Identification of hyaluronan as a crystal-binding molecule at the surface of migrating and proliferating MDCK cells

Verkoelen, Carl F.; Boom, Burt G. van der; Romijn, Johannes C.

doi:10.1046/j.1523-1755.2000.00262.x

Cited by 101 publications

(35 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The finding that the enzymatic removal of the PCMs from MDCK-I cells only leads to a 50% reduction in crystal binding suggests the presence of apical membrane CBMs beneath the coats. Previously, we have demonstrated that at confluence not only HA disappears from the MDCK-I cell surface, but since these cells practically become nonadherent, apparently also the CBMs that were located underneath the coat [7]. Most likely the latter group of CBMs represents epithelial-polarity-related plasma membrane components which are translocated to the basolateral membrane after the development of a functional epithelium.…”

Section: Discussionmentioning

confidence: 99%

“…Subconfluent cells on inserts were pretreated or not with Streptomyces hyaluronidase in serum-free DMEM at a concentration of 5 U/ml, pH 5.3 at 37°C for 60 min, after which [ 14 C]COM crystal binding was performed as described earlier [7]. Briefly, radiolabeled crystals were added to the cultures and allowed to adhere for 1 h, after which the inserts were extensively rinsed to remove all nonassociated crystals, cut out, and counted in a liquid scintillation counter (Packard, Meriden, Conn., USA).…”

Section: Methodsmentioning

confidence: 99%

“…From these observations, it was speculated that crystal retention in the kidney is caused by some form of tissue damage [6]. The polysaccharide hyaluronan (HA) was subsequently identified as major crystal-binding molecule (CBM) at the surface of renal tubular cells in locomotion [5, 7]. …”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Pericellular Matrix Formation by Renal Tubule Epithelial Cells in Relation to Crystal Binding

Schepers¹,

Asselman²,

Duim³

et al. 2004

Nephron Exp Nephrol

Self Cite

View full text Add to dashboard Cite

Background/Aim: Retention of crystals in the kidney ultimately leads to renal stone formation. Hyaluronan (HA) has been identified as binding molecule for calcium oxalate monohydrate crystals. The association of high molecular mass (M_r) HA with cell surface receptors such as CD44 gives rise to pericellular matrix (PCM) formation by many eukaryotic cells in culture. Here, we study the ability of several renal tubular cell lines to assemble PCMs and to synthesize high-M_r HA during proliferation in relation to crystal retention. Methods: PCM assembly by MDCK-I, MDCK-II, and LLC-PK₁ cells was visualized by particle exclusion assay. Metabolic labeling studies were performed to estimate the cellular production of HA. The expression of CD44 and HA was studied using fluorescent probes, and crystal binding was quantified with radiolabeled calcium oxalate monohydrate. Results: PCMs were formed, and HA was expressed by most MDCK-I and some MDCK-II, but not by LLC-PK₁ cells. All cell types expressed CD44 at their apical surface. MDCK-I and MDCK-II cells secreted, respectively, 14.7 ± 1.6 and 0.5 ± 0.2 pmol [³H]glucosamine incorporated in high-M_r HA, whereas LLC-PK₁ cells did not secrete HA. Streptomyces hyaluronidase treatment significantly decreased crystal binding (µg/cm²) to MDCK-I cells (from 8.6 ± 0.4 to 3.9 ± 0.9), but hardly to MDCK-II cells (from 10.2 ± 0.2 to 9.6 ± 0.1) or LLC-PK₁ cells (from 10.2 ± 0.8 to 9.9 ± 0.3). Conclusions: There are various forms of crystal binding to renal tubular cells in culture. Crystal attachment to MDCK-I and some MDCK-II cells involves PCM assembly that requires high-M_r HA synthesis. HA production and PCM formation do not play a role in crystal binding to LLC-PK₁ and the majority of MDCK-II cells. It remains to be determined which form of binding is involved in renal stone disease.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Pericellular Matrix Formation by Renal Tubule Epithelial Cells in Relation to Crystal Binding

