Age-related changes of calpain II and alpha-crystallin in the lens of hereditary cataract (Nakano) mouse.
The age-related changes of calpain II (high-Ca2+-requiring form of Ca2+-dependent cysteine proteinase; EC 3.4.22.17) and alpha-crystallin in the lens of hereditary cataract (Nakano; cac/cac) mouse were studied. Before the onset of the cataract formation, i.e., at the end of the 2nd week after birth, the calpain activity in Nakano mice was as high as that in the control ICR mice, but it decreased rapidly as the cataract progressed to completion during the 4th and the 12th week. Marked degradation of lens proteins ensued between the 2nd and the 4th weeks, and one of these proteins was identified, using monospecific antibodies, as B chain of alpha-crystallin. A chain of alpha-crystallin was not degraded in vivo, in contrast to its known susceptibility to calpain in vitro. The present data suggest that in Nakano mice, calpain may be involved in the onset or early stage of the cataract formation.
D000375:Aging; D000818:Animals; D002154:Calpain / Q000378:metabolism* / Q000494:pharmacology; D002386:Cataract / Q000235:genetics* / Q000378:metabolism; D003459:Crystallins / Q000378:metabolism*; D005136:Eye Proteins / Q000032:analysis; D007908:Lens, Crystalline / Q000032:analysis; D051379:Mice; D008813:Mice, Inbred ICR; D008815:Mice, Inbred Strains
D003459:Crystallins; D005136:Eye Proteins; D002154:Calpain