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Human Coronary Artery Smooth Muscle Cell Responses to Bioactive Polyelectrolyte Multilayer Interfaces
Title
Human Coronary Artery Smooth Muscle Cell Responses to Bioactive Polyelectrolyte Multilayer Interfaces.
Creator
Newcomer, Robert, Moussallem, Maroun, Keller, Thomas C. S., Schlenoff, Joseph B., Sang, Qing-Xiang
Abstract/Description
Under normal physiological conditions, mature human coronary artery smooth muscle cells (hCASMCs) exhibit a "contractile" phenotype marked by low rates of proliferation and protein synthesis, but these cells possess the remarkable ability to dedifferentiate into a "synthetic" phenotype when stimulated by conditions of pathologic stress. A variety of polyelectrolyte multilayer (PEMU) films are shown here to exhibit bioactive properties that induce distinct responses from cultured hCASMCs....
Show moreUnder normal physiological conditions, mature human coronary artery smooth muscle cells (hCASMCs) exhibit a "contractile" phenotype marked by low rates of proliferation and protein synthesis, but these cells possess the remarkable ability to dedifferentiate into a "synthetic" phenotype when stimulated by conditions of pathologic stress. A variety of polyelectrolyte multilayer (PEMU) films are shown here to exhibit bioactive properties that induce distinct responses from cultured hCASMCs. Surfaces terminated with Nafion or poly(styrenesulfonic acid) (PSS) induce changes in the expression and organization of intracellular proteins, while a hydrophilic, zwitterionic copolymer of acrylic acid and 3-[2-(acrylamido)-ethyl dimethylammonio] propane sulfonate (PAA-co-PAEDAPS) is resistant to cell attachment and suppresses the formation of key cytoskeletal components. Differential expression of heat shock protein 90 and actin is observed, in terms of both their magnitude and cellular localization, and distinct cytoplasmic patterns of vimentin are seen. The ionophore A23187 induces contraction in confluent hCASMC cultures on Nafion-terminated surfaces. These results demonstrate that PEMU coatings exert direct effects on the cytoskeletal organization of attaching hCASMCs, impeding growth in some cases, inducing changes consistent with phenotypic modulation in others, and suggesting potential utility for PEMU surfaces as a coating for coronary artery stents and other implantable medical devices.
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Date Issued
2011
Identifier
FSU_migr_chm_faculty_publications-0011, 10.4061/2011/854068
Format
Citation
Utilization of a Diazene Core to Target Sulfinic Acid
Title
Utilization of a Diazene Core to Target Sulfinic Acid.
Creator
Morgan, Lexi, Department of Biochemistry
Abstract/Description
Hydrogen peroxide (H2O2) regulates an array of physiological functions and acts as a second messenger at low levels. However, the elevation of these levels can lead to oxidative stress, a state that is implicated in the progression of human diseases, such as cancer and Parkinson's disease. Cysteine is highly susceptible to oxidation from hydrogen peroxide because of the nucleophilicity of the thiol group (R-SH) to form sulfenic acid (RSOH). The thiol group can be further oxidized to form...
Show moreHydrogen peroxide (H2O2) regulates an array of physiological functions and acts as a second messenger at low levels. However, the elevation of these levels can lead to oxidative stress, a state that is implicated in the progression of human diseases, such as cancer and Parkinson's disease. Cysteine is highly susceptible to oxidation from hydrogen peroxide because of the nucleophilicity of the thiol group (R-SH) to form sulfenic acid (RSOH). The thiol group can be further oxidized to form sulfinic acid (RSO2H) and sulfonic acid (RSO3H). Each of these species exhibits unique chemical properties as well as a versatile mechanism to alter protein function. While the regulatory function of sulfenic has been widely studied, very little is known about the role sulfinic acid plays. Mounting evidence suggests that the cysteine sulfinic acid is more regulated than once thought. An enzyme called sulfiredoxin was found to reduce the sulfinic form of certain peroxiredoxins. The discovery of a sulfinic acid reductase suggests a more fundamental role for this modification, thus the proposal of the "sulfinic acid switch" in regard to the protein regulation by hydrogen peroxide. At The Scripps Research Institute, Dr. Kate Carroll's goal is to monitor the oxidation of cysteine through the utilization of novel probes. This project focused on the utilization of a diazene core (R-N=N-R) with a variety of functional groups in order to target sulfinic acid. This electrophilic nitrogen-containing species acts as a specific reagent to target the nucleophilic sulfinic acid. This selective ligation reaction with sulfinic acids has potential utility for detections of oxidative modifications, as well as regulations, in biological systems.
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Date Issued
2013
Identifier
FSU_migr_undergradresearch-0010
Format
Citation
δ/ω-Plectoxin-Pt1a
Title
δ/ω-Plectoxin-Pt1a: An Excitatory Spider Toxin with Actions on both Ca(2+) and Na(+) Channels.
Creator
Zhou, Yi, Zhao, Mingli, Fields, Gregg B., Wu, Chun-Fang, Branton, W.
Abstract/Description
The venom of spider Plectreurys tristis contains a variety of peptide toxins that selectively target neuronal ion channels. O-palmitoylation of a threonine or serine residue, along with a characteristic and highly constrained disulfide bond structure, are hallmarks of a family of toxins found in this venom. Here, we report the isolation and characterization of a new toxin, δ/ω-plectoxin-Pt1a, from this spider venom. It is a 40 amino acid peptide containing an O-palmitoylated Ser-39. Analysis...
Show moreThe venom of spider Plectreurys tristis contains a variety of peptide toxins that selectively target neuronal ion channels. O-palmitoylation of a threonine or serine residue, along with a characteristic and highly constrained disulfide bond structure, are hallmarks of a family of toxins found in this venom. Here, we report the isolation and characterization of a new toxin, δ/ω-plectoxin-Pt1a, from this spider venom. It is a 40 amino acid peptide containing an O-palmitoylated Ser-39. Analysis of δ/ω-plectoxin-Pt1a cDNA reveals a small precursor containing a secretion signal sequence, a 14 amino acid N-terminal propeptide, and a C-terminal amidation signal. The biological activity of δ/ω-plectoxin-Pt1a is also unique. It preferentially blocks a subset of Ca(2+) channels that is apparently not required for neurotransmitter release; decreases threshold for Na(+) channel activation; and slows Na(+) channel inactivation. As δ/ω-plectoxin-Pt1a enhances synaptic transmission by prolonging presynaptic release of neurotransmitter, its effects on Na(+) and Ca(2+) channels may act synergistically to sustain the terminal excitability.
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Date Issued
2013
Identifier
FSU_migr_biomed_faculty_publications-0044
Format
Citation