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Article: Synergism between phospholipase D2 and sorbitol accumulation in diabetic cataract formation through modulation of Na,K-ATPase activity and osmotic stress

TitleSynergism between phospholipase D2 and sorbitol accumulation in diabetic cataract formation through modulation of Na,K-ATPase activity and osmotic stress
Authors
Keywordscataract
Na/K-ATPase
osmotic stress
phospholipase
Issue Date2006
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexer
Citation
Experimental Eye Research, 2006, v. 83 n. 4, p. 939-948 How to Cite?
AbstractPhospholipase D (PLD), a highly regulated enzyme that generates the second messenger phosphatidic acid, functions in signal transduction, membrane trafficking and cytoskeletal reorganization. PLD is thought to be involved in the pathogenesis of diabetic complications by activating PKC. Since PKC and PLD are present in the lens we sought to determine if PLD plays a role in diabetic cataract development. We developed transgenic mice that overexpress PLD2, one of the two mammalian isoforms of PLD. These mice developed congenital nuclear cataracts, but not diabetic cataracts. Histological analysis revealed vacuole formation in the fiber cells, mediated potentially by the substantially increased Na,K-ATPase activity. In the presence of the aldose reductase overexpressing transgene that increases lens osmotic pressure, these double transgenic mice developed more severe congenital cataract and became susceptible to develop diabetic cataract. Together, these data suggest that increased PLD2 activity in the lens under hyperglycemic condition might impair its osmoregulatory mechanism and reduce its ability to cope with the osmotic stress triggered by sorbitol accumulation. © 2006 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/146631
ISSN
2015 Impact Factor: 2.998
2015 SCImago Journal Rankings: 1.218
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHuang, Pen_HK
dc.contributor.authorJiang, Zen_HK
dc.contributor.authorTeng, Sen_HK
dc.contributor.authorWong, YCen_HK
dc.contributor.authorFrohman, MAen_HK
dc.contributor.authorChung, SKen_HK
dc.contributor.authorChung, SSMen_HK
dc.date.accessioned2012-05-08T03:21:23Z-
dc.date.available2012-05-08T03:21:23Z-
dc.date.issued2006en_HK
dc.identifier.citationExperimental Eye Research, 2006, v. 83 n. 4, p. 939-948en_HK
dc.identifier.issn0014-4835en_HK
dc.identifier.urihttp://hdl.handle.net/10722/146631-
dc.description.abstractPhospholipase D (PLD), a highly regulated enzyme that generates the second messenger phosphatidic acid, functions in signal transduction, membrane trafficking and cytoskeletal reorganization. PLD is thought to be involved in the pathogenesis of diabetic complications by activating PKC. Since PKC and PLD are present in the lens we sought to determine if PLD plays a role in diabetic cataract development. We developed transgenic mice that overexpress PLD2, one of the two mammalian isoforms of PLD. These mice developed congenital nuclear cataracts, but not diabetic cataracts. Histological analysis revealed vacuole formation in the fiber cells, mediated potentially by the substantially increased Na,K-ATPase activity. In the presence of the aldose reductase overexpressing transgene that increases lens osmotic pressure, these double transgenic mice developed more severe congenital cataract and became susceptible to develop diabetic cataract. Together, these data suggest that increased PLD2 activity in the lens under hyperglycemic condition might impair its osmoregulatory mechanism and reduce its ability to cope with the osmotic stress triggered by sorbitol accumulation. © 2006 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexeren_HK
dc.relation.ispartofExperimental Eye Researchen_HK
dc.subjectcataracten_HK
dc.subjectNa/K-ATPaseen_HK
dc.subjectosmotic stressen_HK
dc.subjectphospholipaseen_HK
dc.subject.meshAnimalsen_US
dc.subject.meshCataract - Congenital - Etiology - Metabolismen_US
dc.subject.meshDiabetes Complications - Metabolismen_US
dc.subject.meshDiabetes Mellitus, Experimental - Complications - Metabolismen_US
dc.subject.meshDisease Progressionen_US
dc.subject.meshDisease Susceptibilityen_US
dc.subject.meshGene Expressionen_US
dc.subject.meshMiceen_US
dc.subject.meshMice, Transgenicen_US
dc.subject.meshOsmosisen_US
dc.subject.meshPhospholipase D - Genetics - Metabolismen_US
dc.subject.meshReverse Transcriptase Polymerase Chain Reaction - Methodsen_US
dc.subject.meshSodium-Potassium-Exchanging Atpase - Metabolismen_US
dc.subject.meshSorbitol - Metabolismen_US
dc.titleSynergism between phospholipase D2 and sorbitol accumulation in diabetic cataract formation through modulation of Na,K-ATPase activity and osmotic stressen_HK
dc.typeArticleen_HK
dc.identifier.emailWong, YC: ycwong@hkucc.hku.hken_HK
dc.identifier.emailChung, SK: skchung@hkucc.hku.hken_HK
dc.identifier.emailChung, SSM: smchung@hkucc.hku.hken_HK
dc.identifier.authorityWong, YC=rp00316en_HK
dc.identifier.authorityChung, SK=rp00381en_HK
dc.identifier.authorityChung, SSM=rp00376en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.exer.2006.05.001en_HK
dc.identifier.pmid16797533-
dc.identifier.scopuseid_2-s2.0-33747888188en_HK
dc.identifier.hkuros129019-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33747888188&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume83en_HK
dc.identifier.issue4en_HK
dc.identifier.spage939en_HK
dc.identifier.epage948en_HK
dc.identifier.isiWOS:000240720600029-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridHuang, P=7403659267en_HK
dc.identifier.scopusauthoridJiang, Z=7404279744en_HK
dc.identifier.scopusauthoridTeng, S=14319219900en_HK
dc.identifier.scopusauthoridWong, YC=7403041798en_HK
dc.identifier.scopusauthoridFrohman, MA=7005482313en_HK
dc.identifier.scopusauthoridChung, SK=7404292976en_HK
dc.identifier.scopusauthoridChung, SSM=14120761600en_HK

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