites within the cell is mediated by distinct intracellular carrier proteins termed copper chaperones. Previous studies in Saccharomyces cerevisiae suggested that the human copper chaperone HAH1 may play a role in copper trafficking to the secretory pathway of the cell. In this current study, HAH1 was detected in lysates from multiple human cell lines and tissues as a single-chain protein distributed throughout the cytoplasm and nucleus. Studies with a glutathione S-transferase-HAH1 fusion protein demonstrated direct protein–protein interaction between HAH1 and the Wilson disease protein, which required the cysteine copper ligands in the amino terminus of HAH1. Consistent with these in vitro observations, coimmunoprecipitation experiments revealed that HAH1 interacts with both the Wilson and Menkes proteins in vivo and that this interaction depends on available copper. When these studies were repeated utilizing three disease-associated mutations in the amino terminus of the Wilson protein, a marked diminution in HAH1 interaction was observed, suggesting that impaired copper delivery by HAH1 constitutes the molecular basis of Wilson disease in patients harboring these mutations. Taken together, these data provide a mechanism for the function of HAH1 as a copper chaperone in mammalian cells and demonstrate that this protein is essential for copper homeostasis.

Categorias objetais : localização ôntica do objeto jurídico / José Wilson Ferreira Sobrinho. --

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Functional expression of the Wilson disease protein reveals mislocalization and impaired copper-dependent trafficking of the common H1069Q mutation

Wilson disease is an autosomal recessive disorder of hepatic copper metabolism caused by mutations in a gene encoding a copper-transporting P-type ATPase. To elucidate the function of the Wilson protein, wild-type and mutant Wilson cDNAs were expressed in a Menkes copper transporter-deficient mottled fibroblast cell line defective in copper export. Expression of the wild-type cDNA demonstrated trans-Golgi network localization and copper-dependent trafficking of the Wilson protein identical to previous observations for the endogenously expressed protein in hepatocytes. Furthermore, expression of the Wilson cDNA rescued the mottled phenotype as evidenced by a reduction in copper accumulation and restoration of cell viability. In contrast, expression of an H1069Q mutant Wilson cDNA did not rescue the mottled phenotype, and immunofluorescence studies showed that this mutant Wilson protein was localized in the endoplasmic reticulum. Consistent with these findings, pulse–chase analysis demonstrated a 5-fold decrease in the half-life of the H1069Q mutant as compared with the wild-type protein. Maintenance of these transfected cell lines at 28°C resulted in localization of the H1069Q protein in the trans-Golgi network, suggesting that a temperature-sensitive defect in protein folding followed by degradation constitutes the molecular basis of Wilson disease in patients harboring the H1069Q mutation. Taken together, these studies describe a tractable expression system for elucidating the function and localization of the copper-transporting ATPases in mammalian cells and provide compelling evidence that the Wilson protein can functionally substitute for the Menkes protein, supporting the concept that these proteins use common biochemical mechanisms to effect cellular copper homeostasis.

The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake.

The CCC2 gene of the yeast Saccharomyces cerevisiae is homologous to the human genes defective in Wilson disease and Menkes disease. A biochemical hallmark of these diseases is a deficiency of copper in ceruloplasmin and other copper proteins found in extracytosolic compartments. Here we demonstrate that disruption of the yeast CCC2 gene results in defects in respiration and iron uptake. These defects could be reversed by supplementing cells with copper, suggesting that CCC2 mutant cells were copper deficient. However, cytosolic copper levels and copper uptake were normal. Instead, CCC2 mutant cells lacked a copper-dependent oxidase activity associated with the extracytosolic domain of the FET3-encoded protein, a ceruloplasmin homologue previously shown to be necessary for high-affinity iron uptake in yeast. Copper restored oxidase activity both in vitro and in vivo, paralleling the ability of copper to restore respiration and iron uptake. These results suggest that the CCC2-encoded protein is required for the export of copper from the cytosol into an extracytosolic compartment, supporting the proposal that intracellular copper transport is impaired in Wilson disease and Menkes disease.