Henry Louis Rey, Spiritualism, and Creoles of Color in Nineteenth-Century New Orleans

This thesis is a biography of Henry Louis Rey (1831-1894), a member of one of New Orleans\u27 most prominent Creole of Color families. During the Civil War, Rey was a captain in both the Confederate and Union Native Guards. In postbellum years, he served as a member of the Louisiana House of Representative and in appointed city offices. Rey became heavily involved with spiritualism in the 1850s and established séance circles in New Orleans during the early 1870s. The voluminous transcripts of these séance circles have survived into the twenty-first century; however, scholarly use of these sources has been limited because most of the transcripts and all marginal annotations later written by René Grandjean are in French. The author\u27s translations of the spirit communications through their entire run reveal insight into the spiritual and material realms negotiated by New Orleans Black Creoles as they weathered declining political and economic fortunes

Henry Louis Rey, Spiritualism, and Creoles of Color in Nineteenth-Century New Orleans

This thesis is a biography of Henry Louis Rey (1831-1894), a member of one of New Orleans\u27 most prominent Creole of Color families. During the Civil War, Rey was a captain in both the Confederate and Union Native Guards. In postbellum years, he served as a member of the Louisiana House of Representative and in appointed city offices. Rey became heavily involved with spiritualism in the 1850s and established séance circles in New Orleans during the early 1870s. The voluminous transcripts of these séance circles have survived into the twenty-first century; however, scholarly use of these sources has been limited because most of the transcripts and all marginal annotations later written by René Grandjean are in French. The author\u27s translations of the spirit communications through their entire run reveal insight into the spiritual and material realms negotiated by New Orleans Black Creoles as they weathered declining political and economic fortunes

Cell cycle-dependent phosphorylation of the 77 kDa echinoderm microtubule-associated protein (EMAP) in vivo and association with the p34(cdc2) kinase

The most abundant microtubule-associated protein in sea urchin eggs and embryos is the 77 kDa echinoderm microtubule-associated protein (EMAP), EMAP localizes to the mitotic spindle as well as the interphase microtubule array and is a likely target for a cell cycle-activated kinase, To determine if EMAP is phosphorylated in vivo, sea urchin eggs and embryos were metabolically labeled with (PO4)-P-32 and a monospecific antiserum was used to immunoprecipitate EMAP from P-32-labeled eggs and embryos, In this study, we demonstrate that the 77 kDa EMAP is phosphorylated in vivo by two distinct mechanisms, In the unfertilized egg, EMAP is constitutively phosphorylated on at least five serine residues, During the first cleavage division following fertilization, EMAP is phosphorylated with a cell cycle-dependent time course, As the embryo enters mitosis, EMAP phosphorylation increases, and as the embryo exits mitosis, phosphorylation decreases, During mitosis, EMAP is phosphorylated on 10 serine residues and two-dimensional phosphopeptide mapping reveals a mitosis-specific site of phosphorylation, At all stages of the cell cycle, a 33 kDa polypeptide copurifies with the 77 kDa EMAP, regardless of phosphorylation state, Antibodies against the cdc2 kinase were used to demonstrate that the 33 kDa polypeptide is the p34(cdc2) kinase. The p34(cdc2) kinase copurifies with the mitotic apparatus and immunostaining indicates that the p34(cdc2) kinase is concentrated at the spindle poles, Models for the interaction of the p34(cdc2) kinase and the 77 kDa EMAP are presented

Zebrafish KLF4 is essential for anterior mesendoderm/pre-polster differentiation and hatching

