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A Novel Terminal Web‐Like Structure in Cortical Lens Fibers: Architecture and Functional Assessment
This study describes a novel cytoskeletal array in fiber cells of the ocular lens of the rat and shows its relationship to the classical terminal web of other epithelial tissues. Naive adult Sprague‐Dawley rats (n = 28) were utilized. F‐actin, fodrin, myosin IIA, and CP49 distribution was assessed i...
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Published in: | Anatomical record (Hoboken, N.J. : 2007) N.J. : 2007), 2010-11, Vol.293 (11), p.1805-1815 |
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description | This study describes a novel cytoskeletal array in fiber cells of the ocular lens of the rat and shows its relationship to the classical terminal web of other epithelial tissues. Naive adult Sprague‐Dawley rats (n = 28) were utilized. F‐actin, fodrin, myosin IIA, and CP49 distribution was assessed in anterior and posterior polar sections. For functional analysis, lenses were cultured with or without cytochalasin‐D for 3 hr, then processed for confocal microscopy or assessed by laser scan analysis along sutures. Phalloidin labeling demonstrated a dense mesh of F‐actin adjacent to posterior sutural domains to a subcapsular depth of 400 μm. Anterior polar sections revealed a comparable actin structure adjacent to anterior suture branches however, it was not developed in superficial fibers. Fodrin and myosin were localized within the web‐like actin apparatus. The data was used to construct a model showing that the cytoskeletal array is located within the blunt, variable‐width fiber ends that abut at sutures such that the “terminal web” flanks the suture on either side. Treatment with cytochalasin‐D resulted in partial disassembly of the “terminal web” and perturbed cellular organization. Laser scan analysis revealed that cytochalasin‐D treated lenses had significantly greater focal variability than control lenses (P = 0.020). We conclude that cortical fibers of rat lenses contain a bipolar structure that is structurally and compositionally analogous to classical terminal webs. The results indicate that the lens “terminal web” functions to stabilize lens fiber ends at sutures thus minimizing structural disorder, which in turn, promotes the establishment and maintenance of lens transparency. Anat Rec, 2010. © 2010 Wiley‐Liss, Inc. |
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Naive adult Sprague‐Dawley rats (n = 28) were utilized. F‐actin, fodrin, myosin IIA, and CP49 distribution was assessed in anterior and posterior polar sections. For functional analysis, lenses were cultured with or without cytochalasin‐D for 3 hr, then processed for confocal microscopy or assessed by laser scan analysis along sutures. Phalloidin labeling demonstrated a dense mesh of F‐actin adjacent to posterior sutural domains to a subcapsular depth of 400 μm. Anterior polar sections revealed a comparable actin structure adjacent to anterior suture branches however, it was not developed in superficial fibers. Fodrin and myosin were localized within the web‐like actin apparatus. The data was used to construct a model showing that the cytoskeletal array is located within the blunt, variable‐width fiber ends that abut at sutures such that the “terminal web” flanks the suture on either side. Treatment with cytochalasin‐D resulted in partial disassembly of the “terminal web” and perturbed cellular organization. Laser scan analysis revealed that cytochalasin‐D treated lenses had significantly greater focal variability than control lenses (P = 0.020). We conclude that cortical fibers of rat lenses contain a bipolar structure that is structurally and compositionally analogous to classical terminal webs. The results indicate that the lens “terminal web” functions to stabilize lens fiber ends at sutures thus minimizing structural disorder, which in turn, promotes the establishment and maintenance of lens transparency. Anat Rec, 2010. © 2010 Wiley‐Liss, Inc.