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Hippocampal neurogenesis in the SERT ALA56 mouse model to autism
Title
Hippocampal neurogenesis in the SERT ALA56 mouse model to autism.
Creator
Di Mase, Julieta Maria, Guthrie, Kathleen, Florida Atlantic University, Charles E. Schmidt College of Science, Department of Biological Sciences
Abstract/Description
The causes of autism spectrum disorder (ASD) are not all known, but it is suspected that the serotonin transporter (SERT) plays an important role for some subjects with ASD. Mutations in the SLC6A4 gene, that encodes SERT, including the Ala56 mutation (Gly56Ala), have been found in some autism patients. This mutation makes the transporter more active and reduces the probability of serotonergic neurotransmission in the brain, which is linked to behavioral changes that are associated with core...
Show moreThe causes of autism spectrum disorder (ASD) are not all known, but it is suspected that the serotonin transporter (SERT) plays an important role for some subjects with ASD. Mutations in the SLC6A4 gene, that encodes SERT, including the Ala56 mutation (Gly56Ala), have been found in some autism patients. This mutation makes the transporter more active and reduces the probability of serotonergic neurotransmission in the brain, which is linked to behavioral changes that are associated with core domain deficits of ASD 1. Depression also has been linked to decreases in the availability of serotonin (5-hydroxytryptamine; 5-HT) in the central nervous system (CNS), and is associated with reduced hippocampal neurogenesis. Selective serotonin reuptake inhibitors (SSRIs), drugs used to block SERTs, are used to treat depression and/or anxiety by inhibiting SERT to increase synaptic 5-HT levels.
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Date Issued
2019
PURL
http://purl.flvc.org/fau/fd/FA00013297
Subject Headings
Autism Spectrum Disorder, Hippocampus, Neurogenesis, Serotonin Plasma Membrane Transport Proteins
Format
Document (PDF)
INSIG2 gene polymorphism is associated with increased subcutaneous fat in women and poor response to resistance training in men
Title
INSIG2 gene polymorphism is associated with increased subcutaneous fat in women and poor response to resistance training in men.
Creator
Orkunoglu-Suer, Funda E., Gordish-Dressman, Heather, Clarkson, Priscilla M., Thompson, Paul D., Angelopoulos, Theodore J., Gordon, Paul M., Moyna, Niall M., Pescatello, Linda S., Visich, Paul S., Zoeller, Robert F., Harmon, Brennan, Seip, Richard L., Hoffman, Eric P., Devaney, Joseph M.
Date Issued
2008-12-23
PURL
http://purl.flvc.org/fcla/dt/3327172
Subject Headings
Adiposity --genetics, Alleles, Gene Frequency, Intracellular Signaling Peptides and Proteins, Resistance Training, Subcutaneous Fat, INSIG2 protein, Obesity, Genotype, Membrane Proteins, Membrane Proteins --Genetics
Format
Document (PDF)
Investigation of talin head-tail interactions
Title
Investigation of talin head-tail interactions.
Creator
Butyn, Amber., Harriet L. Wilkes Honors College
Abstract/Description
Talin is a ubiquitous, high-molecular-weight, flexible protein that plays a critical role in focal adhesions by activating, as well as connecting, integrins to the actin cytoskeleton. Talin's inactive auto-inhibitory state is speculated to be one of its modes of regulation inside the cell and is achieved through its head-tail interactions. In order to decipher the stability of this interaction, the head domain (residues 206-405) was cloned into a modified pET28m vector while the tail domains ...
Show moreTalin is a ubiquitous, high-molecular-weight, flexible protein that plays a critical role in focal adhesions by activating, as well as connecting, integrins to the actin cytoskeleton. Talin's inactive auto-inhibitory state is speculated to be one of its modes of regulation inside the cell and is achieved through its head-tail interactions. In order to decipher the stability of this interaction, the head domain (residues 206-405) was cloned into a modified pET28m vector while the tail domains (residues 1654-2344 and 2225-2344) were cloned into the pET32a vector to obtain octa-histidine tagged and un-tagged peptide, respectively. Neither co-expression nor pull-down using the His-tagged head domain was successful in purifying a stable head-tail complex. Our results indicate rather weak interactions between the talin head and rod domains and hence, under our experimental conditions, do not lead to a stable auto-inhibitory complex that can be purified for further studies.
