Differential synthesis of rat lens proteins during development.
Developmental regulation of crystallin protein synthesis was observed in rat lenses between embryonic day 19 and postnatal day 21. Studies on lenses incubated in [35S]-methionine and on lens messenger RNAs translated in a reticulocyte lysate showed that several new polypeptides were synthesized in the lens beginning approximately 1 week after birth. One new polypeptide which had a molecular weight of 27 000 comigrated with the beta crystallins on SDS-PAGE and became a predominant component in older lenses. By crossed rocket immunoelectrophoresis and isoelectric focusing, synthesis of several native beta crystallins and one gamma crystallin was detected only in the postnatal lens. Many crystallin proteins were synthesized in the embryonic and the postnatal lens and did not change during the time period studied. These data suggest a differential regulation of the crystallin proteins during development. It appears that the lens undergoes a transition from embryonic to adult crystallin expression during the first weeks after birth. Factors such as maturation of the retina may be necessary for this transition.
D000375:Aging; D000818:Animals; D003459:Crystallins / Q000096:biosynthesis*; D004591:Electrophoresis, Polyacrylamide Gel; D007123:Immunoelectrophoresis, Two-Dimensional; D007525:Isoelectric Focusing; D007908:Lens, Crystalline / Q000196:embryology / Q000254:growth & development / Q000378:metabolism*; D008970:Molecular Weight; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000096:biosynthesis; D051381:Rats; D011919:Rats, Inbred Strains
D003459:Crystallins; D012333:RNA, Messenger