title: Mechanisms of calcium oxalate crystal attachment to injured renal collecting duct cells.
abstract: BACKGROUND
  Renal cell or tissue injury results in a loss of membrane lipid asymmetry and/or loss of cell polarity, and both events lead to changes on the surface of the cell membranes that enhance crystal attachment. We have proposed two distinct mechanisms of crystal attachment following membrane changes induced by various modes of injury.
  
  
  METHODS
  Annexin V was used to determine whether phosphatidylserine (PS) exposure on the cell membrane surface plays a role in calcium oxalate monohydrate (COM) crystal attachment to cells that have lost their polarity as well as to cells that have lost their lipid asymmetry. We utilized two different experimental models of injury to renal epithelial cells in culture. The first model used calcium ionophore A23187 to induce a loss of lipid asymmetry, and the second model used EGTA to break down tight junctions and lose cell polarity.
  
  
  RESULTS
  Inner medullary collecting duct cells that have lost lipid asymmetry demonstrated an increase in the number of cells that bound annexin V. However, when cells lost their polarity, they did not bind annexin V. In addition, the attachment of crystals to cells following a loss of cell polarity was not inhibited by annexin V.
  
  
  CONCLUSIONS
  This study indicates that both individual cell injury (loss of lipid asymmetry) and generalized cell monolayer injury (loss of cell polarity) result in the presentation of different cell surfaces and that both forms of injury result in an increased affinity for crystal attachment. Both mechanisms could be important independently or collectively in the retention of microcrystals to renal collecting duct cells in urolithiasis.
authors.affiliation: Department of Medicine, Medical College of Wisconsin and Department of Veterans Affairs Medical Center, Milwaukee, Wisconsin, USA.
authors.forename: J H
authors.initials: JH
authors.lastname: Wiessner
authors.forename: A T
authors.initials: AT
authors.lastname: Hasegawa
authors.forename: L Y
authors.initials: LY
authors.lastname: Hung
authors.forename: G S
authors.initials: GS
authors.lastname: Mandel
authors.forename: N S
authors.initials: NS
authors.lastname: Mandel
mesh_terms: D000818:Animals; D017304:Annexin A5 / Q000378:metabolism / Q000494:pharmacology; D000001:Calcimycin / Q000494:pharmacology; D002129:Calcium Oxalate / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000187:drug effects; D016764:Cell Polarity / Q000187:drug effects; D002478:Cells, Cultured; D003460:Crystallization; D004533:Egtazic Acid / Q000494:pharmacology; D007476:Ionophores / Q000494:pharmacology; D007685:Kidney Tubules, Collecting / Q000166:cytology / Q000187:drug effects / Q000378:metabolism* / Q000502:physiology; D050356:Lipid Metabolism; D010718:Phosphatidylserines / Q000494:pharmacology; D051381:Rats; D019108:Tight Junctions / Q000187:drug effects
chemical_list: D017304:Annexin A5; D007476:Ionophores; D010718:Phosphatidylserines; D002129:Calcium Oxalate; D000001:Calcimycin; D004533:Egtazic Acid