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Related Experiment Videos

Urinary crystallization inhibitors do not prevent crystal binding.

Marieke S J Schepers1, Burt G van der Boom, Johannes C Romijn

  • 1Department of Urology, Erasmus University Rotterdam, Rotterdam, The Netherlands.

The Journal of Urology
|March 26, 2002
PubMed
Summary

Urinary proteins do not prevent calcium oxalate crystal binding to kidney cells, suggesting renal tubular epithelium surface properties are key to kidney stone formation. This impacts understanding of crystal retention in renal stone disease.

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Area of Science:

  • Nephrology
  • Biochemistry
  • Cell Biology

Background:

  • Renal stone formation involves crystal retention in the kidney.
  • Calcium oxalate monohydrate (COM) crystal binding to renal cells is developmentally regulated.
  • Hyaluronan (HA) is involved in COM crystal adherence to certain kidney cell models.

Purpose of the Study:

  • To investigate the influence of urinary substances, including glycoprotein inhibitors, on COM crystal binding to renal tubular epithelial cells.
  • To determine if urinary protein coatings affect crystal adherence to different kidney cell types and immobilized HA.

Main Methods:

  • Studied COM crystal binding to Madin Darby canine kidney strain I (MDCK-I) and LLC-PK1 cells.
  • Utilized [14C] COM pretreated with urine from healthy volunteers.

Related Experiment Videos

  • Analyzed crystal coating with urine-derived proteins using SDS-PAGE and Western blot.

    • Main Results:

    • Pretreated COM crystals were coated with crystallization inhibitors.
    • This protein coat did not significantly affect crystal binding to MDCK-I or LLC-PK1 cells.
    • Urine treatment significantly reduced adherence of crystals to immobilized HA.

    Conclusions:

    • Crystal adherence to pericellular matrices may involve more than just HA.
    • Coating COM crystals with urinary glycoproteins does not prevent renal retention.
    • Calcium oxalate crystal retention likely depends predominantly on renal tubular epithelial cell surface properties.