Protein synthesis during corneal epithelial wound healing.
Previous investigations have shown that corneal epithelium, migrating to cover a wound, synthesizes protein and glycoprotein at a faster rate than does normal stratified epithelium. The authors have found that the maximal rate of synthesis, as indicated by the incorporation of leucine and glucosamine, occurs 16 hr after wounding, 6 hr before wound closure. A comparison of total protein and protein synthesized during migration indicates that the increased synthesis is the result of the enhanced synthesis of many of the proteins present in unwounded epithelia. However, one protein band with a molecular weight of 110 K daltons was present to a much greater extent in migrating tissue than in normal epithelium. A time course analysis indicates that this band is apparent during migration and is not present either before wounding or 24 hr after wound closure.
D000818:Animals; D001345:Autoradiography; D002465:Cell Movement; D003078:Colchicine / Q000494:pharmacology; D003315:Cornea / Q000378:metabolism / Q000502:physiology; D065306:Corneal Injuries; D004848:Epithelium / Q000378:metabolism / Q000502:physiology; D005136:Eye Proteins / Q000096:biosynthesis*; D007930:Leucine / Q000378:metabolism; D008938:Mitosis / Q000187:drug effects; D009924:Organ Culture Techniques; D051381:Rats; D011919:Rats, Inbred Strains; D014945:Wound Healing
D005136:Eye Proteins; D007930:Leucine; D003078:Colchicine