</description><identifier>ISSN: 1932-8486</identifier><identifier>EISSN: 1932-8494</identifier><identifier>DOI: 10.1002/ar.21216</identifier><identifier>PMID: 20730867</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Actins - analysis ; Actins - physiology ; Actins - ultrastructure ; Animals ; Carrier Proteins - analysis ; Carrier Proteins - physiology ; Carrier Proteins - ultrastructure ; Cytochalasin D - pharmacology ; cytoskeleton ; Cytoskeleton - drug effects ; Cytoskeleton - physiology ; Cytoskeleton - ultrastructure ; Eye Proteins - analysis ; Eye Proteins - physiology ; Eye Proteins - ultrastructure ; immunocytochemistry ; Intermediate Filament Proteins - analysis ; Intermediate Filament Proteins - physiology ; Intermediate Filament Proteins - ultrastructure ; laser scan analysis ; lens ; Lens, Crystalline - chemistry ; Lens, Crystalline - cytology ; Lens, Crystalline - physiology ; Microfilament Proteins - analysis ; Microfilament Proteins - physiology ; Microfilament Proteins - ultrastructure ; Microscopy, Confocal ; Nonmuscle Myosin Type IIA - analysis ; Nonmuscle Myosin Type IIA - physiology ; Nonmuscle Myosin Type IIA - ultrastructure ; Nucleic Acid Synthesis Inhibitors - pharmacology ; Rats ; Rats, Sprague-Dawley ; terminal web</subject><ispartof>Anatomical record (Hoboken, N.J. : 2007), 2010-11, Vol.293 (11), p.1805-1815</ispartof><rights>Copyright © 2010 Wiley‐Liss, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4096-ca169bd28bc019b6570cb4bc2282eaefc692768c6af506695cfa57819249811f3</citedby><cites>FETCH-LOGICAL-c4096-ca169bd28bc019b6570cb4bc2282eaefc692768c6af506695cfa57819249811f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20730867$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Al‐Ghoul, Kristin J.</creatorcontrib><creatorcontrib>Lindquist, Timothy P.</creatorcontrib><creatorcontrib>Kirk, Spencer S.</creatorcontrib><creatorcontrib>Donohue, Sean T.</creatorcontrib><title>A Novel Terminal Web‐Like Structure in Cortical Lens Fibers: Architecture and Functional Assessment</title><title>Anatomical record (Hoboken, N.J. : 2007)</title><addtitle>Anat Rec (Hoboken)</addtitle><description>This study describes a novel cytoskeletal array in fiber cells of the ocular lens of the rat and shows its relationship to the classical terminal web of other epithelial tissues. Naive adult Sprague‐Dawley rats (n = 28) were utilized. F‐actin, fodrin, myosin IIA, and CP49 distribution was assessed in anterior and posterior polar sections. For functional analysis, lenses were cultured with or without cytochalasin‐D for 3 hr, then processed for confocal microscopy or assessed by laser scan analysis along sutures. Phalloidin labeling demonstrated a dense mesh of F‐actin adjacent to posterior sutural domains to a subcapsular depth of 400 μm. Anterior polar sections revealed a comparable actin structure adjacent to anterior suture branches however, it was not developed in superficial fibers. Fodrin and myosin were localized within the web‐like actin apparatus. The data was used to construct a model showing that the cytoskeletal array is located within the blunt, variable‐width fiber ends that abut at sutures such that the “terminal web” flanks the suture on either side. Treatment with cytochalasin‐D resulted in partial disassembly of the “terminal web” and perturbed cellular organization. Laser scan analysis revealed that cytochalasin‐D treated lenses had significantly greater focal variability than control lenses (P = 0.020). We conclude that cortical fibers of rat lenses contain a bipolar structure that is structurally and compositionally analogous to classical terminal webs. The results indicate that the lens “terminal web” functions to stabilize lens fiber ends at sutures thus minimizing structural disorder, which in turn, promotes the establishment and maintenance of lens transparency. Anat Rec, 2010. © 2010 Wiley‐Liss, Inc.