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Breakdown of the crystalloid endoplasmic reticulum of UT-1 cells
dc.contributor.advisor | Kochevar, Deborah T. | |
dc.creator | Mitchell, Linda Deanne Moore | |
dc.date.accessioned | 2020-09-02T20:23:51Z | |
dc.date.available | 2020-09-02T20:23:51Z | |
dc.date.issued | 1994 | |
dc.identifier.uri | https://hdl.handle.net/1969.1/DISSERTATIONS-1551994 | |
dc.description | Vita. | en |
dc.description.abstract | The studies described focus on the sterol-regulated mechanism by which UT-1 cells dispose of an elaborate intracellular membrane system of smooth endoplasmic reticulum (ER) termed crystalloid ER (CER). The CER is formed in response to lipoprotein deprivation and competitive inhibition o f 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR). Under these conditions, UT-1 cells produce up to 500-fold more HMGR than parental CHO cells. HMGR has been shown to occupy the CER. Addition of sterols to the growth media of UT-1 cells has been shown to cause the degradation of HMGR and breakdown of the CER membrane system. It has also been shown that sterol-accelerated degradation of CER membranes occurs via a non-lysosomal pathway. Other possible mechanisms of CER elimination include intra- ER degradation and expulsion of CER membranes to the extracellular media. There were four specific aims included in these studies. First, indirect immunofluorescence microscopy and brefeldin A were used to determine the existence of an intra-ER degradative pathway for HMGR in UT-1 cells. Second, silver stain, 45ca2+, and 32p_(}TP overlay techniques were used on proteins separated by 2-D SDS-PAGE to determine changes in proteins during incubation of UT-1 cells in sterols. Third, immunoblotting of immunoprecipitated proteins was used to account for both intra- and extracellular disposition of CER membranes and proteins during CER breakdown. Lastly, a major constituent protein of the CER of UT-1 cells, CERp60, was purified and submitted for sequencing to determine if it was related to a multifiinctional ER protein, protein disulfide isomerase. The goals of these studies was to further define the location of HMGR degradation, to determine sterol-mediated changes in UT-1 proteins, in particular Ca^+- and GTP-binding proteins, and to determine if CERp60 was related to protein disulfide isomerase. | en |
dc.format.extent | xi, 118 leaves | en |
dc.format.medium | electronic | en |
dc.format.mimetype | application/pdf | |
dc.language.iso | eng | |
dc.rights | This thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use. | en |
dc.rights.uri | http://rightsstatements.org/vocab/InC/1.0/ | |
dc.subject | Major veterinary physiology | en |
dc.title | Breakdown of the crystalloid endoplasmic reticulum of UT-1 cells | en |
dc.type | Thesis | en |
thesis.degree.grantor | Texas A&M University | en |
thesis.degree.name | Doctor of Philosophy | en |
thesis.degree.name | Ph. D | en |
dc.contributor.committeeMember | Meininger, Cynthia J. | |
dc.contributor.committeeMember | Ramos, Kenneth | |
dc.contributor.committeeMember | Burghardt, Robert C. | |
dc.type.genre | dissertations | en |
dc.type.material | text | en |
dc.format.digitalOrigin | reformatted digital | en |
dc.publisher.digital | Texas A&M University. Libraries | |
dc.identifier.oclc | 34743726 |
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