Regulation and Characterization of Cardiac Phosphoinositide-Specific Phospholipase C (PLC) Isoenzymes

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dc.contributor.advisorEugene E. Quist
dc.contributor.committeeMemberThomas Yorio
dc.contributor.committeeMemberMing-Chi Wu
dc.creatorWang, Juan
dc.date.accessioned2019-08-22T21:48:29Z
dc.date.available2019-08-22T21:48:29Z
dc.date.issued1997-12-01
dc.date.submitted2014-04-09T06:36:22-07:00
dc.description.abstractWang, Juan, Regulation and Characterization of Cardiac Phosphoinositide-Specific Phospholipase C Isoenzymes. Master of Biomedical Science, Dec., 1997, 79 pp., 20 illustration, bibliography, 62 titles. It is hypothesized that myocardial phosphoinositide-specific phospholipase C (PLC) isoenzymes are regulated by physiological intracellular Ca2+ and by cytosol-membrane translocation. The regulation and identification of PLC isoenzymes in rat and dog ventricular subcellular fractions were studied. PLC-β1, PLC-β3 and PLC-δ1 were identified in rat and dog cytosol and microsomal membranes by chromatographic separation, enzyme assays and western blotting. Truncated PLC-β isoforms with molecular weights of 69 kDa and 114 kDa were isolated from rat and dog cytosol, respectively. Species differences in the relative distribution of PLC isoenzymes were evident as PLC-δ dominant in rat whereas PLC-β isoenzymes were dominant in dog. A 91 kDa cytosolic protein which did not contain PLC activity alone markedly led to PLC activation when combined with microsomes. The activator protein was immunoprecipitated with an anti-PLC-δ identifying this activator as an inactive PLC-δ isoenzyme. These studies indicate that cytosolic PLC-δ may be activated by translocating to membranes. In addition, proteolysis may be involved in long term activation of cytosolic PLC isoenzymes. Further studies will be required to resolve the physiological significance of these modes of cardiac PLC activation.
dc.format.mimetypeapplication/pdf
dc.identifier.urihttps://hdl.handle.net/20.500.12503/29598
dc.language.isoen
dc.provenance.legacyDownloads0
dc.subjectCardiovascular System
dc.subjectCell and Developmental Biology
dc.subjectCell Biology
dc.subjectCells
dc.subjectCellular and Molecular Physiology
dc.subjectCirculatory and Respiratory Physiology
dc.subjectComparative and Laboratory Animal Medicine
dc.subjectImmunity
dc.subjectImmunology and Infectious Disease
dc.subjectLife Sciences
dc.subjectMedical Cell Biology
dc.subjectMedical Sciences
dc.subjectMedicine and Health Sciences
dc.subjectOther Cell and Developmental Biology
dc.subjectOther Immunology and Infectious Disease
dc.subjectPhysiology
dc.subjectSystems and Integrative Physiology
dc.subjectRegulation
dc.subjectcharacterization
dc.subjectcardiac phophoinositide-specific phospholipase C isoenzymes
dc.subjectPLC
dc.subjectintracellular calcium
dc.subjectCa2+
dc.subjectisoenzymes
dc.subjectrats
dc.subjectdogs
dc.subjectcytosolic protein
dc.subjectcytosolic PLC-δ
dc.titleRegulation and Characterization of Cardiac Phosphoinositide-Specific Phospholipase C (PLC) Isoenzymes
dc.typeThesis
dc.type.materialtext
thesis.degree.departmentGraduate School of Biomedical Sciences
thesis.degree.disciplinePharmacology and Neuroscience
thesis.degree.grantorUniversity of North Texas Health Science Center at Fort Worth
thesis.degree.nameMaster of Science

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