title: Expression of 27 kDa heat shock protein (Hsp27) in immature rat brain after a cortical aspiration lesion.
abstract: The 27 kDa heat shock protein (Hsp27) is a well-known member of the astroglial response to injury, playing a protective role against oxidative stress, apoptosis, and cytoskeletal destruction. Although several studies have been focused on the damaged adult brain, little is known about Hsp27 expression in the immature brain. In this work, we have examined the spatiotemporal pattern of Hsp27 expression in the normal postnatal rat brain following a cortical aspiration lesion at postnatal day 9. In the immature brain, Hsp27 is mainly observed in the internal capsule, although some scattered cells are also found in the ependyma, the corpus callosum, the septum, and hypothalamic glia limitans. In the internal capsule, Hsp27 expression is developmentally regulated, being significantly decreased from postnatal day 14. After a cortical aspiration lesion, de novo expression of Hsp27 is observed in cortical injured areas as well as in the secondary affected thalamus. In the cortex, expression of Hsp27 is first seen at day 1 postlesion (PL) surrounding the neurodegenerative area, becoming restricted to the glial scar at longer survival times. Although a pulse-like expression of Hsp27 is observed in some microglial cells at day 1 PL, most Hsp27-labeled cells are reactive astrocytes, which show GFAP overexpression and coexpress vimentin from day 3 PL. In the thalamus, astroglial Hsp27 expression is delayed, being first observed at day 5 PL. Thalamic Hsp27-labeled astrocytes do not show vimentin expression. Our observations demonstrate astroglial expression of Hsp27 in areas of tissue damage following postnatal traumatic injury, suggesting an involvement of this cytoskeleton-stabilizing protein in the remodeling processes following postnatal brain damage.
authors.affiliation: Department of Cell Biology, Physiology and Immunology, Unit of Histology, Faculty of Medicine, Autonomous University of Barcelona, Bellaterra, Spain.
authors.forename: O
authors.initials: O
authors.lastname: Sanz
authors.forename: L
authors.initials: L
authors.lastname: Acarin
authors.forename: B
authors.initials: B
authors.lastname: González
authors.forename: B
authors.initials: B
authors.lastname: Castellano
mesh_terms: D000375:Aging / Q000378:metabolism*; D000818:Animals; D001253:Astrocytes / Q000378:metabolism*; D001921:Brain / Q000254:growth & development / Q000378:metabolism / Q000473:pathology; D001930:Brain Injuries / Q000378:metabolism* / Q000503:physiopathology; D002540:Cerebral Cortex / Q000254:growth & development* / Q000293:injuries* / Q000378:metabolism; D005260:Female; D018507:Gene Expression Regulation, Developmental / Q000502:physiology; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D005911:Gliosis / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D007150:Immunohistochemistry; D008297:Male; D017628:Microglia / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism*; D051381:Rats; D020318:Rats, Long-Evans; D014746:Vimentin / Q000378:metabolism
chemical_list: D005904:Glial Fibrillary Acidic Protein; D055551:HSP27 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; D009363:Neoplasm Proteins; D014746:Vimentin