{"id":{"repo_id":"texas-state","oai_identifier":"oai:digital.library.txst.edu:10877/5478"},"canonical_url":"https://search.dev.ndltd.org/etd/texas-state/oai:digital.library.txst.edu:10877/5478","repository":{"repo_id":"texas-state","name":"Texas State University","base_url":"https://digital.library.txst.edu/server/oai/request"},"display":{"title":"Identification of Residues Critical to Epithelial Sodium Channel Assembly","abstract":"The Epithelial Sodium Channel (ENaC) is a major determinant in fine-tuning the volume and pressure of blood within the cardiovascular system. Understanding the regulation, structural assembly, and arrangement of ENaC is needed. This study describes a method for identifying residues that participate in structural stability interactions between and within subunits as well as those critical to function. A novel yeast screen was used to describe salt-sensitive phenotypes observed in S. cerevisiae that express ENaC and show growth inhibition. Error prone polymerase chain reaction (EP-PCR) was employed to promote random mutagenesis in the extracellular loop of alpha-ENaC. The levels of growth inhibition were monitored in the yeast strain S1InsE4A and subsequently characterized. The location of the point mutations and the corresponding amino acid transitions cause varying degrees of function. This study successfully illustrates a method for inducing mutations in areas of interest in the gene and screening the resulting mutants. We also identify several mutations of the extracellular domain of alpha ENaC which are critical to function.","abstract_html":"The Epithelial Sodium Channel (ENaC) is a major determinant in fine-tuning the volume and pressure of blood within the cardiovascular system. Understanding the regulation, structural assembly, and arrangement of ENaC is needed. This study describes a method for identifying residues that participate in structural stability interactions between and within subunits as well as those critical to function. A novel yeast screen was used to describe salt-sensitive phenotypes observed in S. cerevisiae that express ENaC and show growth inhibition. Error prone polymerase chain reaction (EP-PCR) was employed to promote random mutagenesis in the extracellular loop of alpha-ENaC. The levels of growth inhibition were monitored in the yeast strain S1InsE4A and subsequently characterized. The location of the point mutations and the corresponding amino acid transitions cause varying degrees of function. This study successfully illustrates a method for inducing mutations in areas of interest in the gene and screening the resulting mutants. We also identify several mutations of the extracellular domain of alpha ENaC which are critical to function.","abstract_has_math":false,"creators":["Whisenant, Ty E."],"institution":"Texas State University-San Marcos","degree_name":"Master of Science","degree_level":"Masters","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":["Booth, Rachell Eschette"],"committee_chairs":[],"committee_members":["David, Wendi M.","Watkins, Linette"],"year":2011,"date_issued":"2011-08","date_published":"2011-08","updated_at":"2026-07-27T21:22:51Z","subjects":["ENaC","sodium ion channel","sodium reabsorption"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/10877/5478","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Booth, Rachell Eschette"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["David, Wendi M.","Watkins, Linette"]},{"key":"dc:creator","label":"Author","values":["Whisenant, Ty E."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2015-04-06T17:38:24Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2015-04-06T17:38:24Z"]},{"key":"dc:date.issued","label":"Date","values":["2011-08"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Texas State University-San Marcos"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["ENaC","sodium ion channel","sodium reabsorption"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/10877/5478"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The Epithelial Sodium Channel (ENaC) is a major determinant in fine-tuning the volume and pressure of blood within the cardiovascular system. Understanding the regulation, structural assembly, and arrangement of ENaC is needed. This study describes a method for identifying residues that participate in structural stability interactions between and within subunits as well as those critical to function. A novel yeast screen was used to describe salt-sensitive phenotypes observed in S. cerevisiae that express ENaC and show growth inhibition. Error prone polymerase chain reaction (EP-PCR) was employed to promote random mutagenesis in the extracellular loop of alpha-ENaC. The levels of growth inhibition were monitored in the yeast strain S1InsE4A and subsequently characterized. The location of the point mutations and the corresponding amino acid transitions cause varying degrees of function. This study successfully illustrates a method for inducing mutations in areas of interest in the gene and screening the resulting mutants. We also identify several mutations of the extracellular domain of alpha ENaC which are critical to function."]},{"key":"dc:format","label":"Dc Format","values":["Text"]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["1 file (.pdf)"]},{"key":"dc:title","label":"Title","values":["Identification of Residues Critical to Epithelial Sodium Channel Assembly"]}]}],"canonical_facts":{"dc:contributor.advisor":["Booth, Rachell Eschette"],"dc:contributor.committeemember":["David, Wendi M.","Watkins, Linette"],"dc:creator":["Whisenant, Ty E."],"dc:date.accessioned":["2015-04-06T17:38:24Z"],"dc:date.available":["2015-04-06T17:38:24Z"],"dc:date.issued":["2011-08"],"dc:description.abstract":["The Epithelial Sodium Channel (ENaC) is a major determinant in fine-tuning the volume and pressure of blood within the cardiovascular system. Understanding the regulation, structural assembly, and arrangement of ENaC is needed. This study describes a method for identifying residues that participate in structural stability interactions between and within subunits as well as those critical to function. A novel yeast screen was used to describe salt-sensitive phenotypes observed in S. cerevisiae that express ENaC and show growth inhibition. Error prone polymerase chain reaction (EP-PCR) was employed to promote random mutagenesis in the extracellular loop of alpha-ENaC. The levels of growth inhibition were monitored in the yeast strain S1InsE4A and subsequently characterized. The location of the point mutations and the corresponding amino acid transitions cause varying degrees of function. This study successfully illustrates a method for inducing mutations in areas of interest in the gene and screening the resulting mutants. We also identify several mutations of the extracellular domain of alpha ENaC which are critical to function."],"dc:format":["Text"],"dc:format.medium":["1 file (.pdf)"],"dc:identifier.uri":["https://hdl.handle.net/10877/5478"],"dc:language.iso":["en"],"dc:subject":["ENaC","sodium ion channel","sodium reabsorption"],"dc:title":["Identification of Residues Critical to Epithelial Sodium Channel Assembly"],"dc:type":["Thesis"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Texas State University-San Marcos"]},"updated_at":"2026-07-27T21:22:51Z"}