Lens crystallin changes associated with amphibian metamorphosis: involvement of a beta-crystallin polypeptide.
Lens crystallins isolated from the tadpole and frog lenses were compared with regard to the developmental changes of crystallin compositions. The major changes during the process of metamorphosis were (1) the total contents of alpha- and gamma-crystallins decrease from more than 70% to less than 60% and (2) one of the major beta-crystallin polypeptides increases from less than 1% to about 6% and (3) an amphibian-specific rho-crystallin also increases from about 6% to more than 10% of total soluble proteins of the lens. We have characterized the metamorphosis-dependent beta-crystallin polypeptide by peptide mapping and sequence determination of the protease-digested fragments. This polypeptide showed very high sequence homology to that of the major beta Bp-crystallin chain reported for the mammalian lenses. The changes of the relative abundance of various crystallins and the gradually-elevated levels of the expression of this beta Bp-like crystallin in the developing lens during metamorphosis may also have some bearing on the maintenance of lens stability in the adult frog lenses.
Jiang
Y J
YJ
Institute of Biochemical Sciences, National Taiwan University, Taipei, R.O.C.
Chiou
S H
SH
Chang
W C
WC
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003459:Crystallins / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007908:Lens, Crystalline / Q000254:growth & development*; D008675:Metamorphosis, Biological; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011892:Rana catesbeiana; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin
D003459:Crystallins; D010446:Peptide Fragments; D014357:Trypsin