Action of elastase, collagenase and other enzymes upon linkages between stereocilia in the guinea-pig cochlea

Acta Otolaryngol. Jul-Aug 1990;110(1-2):37-45. doi: 10.3109/00016489009122513.


Enzymes, which degrade elements of the extracellular environment, were studied for their actions upon stereocilia and their cross-linkages by scanning electron microscopy. Chondroitinase, hyaluronidase and keratanase, which attack carbohydrate moieties of the extracellular matrix, had little effect upon hair bundles. Collagenase and plasmin (fibrinolysin) also had only marginal effects. Elastase produced dramatic effects upon hair bundles. Both lateral and tip links were degraded resulting in separation and splaying of stereocilia. Many stereocilia showed no marked loss of rigidity, although some were bent or kinked. In general, inner hair cells were the most susceptible to elastase followed by row 3, row 2, row 1 of the outer hair cells. The proteolytic enzyme trypsin did not noticeably disrupt the hair bundles. Protease caused loss of rigidity and fracture of stereocilia resulting in considerable collapse of hair bundles. Crosslinkages between stereocilia were less noticeably degraded. These results indicate that both lateral and tip links of stereocilia comprise a proteinaceous moiety which could be elastin or some chemically related structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Endopeptidases / metabolism
  • Glycoside Hydrolases*
  • Guinea Pigs
  • Hair Cells, Auditory / enzymology*
  • Hair Cells, Auditory / ultrastructure
  • Hyaluronoglucosaminidase / metabolism
  • Microbial Collagenase / metabolism*
  • Microscopy, Electron, Scanning
  • Pancreatic Elastase / metabolism*
  • Trypsin / metabolism
  • beta-Galactosidase / metabolism


  • Glycoside Hydrolases
  • keratan-sulfate endo-1,4-beta-galactosidase
  • beta-Galactosidase
  • Hyaluronoglucosaminidase
  • Endopeptidases
  • Pancreatic Elastase
  • Trypsin
  • Microbial Collagenase