May 2007
Volume 48, Issue 13
ARVO Annual Meeting Abstract  |   May 2007
Is B-Crystallin a Soluble Protein?
Author Affiliations & Notes
  • S. P. Bhat
    Ophthalmology, Jules Stein Eye Institute UCLA, Geffen School of Medicine, California
    Brain Research Institute and Molecular Biology Institute, University of California, Los Angeles, California
  • R. K. Gangalum
    Ophthalmology, Jules Stein Eye Institute UCLA, Los Angeles, California
  • Footnotes
    Commercial Relationships S.P. Bhat, None; R.K. Gangalum, None.
  • Footnotes
    Support NIH(NEI) Grant EY006044 and Research to Prevent Blindness Inc.,
Investigative Ophthalmology & Visual Science May 2007, Vol.48, 1528. doi:
  • Views
  • Share
  • Tools
    • Alerts
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      S. P. Bhat, R. K. Gangalum; Is B-Crystallin a Soluble Protein?. Invest. Ophthalmol. Vis. Sci. 2007;48(13):1528. doi:

      Download citation file:

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

  • Supplements

Purpose:: Among crystallins, a small fraction of α-crystallins have been historically known to associate with membranous components in the cell. We have recently demonstrated a significant association of αB-crystallin with perinulcear Golgi in the human Glioblastoma U373 cell line. Additional studies have established that αB-crystallin is also associated with Golgi in the ocular lens. In order to understand the functional import of the association of αB-crystallin with the membrane (in the backdrop of the dogma that this protein belongs to the soluble compartment); present studies were conducted to investigate the status of this protein in various membrane fractions isolated from the developing ocular lens.

Methods:: Rat lenses of various ages were used for this study. Discontinuous sucrose density gradients were used to enrich for Golgi membrane and high density vesicular membrane fractions. Proteins were identified by immunoblotting. Light and confocal microscopy were used to examine the status of αB-crystallin in the various cellular and metabolic compartments of the ocular lens.

Results:: In this investigation we show that in the fetal and early post-natal rat lens almost all of αB-crystallin is associated with the Golgi membrane fraction. Immunolocalization, coupled with confocal microscopy, reveals a polar location for αB-crystallin in the epithelium; this location abuts the apical interface between fiber cells and the overlying epithelium. Of special note is the presence of αB-crystallin in perinuclear Golgi streaks in differentiating lens fiber cells, which contain elongating, degenerating nuclei. This association is sensitive to Brefeldin A, a fungal metabolite, which disorganizes Golgi. Comparisons of the distribution of αB-crystallin in two membrane fractions i.e., the vesicular and the Golgi fractions reveal that the vesicular: Golgi ratio increases appreciably from fetal to post natal life suggesting a possible involvement of Golgi -associated proteins and processes in fiber cell growth and maturation.

Conclusions:: (a) Much against the perception that lens is ‘a crystallin-crammed bag’, the location of αB-crystallin (and therefore, the location of Golgi) is compartmentalized in the lens epithelium; in differentiating fiber cells αB-crystallin is present in Golgi streaks that follow the nuclear morphology. (b) In the early developing lens αB-crystallin must be regarded as a membrane associated protein.

Keywords: crystallins • development • protein structure/function 

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.