Changes in chick lens proteins with aging: Paper from the symposium “lens proteins and related subjects,” Ghent, Belgium, June 1967

Abstract

The distribution of proteins in the whole and different parts of the chick lens was studied by immunological and electrophoretic methods. In the lenses of 15-day-old embryos, α-, β- and δ-crystallins were found in the annular pad cells and cortical fiber cells. The nuclear fiber cells contained principally δ-crystallin. In 10-day-old animals only α- and β- crystallins were found in the annular pad cells, while all proteins were present in the fiber cells. In adult animal (1–2 years old) δ-crystallin was no longer present in the cortical fiber cells. Thus, with increased age, there is a disappearance of δ-crystallin, affecting first the short fiber cells of the equatorial region and then the superficial cortical fiber cells. α- Crystallin undergoes slight changes during development. However, in the annular pad cells and cortical fiber cells, it accumulates in relatively high concentration and exhibits differences in mobility. Protein ontogeny during postnatal development is also characterized by a progressive increase of anionic β-crystallins. These last fractions seem to be a typical feature of the highly differentiated lens fibers. It may be suggested that cationic β-crystallins are synthesized mainly in the young lens fibers.