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003 OCoLC;

005 20260420152354.0;

008 010517s1999 xx a bm 000 0 eng d;

035 a| (Sirsi) o46961573;

035 a| (OCoLC)46961573;

049 a| EREE;

050 4 a| QD281.N5b| R69 1999;

100 1 a| Rowan, William H.,c| III,e| author.;

245 10 a| Nitration of annexin II tetramer :b| a novel post-translational modification with implications in lung surfactant secretion /c| by William H. Rowan, III.;

264 0 c| 1999.;

300 a| ix, 99 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| 1999;

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

500 a| Advisor: Lin Liu;

500 a| Advisor: Gerhard W. Kalmus;

520 3 a| Lung surfactant, a phospholipid rich lipoprotein complex, is stored in lamellar bodies and secreted exocytotically by alveolar type II cells. The major function of surfactant has classically been to lower surface tension to prevent alveolar collapse at end-expiration. More recently, surfactant has been shown to play a role in non-specific host defense. Annexin II tetramer (AIIt) is a member of the Ca²⁺ and phospholipid binding protein family and is implicated in membrane fusion during surfactant secretion. It had previously been shown that high concentrations of nitric oxide (NO) inhibits surfactant secretion from lung type II cells. Nitric Oxide reacts with superoxide to form peroxynitrite (ONOO ), a tyrosine nitrating agent, which is found in lungs under certain pathological conditions. It is therefore hypothesized that nitration of AIL by ONOO' may be a mechanism for the NO inhibition of regulated exocytosis. Western blot analysis using anti-nitrotyrosine antibodies showed a dose-dependent nitration of tyrosine residues in AIIt treated with ONOO'. Nitration occurred on the core domain of the protein, as well as on the pi 1 subunit. ONOO' also caused the formation of dimers between p36 and pi 1 subunits which were stable in the presence of heating, SDS treatment, and [beta]-mercaptoethanol. AIIt-mediated liposome aggregation was inhibited by ONOO' with an IC₅₀ of ~ 30 [mu]M. The inhibition was abolished by urate (a scavenger of ONOO' and OH), but not by mannitol (a scavenger of OH) or SOD (a scavenger of 0₂) and appeared to be specific to Alf, since ONOO' only slightly influenced annexin I-mediated liposome aggregation. The conformational change of [mu]Alf induced by Ca²⁺ had no effect on the inhibition. Alf bound to membranes was protected from ONOO'-mediated inhibition. Furthermore, ONOO" had no significant effect on the binding of Alf to membranes. SIN-1 (a ONOO' donor), and the known nitrating agent tetranitromethane (TNM), also inhibited AIIt-mediated liposome aggregation. Nitration of AIIt, also occurs in intact lung epithelial cells (A549) treated with ONOO'. The results of this study suggest that regulated secretion in type II cells could be attenuated via nitration of AIIt, by ONOO'. This finding could have significance with respect to pulmonary diseases such as respiratory distress syndromes in adults or infants.;

504 a| Includes bibliographical references (leaves 86-99).;

650 0 a| Nitration.;

650 0 a| Lipocortins.;

650 0 a| Post-translational modification.;

650 7 a| Lipocortins.2| fast0| (OCoLC)fst00999394;

650 7 a| Nitration.2| fast0| (OCoLC)fst01037974;

650 7 a| Post-translational modification.2| fast0| (OCoLC)fst01072761;

655 7 a| dissertations.2| aat0| (CStmoGRI)aatgf300028029;

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| Liu, Lin,e| degree supervisor.;

700 1 a| Kalmus, Gerhard W.,e| degree supervisor.;

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

856 41 z| Access via ScholarShipu| http://hdl.handle.net/10342/12733;

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

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

994 a| C0b| ERE;

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999 a| ASK AT SPECIAL COLLECTIONS DESKw| ASISc| 1i| 1340902d| 5/29/2001l| JSCJTHDm| JOYNERr| Ys| Yt| JSCJTHDu| 5/17/2001x| ETDz| JSPECCOLLo| .STAFF. 0;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 801604-3001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 4/16/2026x| ETDz| JERESOURCE;

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Nitration of annexin II tetramer : a novel post-translational modification with implications in lung surfactant secretion / by William H. Rowan, III.

Author/creator	Rowan, William H. author.
Other author	Liu, Lin, degree supervisor.
Other author	Kalmus, Gerhard W., degree supervisor.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Production	1999.
Description	ix, 99 leaves : illustrations ; 28 cm
Supplemental Content	Access via ScholarShip
Subjects	Nitration. Lipocortins. Post-translational modification.

Summary	Lung surfactant, a phospholipid rich lipoprotein complex, is stored in lamellar bodies and secreted exocytotically by alveolar type II cells. The major function of surfactant has classically been to lower surface tension to prevent alveolar collapse at end-expiration. More recently, surfactant has been shown to play a role in non-specific host defense. Annexin II tetramer (AIIt) is a member of the Ca²⁺ and phospholipid binding protein family and is implicated in membrane fusion during surfactant secretion. It had previously been shown that high concentrations of nitric oxide (NO) inhibits surfactant secretion from lung type II cells. Nitric Oxide reacts with superoxide to form peroxynitrite (ONOO ), a tyrosine nitrating agent, which is found in lungs under certain pathological conditions. It is therefore hypothesized that nitration of AIL by ONOO' may be a mechanism for the NO inhibition of regulated exocytosis. Western blot analysis using anti-nitrotyrosine antibodies showed a dose-dependent nitration of tyrosine residues in AIIt treated with ONOO'. Nitration occurred on the core domain of the protein, as well as on the pi 1 subunit. ONOO' also caused the formation of dimers between p36 and pi 1 subunits which were stable in the presence of heating, SDS treatment, and [beta]-mercaptoethanol. AIIt-mediated liposome aggregation was inhibited by ONOO' with an IC₅₀ of ~ 30 [mu]M. The inhibition was abolished by urate (a scavenger of ONOO' and OH), but not by mannitol (a scavenger of OH) or SOD (a scavenger of 0₂) and appeared to be specific to Alf, since ONOO' only slightly influenced annexin I-mediated liposome aggregation. The conformational change of [mu]Alf induced by Ca²⁺ had no effect on the inhibition. Alf bound to membranes was protected from ONOO'-mediated inhibition. Furthermore, ONOO" had no significant effect on the binding of Alf to membranes. SIN-1 (a ONOO' donor), and the known nitrating agent tetranitromethane (TNM), also inhibited AIIt-mediated liposome aggregation. Nitration of AIIt, also occurs in intact lung epithelial cells (A549) treated with ONOO'. The results of this study suggest that regulated secretion in type II cells could be attenuated via nitration of AIIt, by ONOO'. This finding could have significance with respect to pulmonary diseases such as respiratory distress syndromes in adults or infants.
General note	Submitted to the faculty of the Department of Biology.
General note	Advisor: Lin Liu
General note	Advisor: Gerhard W. Kalmus
Dissertation note	M.S. East Carolina University 1999
Bibliography note	Includes bibliographical references (leaves 86-99).
Genre/form	dissertations.
Genre/form	Academic theses.
Genre/form	Academic theses.
Genre/form	Thèses et écrits académiques.

Nitration of annexin II tetramer : a novel post-translational modification with implications in lung surfactant secretion / by William H. Rowan, III.

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