</description><subject>Actins - analysis</subject><subject>Actins - physiology</subject><subject>Actins - ultrastructure</subject><subject>Animals</subject><subject>Carrier Proteins - analysis</subject><subject>Carrier Proteins - physiology</subject><subject>Carrier Proteins - ultrastructure</subject><subject>Cytochalasin D - pharmacology</subject><subject>cytoskeleton</subject><subject>Cytoskeleton - drug effects</subject><subject>Cytoskeleton - physiology</subject><subject>Cytoskeleton - ultrastructure</subject><subject>Eye Proteins - analysis</subject><subject>Eye Proteins - physiology</subject><subject>Eye Proteins - ultrastructure</subject><subject>immunocytochemistry</subject><subject>Intermediate Filament Proteins - analysis</subject><subject>Intermediate Filament Proteins - physiology</subject><subject>Intermediate Filament Proteins - ultrastructure</subject><subject>laser scan analysis</subject><subject>lens</subject><subject>Lens, Crystalline - chemistry</subject><subject>Lens, Crystalline - cytology</subject><subject>Lens, Crystalline - physiology</subject><subject>Microfilament Proteins - analysis</subject><subject>Microfilament Proteins - physiology</subject><subject>Microfilament Proteins - ultrastructure</subject><subject>Microscopy, Confocal</subject><subject>Nonmuscle Myosin Type IIA - analysis</subject><subject>Nonmuscle Myosin Type IIA - physiology</subject><subject>Nonmuscle Myosin Type IIA - ultrastructure</subject><subject>Nucleic Acid Synthesis Inhibitors - pharmacology</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>terminal web</subject><issn>1932-8486</issn><issn>1932-8494</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNp1kctKxDAUhoMoOo6CTyDZ6aaapG2auBDK4KgwKHjBZUgzpxrtRZN2ZHY-gs_ok1jtOOjC1TlwPr7_wI_QDiUHlBB2qN0Bo4zyFTSgMmSBiGS0utwF30Cb3j8SEkdEhutog5EkJIInAwQpvqhnUOAbcKWtdIHvIPt4e5_YJ8DXjWtN0zrAtsKj2jXWdMAEKo_HNgPnj3DqzINtoKd0NcXjtjKNrb9MqffgfQlVs4XWcl142F7MIbodn9yMzoLJ5en5KJ0EpnuMB0ZTLrMpE5khVGY8TojJoswwJhhoyA2XLOHCcJ3HhHMZm1zHiaCSRVJQmodDdNx7n9ushKnpop0u1LOzpXZzVWur_l4q-6Du65likiexoJ1gbyFw9UsLvlGl9QaKQldQt14lnBEmSRh25H5PGld77yBfplCivkpR2qnvUjp09_dXS_CnhQ4IeuDVFjD_V6TSq174Ccsxlzo</recordid><startdate>201011</startdate><enddate>201011</enddate><creator>Al‐Ghoul, Kristin J.</creator><creator>Lindquist, Timothy P.</creator><creator>Kirk, Spencer S.</creator><creator>Donohue, Sean T.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201011</creationdate><title>A Novel Terminal Web‐Like Structure in Cortical Lens Fibers: Architecture and Functional Assessment</title><author>Al‐Ghoul, Kristin J. ; Lindquist, Timothy P. ; Kirk, Spencer S. ; Donohue, Sean T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4096-ca169bd28bc019b6570cb4bc2282eaefc692768c6af506695cfa57819249811f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Actins - analysis</topic><topic>Actins - physiology</topic><topic>Actins - ultrastructure</topic><topic>Animals</topic><topic>Carrier Proteins - analysis</topic><topic>Carrier Proteins - physiology</topic><topic>Carrier Proteins - ultrastructure</topic><topic>Cytochalasin D - pharmacology</topic><topic>cytoskeleton</topic><topic>Cytoskeleton - drug effects</topic><topic>Cytoskeleton - physiology</topic><topic>Cytoskeleton - ultrastructure</topic><topic>Eye Proteins - analysis</topic><topic>Eye Proteins - physiology</topic><topic>Eye Proteins - ultrastructure</topic><topic>immunocytochemistry</topic><topic>Intermediate Filament Proteins - analysis</topic><topic>Intermediate Filament Proteins - physiology</topic><topic>Intermediate Filament Proteins - ultrastructure</topic><topic>laser scan analysis</topic><topic>lens</topic><topic>Lens, Crystalline - chemistry</topic><topic>Lens, Crystalline - cytology</topic><topic>Lens, Crystalline - physiology</topic><topic>Microfilament Proteins - analysis</topic><topic>Microfilament Proteins - physiology</topic><topic>Microfilament Proteins - ultrastructure</topic><topic>Microscopy, Confocal</topic><topic>Nonmuscle Myosin Type IIA - analysis</topic><topic>Nonmuscle Myosin Type IIA - physiology</topic><topic>Nonmuscle Myosin Type IIA - ultrastructure</topic><topic>Nucleic Acid Synthesis Inhibitors - pharmacology</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>terminal web</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Al‐Ghoul, Kristin J.