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Date Issued
2009
PURL
http://purl.flvc.org/FAU/209984
Subject Headings
Membrane proteins, Structure-activity relationships, Cell membranes, Physiology, Molecular biology, Cell interaction, Developmental cytology
Format
Document (PDF)
Purification and characterization of two members of the protein tyrosine phosphatase family
Title
Purification and characterization of two members of the protein tyrosine phosphatase family: dual specificity phosphatase PVP and low molecular weight phosphatase WZB.
Creator
Livingston, Paula A., Charles E. Schmidt College of Science, Department of Chemistry and Biochemistry
Abstract/Description
Two protein tyrosine phosphatases, dual specificity phosphatase PVP and low molecular weight phosphatase WZB were purified and characterized. PVP was expressed as inclusion bodies and a suitable purification and refolding method was devised. Enzyme kinetics revealed that p-nitrophenylphosphate and (Sb(B-naphthyl phosphate were substrates with KM of 4.0mM and 8.1mM respectively. PVP showed no reactivity towards phosphoserine. Kinetic characterization of WZB showed that only...
Show moreTwo protein tyrosine phosphatases, dual specificity phosphatase PVP and low molecular weight phosphatase WZB were purified and characterized. PVP was expressed as inclusion bodies and a suitable purification and refolding method was devised. Enzyme kinetics revealed that p-nitrophenylphosphate and (Sb(B-naphthyl phosphate were substrates with KM of 4.0mM and 8.1mM respectively. PVP showed no reactivity towards phosphoserine. Kinetic characterization of WZB showed that only pnitrophenylphosphate was a substrate with no affinity for Ç-naphthyl phosphate and phosphoserine. Optimal conditions for activity with PNPP were found at a pH of 5 with a KM of 1.1mM, kcat of 35.4s-1 and kcat/KM of 32.2s-1mM-1. Inhibition studies showed that phosphate, fluoride, and molybdate were competitive inhibitors with Ki of 3.2mM, 71.7mM, and 50.4(So(BM respectively and hydrogen peroxide abolished activity. Active site mutants of WZB Cys9Ser and Asp115Asn showed no activity.
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Date Issued
2009
PURL
http://purl.flvc.org/FAU/332911
Subject Headings
Protein-tyrosine phosphatase, Cellular signal transduction, Cell cycle, Regulation, Membrane proteins, Structure-activity relationships, Protein kinases
Format
Document (PDF)
Characterization of RNase in Mycoplasma genitalium and study of its possible role in tRNA processing
Title
Characterization of RNase in Mycoplasma genitalium and study of its possible role in tRNA processing.
Creator
Lalonde, Maureen S., Florida Atlantic University, Li, Zhongwei, Charles E. Schmidt College of Medicine, Department of Biomedical Science
Abstract/Description
Exoribonucleases degrade RNA and are important in RNA metabolism and gene expression. Mycoplasma genitalium, a bacterium with the smallest genome known, has only one identified exoribonuclease, RNase R (MgR). In this work RNA degradation properties of purified MgR were examined. As observed in Escherichia coli RNase R (EcR) studies, MgR degrades poly(A), rRNA, and oligoribonucleotides in 3'--->5' direction, though its substrate specificity and optimal activity requirements vary. Interestingly...
Show moreExoribonucleases degrade RNA and are important in RNA metabolism and gene expression. Mycoplasma genitalium, a bacterium with the smallest genome known, has only one identified exoribonuclease, RNase R (MgR). In this work RNA degradation properties of purified MgR were examined. As observed in Escherichia coli RNase R (EcR) studies, MgR degrades poly(A), rRNA, and oligoribonucleotides in 3'--->5' direction, though its substrate specificity and optimal activity requirements vary. Interestingly, MgR is sensitive to 2-O-methylation stopping downstream of such modifications in native rRNA and synthetic oligoribonucleotides. MgR removes the 3' trailer sequence from a tRNA precursor of M. genitalium and generates products equal to the mature tRNA, demonstrating a role of MgR in tRNA maturation. The 3' terminal CCA sequence and the acceptor stem of tRNA play a role in determining the formation of such products by MgR. These results suggest multiple functions of RNase R in RNA metabolism in Mycoplasma.
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Date Issued
2006
PURL
http://purl.flvc.org/fcla/dt/13317
Subject Headings
Gene expression, RNA-protein interactions, Cellular control mechanisms, Ribonucleases--Analysis, Cell membranes
Format
Document (PDF)