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αB‐crystallin in the rat lens is phosphorylated at an early post‐natal age
Author(s) -
Ito Hidenori,
Iida Kayo,
Kamei Keiko,
Iwamoto Ikuko,
Inaguma Yutaka,
Kato Kanefusa
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00242-2
Subject(s) - phosphorylation , isoelectric focusing , crystallin , microbiology and biotechnology , serine , gel electrophoresis , kinase , western blot , polyacrylamide gel electrophoresis , threonine , sodium dodecyl sulfate , blot , biology , lens (geology) , biochemistry , chemistry , enzyme , gene , paleontology
We determined the developmental changes in the phosphorylation state of αB‐crystallin in lenses from rats at various post‐natal ages by isoelectric focusing gel electrophoresis or sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and a subsequent Western blot analysis of extracts of lenses using antibodies that recognized the carboxy‐terminal sequence or each of the three phosphorylated serine residues (Ser‐19, Ser‐45 and Ser‐59) in αB‐crystallin. Phosphorylated forms of αB‐crystallin were barely detected at birth but they became detectable at 3 weeks of age and reached plateau levels at 8 weeks of age. The phosphorylation of αB‐crystallin at Ser‐45 was observed preferentially. The active form of p44/42 MAP kinase, which is responsible for the phosphorylation of Ser‐45 in αB‐crystallin, also increased in a development‐dependent manner. Thus we found that the developmental increase of the phosphorylation at Ser‐45 of αB‐crystallin in the rat lens was due to the developmental activation of p44/42 MAP kinase.