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A novel peroxisomal enzyme, D‐3‐hydroxyacyl‐CoA dehydratase/D‐3‐hydroxyacyl‐CoA dehydrogenase bifunctional protein: Its expression in the developing human brain
Author(s) -
Itoh Masayuki,
Suzuki Yasuyuki,
Takashima Sachio
Publication year - 1999
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/(sici)1097-0029(19990615)45:6<383::aid-jemt5>3.0.co;2-7
Subject(s) - phosphofructokinase 2 , bifunctional , biology , biochemistry , white matter , human brain , medicine , enzyme , endocrinology , neuroscience , radiology , magnetic resonance imaging , catalysis
D‐bifunctional protein, which is a newly recognized peroxisomal enzyme (D‐3‐hydroxyacyl‐CoA dehydratase/D‐3‐hydroxyacyl‐CoA dehydrogenase), demonstrates a characteristic development of pattern in the human brain. At 13 gestational weeks (GW), D‐bifunctional protein immunoreactivity first appeared in the brain. Each neuron exhibited increased immunoreactivity along with growth in size as age increased and size with age. Glial cells in the white matter showed immunoreactivity after 30 GW. On the other hand, the L‐bifunctional protein immunoreactivity was reported in neurons from 23 or 25 GW and in the white matter from 12 or 14 GW. Because of polymicrogyria in conditions such as infantile Refsum disease and infantile adrenoleukodystrophy, peroxisomal enzymes are thought to play an important role in neuronal migration and possibly myelination. D‐bifunctional protein may be relevant to neuronal migration and L‐bifunctional protein may be involved in axonal growth and synaptic development. This study is designed to access the ontogeny of D‐bifunctional protein in the human brain. Microsc. Res. Tech. 45:383–388, 1999. © 1999 Wiley‐Liss, Inc.