Schepers¹,

Asselman²,

Duim³

et al. 2004

Nephron Exp Nephrol

Self Cite

View full text Add to dashboard Cite

show abstract

“…Carl Verkoelen and his co-workers from the department of Urology of the Erasmus Medical Center Rotterdam started to work on the subject of crystal-cell interaction over ten years ago [5]. They carried out in vitro studies with MDCK-I cells [6][7][8][9], a cell line very like that of the epithelium of the renal distal tubules/collecting ducts [10][11][12][13]. Cells were cultured on porous supports to mimic the in vivo situation; it has been shown the use of these permeable supports allows cells to develop with higher levels of differentiation compared to cells cultured on solid supports [7,14].…”

Section: Previous Workmentioning

confidence: 99%

Hyaluronan and Stone Disease

Asselman¹

2008

AIP Conference Proceedings

View full text Add to dashboard Cite

“…Internalization of COM has been shown to correlate with the degree of cell death, demonstrating the key role of intracellular uptake in COM-induced toxicity to tubular cells [17]. Cellular uptake can be inhibited by various polyanions [18], which appear to decrease the interaction between COM crystals and various negatively charged sites on the cell membrane such as hyaluronan [19], surface glycoproteins [1] and anionic phospholipids, including phosphatidylserine (PS) [20]. In order to understand the binding and uptake of COM by cells, the interaction of COM with various components of the cell membrane has been the subject of intensive research.…”

Section: Introductionmentioning

confidence: 99%

Aluminum Citrate Blocks Toxicity of Calcium Oxalate Crystals by Preventing Binding with Cell Membrane Phospholipids

Guo

Dugas²,

Scates³

et al. 2013

Am J Nephrol

View full text Add to dashboard Cite

Background/Aims: Renal damage from ethylene glycol and primary hyperoxaluria is linked to accumulation of calcium oxalate monohydrate (COM) crystals in the renal proximal tubule (PT). In vitro studies have shown that aluminum citrate (AC), uniquely among citrate salts, blocks COM cytotoxicity to tubular cells. These studies were designed to evaluate the interaction of COM with membrane phospholipids and the ability of AC to reduce COM toxicity by interfering with this interaction. Methods: Interaction of COM with phospholipids was assessed using differential scanning calorimetric analysis of structural changes in specific liposomes. Interaction of COM with cell membranes was studied by measuring binding of radiolabeled crystals by human PT (HPT) cells. Results: Analysis of liposomes prepared from phosphatidylserine (PS) or phosphatidylcholine (PC) showed that COM interfered with the gel-liquid transition of PS liposomes, but not that of PC liposomes. AC reversed the COM-induced changes in liposomal structure. AC inhibited the binding of [¹⁴C]-COM by HPT cells in a concentration-dependent manner. AC blocked COM binding by interacting with the crystal surface and not the cell membrane. Conclusion: These results indicate that AC blocks the binding of COM by PT cells, and consequently its cytotoxicity, by attaching to the surface of the crystal. Thus, AC, or a related compound that works by the same mechanism, could be a useful adjunct therapy to reduce the renal damage produced by severe hyperoxaluria.

show abstract

Identification of hyaluronan as a crystal-binding molecule at the surface of migrating and proliferating MDCK cells

Abstract: These results identify HA as binding molecule for COM crystals at the surface of migrating and proliferating MDCK cells.

Cited by 101 publications

References 31 publications

Pericellular Matrix Formation by Renal Tubule Epithelial Cells in Relation to Crystal Binding

Pericellular Matrix Formation by Renal Tubule Epithelial Cells in Relation to Crystal Binding

Hyaluronan and Stone Disease

Aluminum Citrate Blocks Toxicity of Calcium Oxalate Crystals by Preventing Binding with Cell Membrane Phospholipids

Contact Info

Product

Resources

About