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The role of the HepII domain of fibr...
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The University of Wisconsin - Madison.
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The role of the HepII domain of fibronectin in the regulation of aqueous humor outflow.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
The role of the HepII domain of fibronectin in the regulation of aqueous humor outflow./
作者:
Gonzalez, Jose M., Jr.
面頁冊數:
171 p.
附註:
Adviser: Donna M. Peters.
Contained By:
Dissertation Abstracts International70-02B.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3348767
ISBN:
9781109043129
The role of the HepII domain of fibronectin in the regulation of aqueous humor outflow.
Gonzalez, Jose M., Jr.
The role of the HepII domain of fibronectin in the regulation of aqueous humor outflow.
- 171 p.
Adviser: Donna M. Peters.
Thesis (Ph.D.)--The University of Wisconsin - Madison, 2008.
Elevated intraocular pressure, the primary risk factor for primary open angle glaucoma, is caused by an increase in the resistance of aqueous humor outflow from the trabecular meshwork (TM). Discovery of agents that can alter aqueous humor outflow via the TM would not only be useful as potential therapies but may also help elucidate the etiology and pathology of glaucoma.
ISBN: 9781109043129Subjects--Topical Terms:
1017686
Biology, Cell.
The role of the HepII domain of fibronectin in the regulation of aqueous humor outflow.
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Elevated intraocular pressure, the primary risk factor for primary open angle glaucoma, is caused by an increase in the resistance of aqueous humor outflow from the trabecular meshwork (TM). Discovery of agents that can alter aqueous humor outflow via the TM would not only be useful as potential therapies but may also help elucidate the etiology and pathology of glaucoma.
520
$a
Actin cytoskeleton disrupting agents have been identified as being selective and effective regulators of aqueous humor outflow through the TM. Fibronectin is an extracellular matrix protein found in the TM and a known regulator of the actin cytoskeleton. Accordingly, recent studies have shown that perfusion of human organ culture anterior segments with recombinant HeparinII (HepII) domain from fibronectin increases outflow facility (OF). The body of work presented here describes the mechanism of action of the HepII domain in mediating the observed increase in OF.
520
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Monolayers of primary and immortalized (TM-1) human TM cells developed gaps in response to 24-hour incubations with the HepII domain. The HepII domain disrupted the actin cytoskeleton of cultured TM cells in dose- and time-dependent manners. This disruption preceded and likely caused the disassembly of N-cadherin based adherens junctions.
520
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The activity of the HepII domain was localized to a hexapeptide sequence, PPRARI which binds heparan sulfate as well as alpha4-integrins. This peptide increased OF in cultured monkey anterior segments similar to that observed with the HepII domain and disrupted the actin cytoskeleton in TM-1 cultures. Heparan sulfate interactions, however, were not required for the actin disrupting activity of the HepII domain. Activating alpha4-integrins with an anti-alpha4 antibody, BU49, or other alpha4-binding ligands (VCAM, QIDPS) disrupted the actin cytoskeleton of TM cultures. Silencing alpha4 integrins with RNAi inhibited the activity of PPRARI and the HepII domain. This suggests that alpha4-integrins may be involved in modulating the ability of the HepII domain to disrupt the actin cytoskeleton in TM cultures and regulate OF in organ cultures.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3348767
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