科研之友
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摘要
PURPOSE. All crystallins have non-crystallin catalytic functions. Because catalytic functions do not require large concentrations of protein, as are seen in the lens, there is a perception of dichotomy in the catalytic/physiological function of crystallins within and outside the lens. The status of alpha B-crystallin, a ubiquitously expressed small heat shock protein (and a crystallin) in the ocular lens, was investigated. METHODS. Discontinuous sucrose density gradients were used for fractionation of Golgi membranes and vesicles. Light microscopy and confocal microscopy were used for immunolocalization in cultured cells and the native lens. RESULTS. alpha B-crystallin is highly organized, as indicated by its polar presence in the apical Golgi in lens epithelium and in the perinuclear Golgi streaks in differentiating lens fiber cells. Assessment of the distribution of alpha B-crystallin in Golgi-enriched and vesicular fractions (characterized by the presence of Golgi membrane protein GM130 and vesicle coat protein gamma COP) in the developing lens reveal a gradual transition from Golgi to vesicular fraction, concomitant with the appearance of alpha B-crystallin as a "soluble" protein. CONCLUSIONS. These data demonstrate that alpha B-crystallin, known to be a soluble protein, starts life as a Golgi-associated membrane protein in the fetal and early postnatal lens and that the developmentally controlled physical state of the Golgi determines the status of this protein in the lens. These findings also show the similarity in the localization/physiological function of alpha B-crystallin within and outside the ocular lens and suggest that non-crystallin/catalytic function is an innate component of the expression of a crystallin in the lens. (Invest Ophthalmol Vis Sci. 2009;50:3283-3290) DOI: 10.1167/iovs.08-3052
- 出版日期2009-7
