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dc.contributor.advisorStephen R. Grant
dc.creatorKang, Xiaoqiang
dc.date.accessioned2019-08-22T19:38:23Z
dc.date.available2019-08-22T19:38:23Z
dc.date.issued1994-06-01T00:00:00-07:00
dc.date.submitted2013-09-13T08:54:07-07:00
dc.identifier.urihttps://hdl.handle.net/20.500.12503/26536
dc.description.abstractXiaoqiang, Kang., Interleukin-8: Baculovirus Expression and the Receptor Signal Transduction Pathway. Doctor of Philosophy (Biomedical Sciences), June, 1994, 150 pp., 4 tables, 36 illustrations, bibliography, 212 titles. The cDNA for human interleukin-8 (IL8) was subcloned from a bacterial source into the eukaryotic baculoviral vector expression system. Recombinant human IL-8 (rhIL-8) was synthesized and secreted from SF9 cells following infection of a recombinant virus harboring the full-length IL-8 structural gene. Recombinant human interleukin-8 was purified ([greater than] 600 fold) to homogeneity using preparative HPLC. The rhIL-8 preparation retained all of the physical, immunological, and biochemical properties of the natural product (monocyte-derived IL-8). Baculovirus vector expression coupled to preparative HPLC proved to be a very efficient method for large-scale recombinant interleukin production. Biochemical mechanisms that mediate IL-8 receptor-stimulated activities are poorly understood. In this study, I have explored the intracellular mechanism(s) induced by IL-8 in differentiated HL-60 cells. IL-8 induced a rapid and transient activation of phospholipase A2 in differentiated HL-60 cells. A consequence of phospholipase A2 activation was the release of arachidonic acid and the generation of lysophospholipids from membrane phospholipids. The IL-8 stimulated-arachidonic acid release was pertussis toxin and phospholipase A2 inhibitor sensitive, and protein kinase C independent. In contrast to another neutrophil chemotactic factor, fMLP, IL-8 did not stimulate the activation of phospholipase C and phospholipase D. When comparing the phosphorylation events induced by IL-8 and fMLP, I found that these two chemotactic factors triggered different protein phosphorylation profiles. Tyrosine phosphorylation of proteins was not detected following IL-8 stimulation in HL-60 cells. However, IL-8 stimulated the rapid autophosphorylation of calcium/calmodulin-dependent protein kinase II (CaM kinase II). These results strongly suggest that the IL-8 receptor is closely coupled to the activation of PLA2 and that CaM kinase II is an integral component of IL-8 receptor signal pathway.
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.subjectCell and Developmental Biology
dc.subjectCell Biology
dc.subjectCells
dc.subjectImmunology and Infectious Disease
dc.subjectInfectious Disease
dc.subjectLife Sciences
dc.subjectMedical Cell Biology
dc.subjectMedical Microbiology
dc.subjectMedicine and Health Sciences
dc.subjectMicrobiology
dc.subjectOther Cell and Developmental Biology
dc.subjectOther Immunology and Infectious Disease
dc.subjectVirology
dc.subjectVirus Diseases
dc.subjectViruses
dc.subjectRecombinant human interleukin-8
dc.subjecteukaryotic baculoviral vector expression
dc.subjectPLA2
dc.subjectCaM kinase II
dc.subjectcalcium/calmodulin-dependent protein kinase II
dc.subjectautophosphorylation
dc.subjectbaculovirus
dc.titleInterleukin-8: Baculovirus Expression and the Receptor Signal Transduction Pathway
dc.typeDissertation
thesis.degree.departmentGraduate School of Biomedical Sciences
thesis.degree.disciplineBiomedical Sciences
thesis.degree.grantorUniversity of North Texas Health Science Center at Fort Worth
thesis.degree.nameDoctor of Philosophy
dc.contributor.committeeMemberRafael Alvarez
dc.contributor.committeeMemberPaula Sumstom
dc.type.materialtext
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