Gene knockout studies of Kruppel-like factors (KLFs) in mice have shown essential roles in organogenesis. A screen for KLF family members in zebrafish identified many KLFs. One of these, zebrafish KLF4 (zKLF4) is the homologue of neptune, a Xenopus laevis KLF. zKLF4 is expressed from approximately 80% epiboly a patch of dorsal/anterior mesendodermal cells called the pre-polster and, subsequently, in the polster and hatching gland. Here we investigate the function of zKLF4 using morpholino-based antisense oligonucleotides. Knockdown of zKLF4 resulted in complete absence of hatching gland formation and subsequent hatching in zebrafish. In addition, there was early knockdown of expression of the pre-polster/anterior mesendoderm markers CatL, cap1, and BMP4. These results indicate zKLF4 is expressed within the pre-polster, an early mesendodermal site, and that it plays a critical role in the differentiation of these cells into hatching gland cells

Structural and Functional Consequences of the Cardiac Troponin C L48Q Ca²⁺-Sensitizing Mutation

Calcium binding to the regulatory domain of cardiac troponin C (cNTnC) causes a conformational change that exposes a hydrophobic surface to which troponin I (cTnI) binds, prompting a series of protein–protein interactions that culminate in muscle contraction. A number of cTnC variants that alter the Ca²⁺ sensitivity of the thin filament have been linked to disease. Tikunova and Davis engineered a series of cNTnC mutations that altered Ca²⁺ binding properties and studied the effects on the Ca²⁺ sensitivity of the thin filament and contraction [Tikunova, S. B., and Davis, J. P. (2004) <i>J. Biol. Chem. 279</i>, 35341–35352]. One of the mutations they engineered, the L48Q variant, resulted in a pronounced increase in the cNTnC Ca²⁺ binding affinity and Ca²⁺ sensitivity of cardiac muscle force development. In this work, we sought structural and mechanistic explanations for the increased Ca²⁺ sensitivity of contraction for the L48Q cNTnC variant, using an array of biophysical techniques. We found that the L48Q mutation enhanced binding of both Ca²⁺ and cTnI to cTnC. Nuclear magnetic resonance chemical shift and relaxation data provided evidence that the cNTnC hydrophobic core is more exposed with the L48Q variant. Molecular dynamics simulations suggest that the mutation disrupts a network of crucial hydrophobic interactions so that the closed form of cNTnC is destabilized. The findings emphasize the importance of cNTnC’s conformation in the regulation of contraction and suggest that mutations in cNTnC that alter myofilament Ca²⁺ sensitivity can do so by modulating Ca²⁺ and cTnI binding

Structural and Functional Consequences of the Cardiac Troponin C L48Q Ca²⁺-Sensitizing Mutation

Calcium binding to the regulatory domain of cardiac troponin C (cNTnC) causes a conformational change that exposes a hydrophobic surface to which troponin I (cTnI) binds, prompting a series of protein–protein interactions that culminate in muscle contraction. A number of cTnC variants that alter the Ca²⁺ sensitivity of the thin filament have been linked to disease. Tikunova and Davis engineered a series of cNTnC mutations that altered Ca²⁺ binding properties and studied the effects on the Ca²⁺ sensitivity of the thin filament and contraction [Tikunova, S. B., and Davis, J. P. (2004) <i>J. Biol. Chem. 279</i>, 35341–35352]. One of the mutations they engineered, the L48Q variant, resulted in a pronounced increase in the cNTnC Ca²⁺ binding affinity and Ca²⁺ sensitivity of cardiac muscle force development. In this work, we sought structural and mechanistic explanations for the increased Ca²⁺ sensitivity of contraction for the L48Q cNTnC variant, using an array of biophysical techniques. We found that the L48Q mutation enhanced binding of both Ca²⁺ and cTnI to cTnC. Nuclear magnetic resonance chemical shift and relaxation data provided evidence that the cNTnC hydrophobic core is more exposed with the L48Q variant. Molecular dynamics simulations suggest that the mutation disrupts a network of crucial hydrophobic interactions so that the closed form of cNTnC is destabilized. The findings emphasize the importance of cNTnC’s conformation in the regulation of contraction and suggest that mutations in cNTnC that alter myofilament Ca²⁺ sensitivity can do so by modulating Ca²⁺ and cTnI binding