Cell type-specific acquired protection from crystal adherence by renal tubule cells in culture

Verkoelen, Carl F.; Boom, Burt G. van der; Kok, Dirk J.; Houtsmuller, Adriaan B.; Visser, Pim; Schröder, Fritz H.; Romijn, Johannes C.

doi:10.1046/j.1523-1755.1999.00383.x

Cited by 63 publications

(35 citation statements)

References 22 publications

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“…MD-CKI cells exhibit variable COM binding at different stages of growth. COM crystal binding is highest between days 2 and 4 after plating; by day 7, it decreases to about 20% of this value (49). Expression of Ax-II during various phases of MDCKI cell cycle has not been determined; however, it is tempting to speculate that this variable COM binding exhibited by MDCKI cells could be due, in part, to altered Ax-II expression during the MDCK cell cycle.…”

Section: Discussionmentioning

confidence: 97%

Annexin II Is Present on Renal Epithelial Cells and Binds Calcium Oxalate Monohydrate Crystals

Kumar¹,

Farell²,

Deganello³

et al. 2003

Journal of the American Society of Nephrology

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Abstract. Attachment of newly formed crystals to renal epithelial cells appears to be a critical step in the development of kidney stones. The current study was undertaken to identify potential calcium oxalate monohydrate (COM) crystal-binding proteins on the surface of renal tubular cells. Apical membranes were prepared from confluent monolayers of renal epithelial cells (MDCKI line), and COM crystal affinity was used to isolate crystal-binding proteins that were then subjected to electrophoresis and electroblotting. Microsequencing of the most prominent COM crystal-binding protein (M r of 37 kD) identified it as annexin II (Ax-II). When exposed proteins on the surface of intact monolayers were biotinylated and then isolated using streptavidin agarose beads, Ax-II was detected, suggesting that at least a portion is exposed on the apical cell surface. Ax-II was not completely extracted by 0.1 M Na 2 CO 3 , suggesting that at least a portion of cellular Ax-II is an intrinsic membrane-bound protein. Using confocal immunofluorescence microscopy, Ax-II was visualized together with Caveolin-1 (Cav-1) on the apical membrane of intact MDCKI cells. Cells pretreated with a monoclonal anti-Ax-II antibody bound significantly fewer COM crystals, whereas anti-LDL receptor antibody did not decrease COM binding, further suggesting a functional role for Ax-II during adhesion of crystals to intact cells. These results suggest that Ax-II avidly binds COM crystals and is present on the apical surface of MDCKI cells.

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Section: Discussionmentioning

confidence: 97%

Annexin II Is Present on Renal Epithelial Cells and Binds Calcium Oxalate Monohydrate Crystals

Kumar¹,

Farell²,

Deganello³

et al. 2003

Journal of the American Society of Nephrology

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“…We suggest that functional coupling of NHA2 and V-ATPase establishes a mechanistically novel Na ϩ (Li ϩ ) efflux pump in mammalian cells. Cultured MDCK cells retain properties of intercalated cells of the distal nephron (29), where V-ATPase localization is known to alternate between apical and basolateral membranes. It is likely that NHA2 localization is also coupled with that of VATPase resulting in a virtual cation-H ϩ efflux mechanism to regulate Na ϩ homeostasis, volume regulation and consequently, hypertension.…”

Section: Discussionmentioning

confidence: 99%

Unconventional Chemiosmotic Coupling of NHA2, a Mammalian Na+/H+ Antiporter, to a Plasma Membrane H+ Gradient

Kondapalli

Kallay

Muszelik

et al. 2012

Journal of Biological Chemistry

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“…Intact, quiescent monolayers of well-differentiated cultured cells have little affinity for crystals (6,10,14). Clinically, crystalluria is frequently observed in the absence of stone disease (15).…”

Section: Discussionmentioning

confidence: 99%

An Acidic Peptide Sequence of Nucleolin-Related Protein Can Mediate the Attachment of Calcium Oxalate to Renal Tubule Cells

Сорокина¹,

Wesson²,

Kleinman³

2004

Journal of the American Society of Nephrology

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Abstract. Crystals that form in tubular fluid must be retained in the kidney to become stones. Nucleolin-related protein (NRP) is found on the surface of inner medullary collecting duct (IMCD) cells in culture (cIMCD) and selectively adsorbs to calcium oxalate (CaOx). We proposed that NRP mediates attachment to the renal tubular epithelium of Ca stone crystals through an electrostatic interaction with a highly acidic region (acidic fragment [AF]) similar to those of other proteins that have been reported to affect urinary crystal formation. The current studies demonstrate that nucleolin is expressed on both apical and basolateral cell surfaces of cIMCD, reaching a peak in the late stages of mitosis and gradually declining to undetectable levels with maturation of the polarized epithelium. Scraping areas of mature monolayers stimulated the cells surrounding the defects to migrate and proliferate so as to repair them, and these areas demonstrate surface NRP expression and enhanced attachment of CaOx monohydrate crystals. Surface expression of the NRP AF was produced by cloning the NRP AF into a display vector. Transfected cIMCD demonstrating copious surface expression of AF enhanced CaOx attachment 6.7-fold compared with control cIMCD, whereas cells transfected with a vector without the AF did not differ from control. AF was also cloned into a replication-deficient adenovirus and expressed in 293 cells, resulting in AF secretion into the nutrient medium. This medium inhibited CaOx attachment to cIMCD, compared with conditioned medium from cells infected with wild-type virus. These results demonstrate that surface-bound AF can mediate CaOx attachment and that secreted AF can inhibit attachment. These results support the notion that surface-associated NRP could mediate attachment of CaOx to the renal tubule epithelium, thereby causing retention of crystals that might eventually become kidney stones.Several groups of investigators have suggested that an important early event in the formation of kidney stones is the attachment of calcium oxalate (CaOx) crystals to the apical surface of renal tubular epithelium (1-3). Well-polarized, undisturbed tubular epithelial cells in culture demonstrate little capacity for crystal attachment (4 -6). This resistance to attachment may be due to the confinement of molecules with crystal-binding properties to domains other than the apical membrane. When tight junctions between cells are disrupted in the course of cellular proliferation or migration or when cells are exposed to a number of different agents, apical membranes seem to express constituents with affinity for CaOx.Nucleolin-related protein (NRP) is a surface-associated protein of cultured inner medullary collecting duct (IMCD) cells that selectively adsorbs to CaOx and binds to membrane skeletal elements in a Ca-dependent manner (7). NRP has a highly acidic region composed of 62% Asp and Glu residues (135KNGKNAKKEDSDEEDDDDSEEEDEEDEDEEDEFE PTVMKAAAAAPAS-DEEEDDEEDDDEDDDEEDEDED-EDDSEEEAMETTPAKGKKAPVKAVPVKAKSTAEE-DEEEDDEDEEDDEE...

show abstract

Cell type-specific acquired protection from crystal adherence by renal tubule cells in culture

Cited by 63 publications

References 22 publications

Annexin II Is Present on Renal Epithelial Cells and Binds Calcium Oxalate Monohydrate Crystals

Annexin II Is Present on Renal Epithelial Cells and Binds Calcium Oxalate Monohydrate Crystals

Unconventional Chemiosmotic Coupling of NHA2, a Mammalian Na+/H+ Antiporter, to a Plasma Membrane H+ Gradient

An Acidic Peptide Sequence of Nucleolin-Related Protein Can Mediate the Attachment of Calcium Oxalate to Renal Tubule Cells

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