Premium
The Distribution and Biochemical Properties of a Cdc2‐Related Kinase, KKIALRE, in Normal and Alzheimer Brains
Author(s) -
Yen ShuHui,
Kenessey Agnes,
Lee Sunhee C.,
Dickson Dennis W.
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.65062577.x
Subject(s) - biology , astrocyte , hyperphosphorylation , gene isoform , cerebellum , neuroglia , alzheimer's disease , gliosis , protein kinase a , kinase , microbiology and biotechnology , biochemistry , central nervous system , pathology , endocrinology , neuroscience , medicine , disease , gene
Abstract: The biochemical properties and distribution of a Cdc2‐related kinase, KKIALRE, were studied in brain tissues and cultured cells with antibodies to a subregion of KKIALRE protein deduced from cDNA. In adult human brain, the KKIALRE‐immunoreactive protein consisted of four or five isoforms having a molecular size of 40–52 kDa, whereas in fetal brain, there was one protein of ∼48 kDa. Cultured astrocytes, neuroblastoma cells, and mouse brains contained the fetal form of KKIALRE protein. KKIALRE‐immunoreactive proteins were capable of phosphorylating histone and synthetic peptides with the X‐Ser‐Pro‐X motif, indicating that these proteins belong to the proline‐directed Ser/Thr protein kinase family. The KKIALRE immunoreactivity was detected primarily in fibrous astrocytes in white matter and perivascular and subpial spaces, as well as in Bergmann glia in the cerebellum. In fetal brains radial glia were weakly immunoreactive. Reactive astrocytes were more intensely labeled than other glia. Neurons in normal brains and brains with Alzheimer's disease (AD) displayed no KKIALRE immunoreactivity. KKIALRE immunoreactivity was similar in neurons with and without neurofibrillary tangles. The results indicate that in CNS, the KKIALRE protein is mainly a glial protein that is up‐regulated in gliosis and that it probably plays no role in the hyperphosphorylation of τ in AD brains.