title: Expression of reelin in adult mammalian blood, liver, pituitary pars intermedia, and adrenal chromaffin cells.
abstract: Reelin regulates telencephalic and cerebellar lamination during mammalian development and is expressed in several structures of the adult brain; however, only traces of reelin were believed to be in peripheral tissues. Because reelin structurally resembles extracellular matrix proteins, and because many of these proteins are expressed in blood, we hypothesized that reelin also might be detectable in the circulation. Reelin (420 kDa) and two reelin-like immunoreactive bands (310 and 160 kDa) are expressed in serum and platelet-poor plasma of rats, mice, and humans, but these three bands were not detectable in serum of homozygous reeler (rl/rl) mice. Reelin plasma levels in heterozygous (rl/+) mice were half of those in wild-type littermates. Western blotting and immunocytochemistry using antireelin mAbs indicated that reelin-like immunoreactivity was expressed in a subset of chromaffin cells within the rat adrenal medulla and in a subset of cells coexpressing alpha-melanocyte-stimulating hormone within the pituitary pars intermedia. However, surgical removal of adrenal or pituitary failed to decrease the amount of reelin (420-kDa band) expressed in serum. Adult liver expressed one-third of the reelin mRNA concentration expressed in adult mouse cerebral cortex. Full-length reelin protein was detectable in liver extracts in situ; acutely isolated liver cells also secreted full-length reelin in vitro. Liver appears to be a prime candidate to produce and maintain the circulating reelin pool. It now becomes relevant to ask whether circulating reelin has a physiologic role on one or more peripheral target tissues.
authors.affiliation: Department of Psychiatry and Psychiatric Institute, University of Illinois at Chicago, M/C 912, 1601 West Taylor Street, Chicago, IL 60612, USA. smalheiser@psych.uic.edu
authors.forename: N R
authors.initials: NR
authors.lastname: Smalheiser
authors.forename: E
authors.initials: E
authors.lastname: Costa
authors.forename: A
authors.initials: A
authors.lastname: Guidotti
authors.forename: F
authors.initials: F
authors.lastname: Impagnatiello
authors.forename: J
authors.initials: J
authors.lastname: Auta
authors.forename: P
authors.initials: P
authors.lastname: Lacor
authors.forename: V
authors.initials: V
authors.lastname: Kriho
authors.forename: G D
authors.initials: GD
authors.lastname: Pappas
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D000313:Adrenal Medulla / Q000378:metabolism*; D000818:Animals; D015816:Cell Adhesion Molecules, Neuronal / Q000096:biosynthesis* / Q000097:blood; D002540:Cerebral Cortex / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000096:biosynthesis* / Q000097:blood; D005260:Female; D008099:Liver / Q000378:metabolism*; D051379:Mice; D008818:Mice, Neurologic Mutants; D009419:Nerve Tissue Proteins / Q000032:analysis; D009928:Organ Specificity; D010902:Pituitary Gland / Q000378:metabolism*; D012333:RNA, Messenger / Q000096:biosynthesis; D051381:Rats; D017207:Rats, Sprague-Dawley; D000091042:Reelin Protein; D012697:Serine Endopeptidases
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D015816:Cell Adhesion Molecules, Neuronal; C115785:DAB1 protein, human; D016326:Extracellular Matrix Proteins; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D000091042:Reelin Protein; C000717129:Reln protein, rat; C000717127:RELN protein, human; C000717128:Reln protein, mouse; D012697:Serine Endopeptidases