July 1987
Volume 28, Issue 7
Articles  |   July 1987
Inhibition of beta-crystallin cross-linking in the Ca2+-treated lens.
Investigative Ophthalmology & Visual Science July 1987, Vol.28, 1218-1222. doi:
  • Views
  • PDF
  • Share
  • Tools
    • Alerts
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      L Lorand, S M Conrad, P T Velasco; Inhibition of beta-crystallin cross-linking in the Ca2+-treated lens.. Invest. Ophthalmol. Vis. Sci. 1987;28(7):1218-1222.

      Download citation file:

      © ARVO (1962-2015); The Authors (2016-present)

  • Supplements

beta-Crystallin dimers of approximately 55,000 weight are among the early products of protein cross-linking in Ca2+-treated rabbit lens, caused by the activation of intrinsic transglutaminase; formation of the cross-linked species can be blocked by 75 mM histamine (Lorand et al, Biochemistry, 24:1525-1531, 1985). As an extension of this work, we initiated a search for more specific inhibitors of cross-linking in this system. Of the compounds tested so far, hydroxylamine, methoxyamine, bisaminoxypropane and aminoacetonitrile were particularly effective, inhibiting the generation of the cross-linked dimer in the 5 to 10 mM concentration range during a 4 hr treatment of the lens with Ca2+-ions.


This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.