Premium
Comparative Study of Glial Marker Proteins in the Hypoplastic Cerebellum of Jaundiced Gunn Rats
Author(s) -
Aono Sachiko,
Sato Hiroshi,
Semba Reiji,
Kashiwamata Shigeo,
Kato Kanefusa,
Eng Lawrence F.
Publication year - 1988
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 - 10.1111/j.1471-4159.1988.tb02973.x
Subject(s) - glial fibrillary acidic protein , enolase , cerebellum , biology , pathology , endocrinology , medicine , microbiology and biotechnology , immunohistochemistry , immunology
The behavior of marker proteins of glial cells [α‐enolase, β‐S100 protein, and glial fibrillary acidic protein (GFAP)] was investigated quantitatively by using enzyme immunoassay systems during the development of eerebellar hypoplasia in jaundiced Gunn rats. A neuronal marker protein, γ‐enolase, was also measured as a reference. At postnatal day 8 corresponding to the early stage of cerebellar damage, the amount of β‐S100 on a protein basis was significantly higher in jaundiced homozygotes ( jj ) than in control nonjaundiced heterozygotes ( j+ ), whereas no differences in α‐ and γ‐enolases and GFAP were observed between the two groups of rats. At days 15 and 30, which correspond, respectively, to the advanced and late stages of cerebellar damage, the three glial proteins, especially GFAP, were higher and the neuronal protein was lower in the jj rat cerebellum than in the control. These results are consistent with the reported histological observations that neuronal cells are vulnerable and damaged by bilirubin, whereas glial cells seem to be less sensitive. On the other hand, the amounts of β‐S100 and α‐enolase per cerebellum were significantly lower in jj rats at days 15 and 30, as in the case of γ‐enolase, whereas that of GFAP remained at the same level as the control at day 15 and showed a slight but significant decrease at day 30. The possibility is suggested that β‐S100 and GFAP may be available as biochemical indicators of glial cells, especially in the early and advanced stages of eerebellar damage, respectively, but that a‐enolase is less available.