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LEADER 04628ctm 2200541 i 4500

001 ocm41569161;

003 OCoLC;

005 20240430153657.0;

008 990618s1996 xx a bm 000 0 eng d;

035 a| (Sirsi) o41569161;

035 a| (OCoLC)41569161;

049 a| EREE;

050 4 a| QP552.A27b| C66 1996;

100 1 a| Cooper, James Bryan,e| author.?| UNAUTHORIZED;

245 10 a| Actin is a PKC[epsilon] anchoring protein :b| role of this cytoskeletal signaling complex in actin organization, PKC[epsilon] activation, and intracellular membrane trafficking /c| by James Bryan Cooper.;

264 0 c| 1996.;

300 a| 70 leaves :b| illustrations ;c| 28 cm;

336 a| textb| txt2| rdacontent;

337 a| unmediatedb| n2| rdamedia;

338 a| volumeb| nc2| rdacarrier;

502 b| M.S.c| East Carolina Universityd| 1996;

500 a| Submitted to the faculty of the Department of Biology.;

500 a| Advisor: David M. Terrian;

520 3 a| Individual isoforms of the protein kinase C (PKC) family of serine threonine kinases may have assumed distinct responsibilities for the control of complex and diverse cellular functions. Enhancement of glutamate release during sustained depolarization of phorbol ester-treated nerve terminals may be due to the persistent, rather than transient, activation of PKC. The [alpha], [epsilon], and [zeta], isoforms of PKC have been shown to be relatively enriched in our preparation of isolated nerve endings. However, only PKC[epsilon] displayed a persistent topogenic response to activation Targeted binding of PKC[epsilon] to actin has been established using overlay, cosedimentation, and competitive binding assays However, the functional implications of this binding remained uncharacterized. The studies described herein provide results supporting three major conclusions which extend our understanding of how the assembly of a PKCs-actin signaling complex might influence the extent of glutamate exocytosis. First, preincubation of hippocampal P₃ synaptosomes with the PKC activator phorbol dibutyrate for at least 10 minutes causes a significant increase in the subplasinalemmal content of monomeric actin but not filamentous actin. Second, after PKCs has bound to the detergent-insoluble fraction following phorbol ester activation, the holoenzyme remains constitutively active in the absence of accepted PKC activators. Third, electron microscopic analysis of depolarized, phorbol ester stimulated nerve terminals has revealed vectorial movement of small synaptic vesicles from the reserve pool to sites proximal to the active zone where the newly recruited vesicles may become docked and primed for subsequent exocytosis. These and several other findings led to the formulation of a model which may explain how release of secretory proteins may be sustained in prolonged bouts of secretory activity. The mechanism responsible for the rearrangement of actin and vectorial movement of vesicles remains unknown; however, the assembly of an isoform-specific signaling complex appears to play a primary role in the PKC-dependent facilitation of glutamate exocytosis.;

504 a| Includes bibliographical references (leaves 62-70).;

650 0 a| Actin.=| ^A412727;

650 0 a| Protein kinase C.=| ^A366722;

650 0 a| Glutamic acidx| Secretion.=| ^A366721;

650 2 a| Actins.0| (DNLM)D000199=| ^A926433;

650 2 a| Protein Kinase C.0| (DNLM)D011493=| ^A930301;

655 2 a| Academic Dissertation.0| (DNLM)D019478?| UNAUTHORIZED;

650 7 a| Actin.2| fast0| (OCoLC)fst00796140;

650 7 a| Protein kinase C.2| fast0| (OCoLC)fst01079692;

655 7 a| Academic theses.2| fast0| (OCoLC)fst01726453;

655 7 a| Academic theses.2| lcgft;

655 7 a| Thèses et écrits académiques.2| rvmgf0| (CaQQLa)RVMGF-000001173;

700 1 a| Terrian, David M.,e| degree supervisor.=| ^A936879;

710 2 a| East Carolina University.b| Department of Biology.=| ^A637467;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/11928;

949 a| Click on web addressw| asish| joyner101;

949 a| Click on web addressw| asish| hsl111;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 650270;

999 a| ASK AT SPECIAL COLLECTIONS DESKw| ASISc| 1i| 1164013d| 11/30/2001l| JSCJTHDm| JOYNERr| Ys| Yt| JSCJTHDu| 11/30/2001x| ETDz| JSPECCOLLo| .STAFF. 0;

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Actin is a PKC[epsilon] anchoring protein : role of this cytoskeletal signaling complex in actin organization, PKC[epsilon] activation, and intracellular membrane trafficking / by James Bryan Cooper.

Author/creator	Cooper, James Bryan author.
Other author	Terrian, David M., degree supervisor.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Production	1996.
Description	70 leaves : illustrations ; 28 cm
Supplemental Content	Access via ScholarShip
Subjects	Actin. Protein kinase C. Glutamic acid--Secretion. Actins. Protein Kinase C.

Summary	Individual isoforms of the protein kinase C (PKC) family of serine threonine kinases may have assumed distinct responsibilities for the control of complex and diverse cellular functions. Enhancement of glutamate release during sustained depolarization of phorbol ester-treated nerve terminals may be due to the persistent, rather than transient, activation of PKC. The [alpha], [epsilon], and [zeta], isoforms of PKC have been shown to be relatively enriched in our preparation of isolated nerve endings. However, only PKC[epsilon] displayed a persistent topogenic response to activation Targeted binding of PKC[epsilon] to actin has been established using overlay, cosedimentation, and competitive binding assays However, the functional implications of this binding remained uncharacterized. The studies described herein provide results supporting three major conclusions which extend our understanding of how the assembly of a PKCs-actin signaling complex might influence the extent of glutamate exocytosis. First, preincubation of hippocampal P₃ synaptosomes with the PKC activator phorbol dibutyrate for at least 10 minutes causes a significant increase in the subplasinalemmal content of monomeric actin but not filamentous actin. Second, after PKCs has bound to the detergent-insoluble fraction following phorbol ester activation, the holoenzyme remains constitutively active in the absence of accepted PKC activators. Third, electron microscopic analysis of depolarized, phorbol ester stimulated nerve terminals has revealed vectorial movement of small synaptic vesicles from the reserve pool to sites proximal to the active zone where the newly recruited vesicles may become docked and primed for subsequent exocytosis. These and several other findings led to the formulation of a model which may explain how release of secretory proteins may be sustained in prolonged bouts of secretory activity. The mechanism responsible for the rearrangement of actin and vectorial movement of vesicles remains unknown; however, the assembly of an isoform-specific signaling complex appears to play a primary role in the PKC-dependent facilitation of glutamate exocytosis.
General note	Submitted to the faculty of the Department of Biology.
General note	Advisor: David M. Terrian
Dissertation note	M.S. East Carolina University 1996
Bibliography note	Includes bibliographical references (leaves 62-70).
Genre/form	Academic theses.
Genre/form	Academic theses.
Genre/form	Thèses et écrits académiques.

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Actin is a PKC[epsilon] anchoring protein : role of this cytoskeletal signaling complex in actin organization, PKC[epsilon] activation, and intracellular membrane trafficking / by James Bryan Cooper.

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