</creatorcontrib><creatorcontrib>Lindquist, Timothy P.</creatorcontrib><creatorcontrib>Kirk, Spencer S.</creatorcontrib><creatorcontrib>Donohue, Sean T.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Anatomical record (Hoboken, N.J. : 2007)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Al‐Ghoul, Kristin J.</au><au>Lindquist, Timothy P.</au><au>Kirk, Spencer S.</au><au>Donohue, Sean T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Novel Terminal Web‐Like Structure in Cortical Lens Fibers: Architecture and Functional Assessment</atitle><jtitle>Anatomical record (Hoboken, N.J. : 2007)</jtitle><addtitle>Anat Rec (Hoboken)</addtitle><date>2010-11</date><risdate>2010</risdate><volume>293</volume><issue>11</issue><spage>1805</spage><epage>1815</epage><pages>1805-1815</pages><issn>1932-8486</issn><eissn>1932-8494</eissn><abstract>This study describes a novel cytoskeletal array in fiber cells of the ocular lens of the rat and shows its relationship to the classical terminal web of other epithelial tissues. Naive adult Sprague‐Dawley rats (n = 28) were utilized. F‐actin, fodrin, myosin IIA, and CP49 distribution was assessed in anterior and posterior polar sections. For functional analysis, lenses were cultured with or without cytochalasin‐D for 3 hr, then processed for confocal microscopy or assessed by laser scan analysis along sutures. Phalloidin labeling demonstrated a dense mesh of F‐actin adjacent to posterior sutural domains to a subcapsular depth of 400 μm. Anterior polar sections revealed a comparable actin structure adjacent to anterior suture branches however, it was not developed in superficial fibers. Fodrin and myosin were localized within the web‐like actin apparatus. The data was used to construct a model showing that the cytoskeletal array is located within the blunt, variable‐width fiber ends that abut at sutures such that the “terminal web” flanks the suture on either side. Treatment with cytochalasin‐D resulted in partial disassembly of the “terminal web” and perturbed cellular organization. Laser scan analysis revealed that cytochalasin‐D treated lenses had significantly greater focal variability than control lenses (P = 0.020). We conclude that cortical fibers of rat lenses contain a bipolar structure that is structurally and compositionally analogous to classical terminal webs. The results indicate that the lens “terminal web” functions to stabilize lens fiber ends at sutures thus minimizing structural disorder, which in turn, promotes the establishment and maintenance of lens transparency. Anat Rec, 2010. © 2010 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>20730867</pmid><doi>10.1002/ar.21216</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Actins - analysis Actins - physiology Actins - ultrastructure Animals Carrier Proteins - analysis Carrier Proteins - physiology Carrier Proteins - ultrastructure Cytochalasin D - pharmacology cytoskeleton Cytoskeleton - drug effects Cytoskeleton - physiology Cytoskeleton - ultrastructure Eye Proteins - analysis Eye Proteins - physiology Eye Proteins - ultrastructure immunocytochemistry Intermediate Filament Proteins - analysis Intermediate Filament Proteins - physiology Intermediate Filament Proteins - ultrastructure laser scan analysis lens Lens, Crystalline - chemistry Lens, Crystalline - cytology Lens, Crystalline - physiology Microfilament Proteins - analysis Microfilament Proteins - physiology Microfilament Proteins - ultrastructure Microscopy, Confocal Nonmuscle Myosin Type IIA - analysis Nonmuscle Myosin Type IIA - physiology Nonmuscle Myosin Type IIA - ultrastructure Nucleic Acid Synthesis Inhibitors - pharmacology Rats Rats, Sprague-Dawley terminal web |
title | A Novel Terminal Web‐Like Structure in Cortical Lens Fibers: Architecture and Functional Assessment |
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