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Phosphorylation of α‐crystallin B in Alexander's disease brain
Author(s) -
Mann Eric,
McDermott Martin J.,
Goldman James,
Chiesa Raúl,
Spector Abraham
Publication year - 1991
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 - 10.1016/0014-5793(91)81359-g
Subject(s) - phosphorylation , crystallin , chemistry , microbiology and biotechnology , biochemistry , biology
The phosphorylation of α‐crystallin B was studied in homogenates of autopsy samples of brain tissue from patients with Alexander's disease, a condition characterized by over‐expression of this protein. After incubation in the presence of [γ‐ 32 P]ATP and cAMP the homogenates were analyzed by two‐dimensional electrophoresis, (isoelectric focusing followed by SDS‐PAGE). Three major polypeptides having the same molecular weight as bovine lens α‐crystallin B and pIs 7.1, 6.9 and 6.7 were detected in the Coomassie blue stained gels. These three polypeptides were recognized by an α‐crystallin B‐specific antiserum in Western blots. The polypeptides with pIs 7.1 and 6.7 co‐migrated in isoelectric focusing gels with bovine lens αB and its phosphorylated form αBp, respectively. Radioautography of the two‐dimensional gels demonstrated the presence of 32 P in the most acidic polypeptide. The results demonstrate the occurrence of αB phosphorylation in Alexander's disease brain tissue.