• Login
    View Item 
    •   Home
    • UA Graduate and Undergraduate Research
    • UA Theses and Dissertations
    • Dissertations
    • View Item
    •   Home
    • UA Graduate and Undergraduate Research
    • UA Theses and Dissertations
    • Dissertations
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of UA Campus RepositoryCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournalThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsPublisherJournal

    My Account

    LoginRegister

    About

    AboutUA Faculty PublicationsUA DissertationsUA Master's ThesesUA Honors ThesesUA PressUA YearbooksUA CatalogsUA Libraries

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Pharmacological and molecular heterogeneity of the "peripheral-type benzodiazepine receptor"

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    azu_td_9103046_sip1_c.pdf
    Size:
    7.996Mb
    Format:
    PDF
    Download
    Author
    Parola, Anthony Lawrence.
    Issue Date
    1990
    Keywords
    Biology.
    Advisor
    Laird III., Hugh E.
    
    Metadata
    Show full item record
    Publisher
    The University of Arizona.
    Rights
    Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
    Abstract
    The rat liver peripheral-type benzodiazepine receptor (PBR) was characterized by ligand binding with [³H]Ro5-4864 and by photolabeling using [³H]PK 14105. The native liver receptor could be solubilized with digitonin. The Mr of the native photolabeled receptor was 170 kDa while a single Mr 19 kDa protein was identified under denaturing conditions. Radioligand binding to rat liver subcellular fractions showed protoporphyrin IX had a 6.2-fold greater affinity for [³H]Ro5-4864 binding sites in mitochondria than in microsomes. Although heterogeneity of the rat liver benzodiazepine binding site, but not the isoquinoline binding site, was observed, a single 19 kDa protein band was identified by photolabeling with an isoquinoline ligand. Bovine and rat PBR have a similar tissue and subcellular distribution, but are pharmacologically and biochemically distinct. The bovine PBR had low affinity for Ro5-4864 and diazepam while [³H]PK 11195 binding was insensitive to modification of histidine residues. The native Mr the receptor was 200 kDa by gel filtration. Photolabeling identified a 17 kDa protein from both rat and bovine adrenal mitochondria under denaturing conditions. An affinity matrix was constructed to purify the native components of the PBR from both species, but the PBR could not be eluted from the matrix. To compare receptor components, the cDNA encoding the rat isoquinoline binding protein was used to screen a fetal calf adrenal cDNA library. A 822 base pair bovine cDNA was identified that encoded a polypeptide of 169 amino acids which had 78% positional identity to the rat protein and was 97% similar after accounting for conserved replacements. Comparison of the amino acid sequences indicates the rat and bovine proteins are homologs and the species differences in ligand binding may not be due to differences in the primary sequence of the isoquionoline binding proteins. Our results indicate the common characteristics of PBR is their ability to bind isoquinoline ligands, not benzodiazepine ligands, with high affinity. A conserved 17-19 kDa protein is required for demonstration of this receptor. A new nomenclature is presented which designates these receptors as τ (tau) receptors.
    Type
    text
    Dissertation-Reproduction (electronic)
    Degree Name
    Ph.D.
    Degree Level
    doctoral
    Degree Program
    Pharmacology & Toxicology
    Graduate College
    Degree Grantor
    University of Arizona
    Collections
    Dissertations

    entitlement

     
    The University of Arizona Libraries | 1510 E. University Blvd. | Tucson, AZ 85721-0055
    Tel 520-621-6442 | repository@u.library.arizona.edu
    DSpace software copyright © 2002-2017  DuraSpace
    Quick Guide | Contact Us | Send Feedback
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.