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Titolo:
Immunodetection of Parkin protein in vertebrate and invertebrate brains: acomparative study using specific antibodies
Autore:
Horowitz, JM; Vernace, VA; Myers, J; Stachowiak, MK; Hanlon, DW; Fraley, GS; Torres, G;
Indirizzi:
Medaille Coll, Buffalo, NY 14214 USA Medaille Coll Buffalo NY USA 14214Medaille Coll, Buffalo, NY 14214 USA SUNY Buffalo, Mol & Struct Neurobiol & Gene Therapy Program, Buffalo, NY 14214 USA SUNY Buffalo Buffalo NY USA 14214 Therapy Program, Buffalo, NY 14214 USA SUNY Buffalo, Dept Anat & Cell Biol, Buffalo, NY 14214 USA SUNY Buffalo Buffalo NY USA 14214 Anat & Cell Biol, Buffalo, NY 14214 USA Oncogene Res Prod, Cambridge, MA 02142 USA Oncogene Res Prod Cambridge MAUSA 02142 es Prod, Cambridge, MA 02142 USA Washington State Univ, Program Neurosci, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 eurosci, Pullman, WA 99164 USA Washington State Univ, Dept Vet & Comparat Anat Pharmacol & Physiol, Pullman, WA 99164 USA Washington State Univ Pullman WA USA 99164 Physiol, Pullman, WA 99164 USA
Titolo Testata:
JOURNAL OF CHEMICAL NEUROANATOMY
fascicolo: 1, volume: 21, anno: 2001,
pagine: 75 - 93
SICI:
0891-0618(200101)21:1<75:IOPPIV>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECESSIVE JUVENILE PARKINSONISM; ANTIGEN RETRIEVAL; RAT-BRAIN; GENE; CLONING; DISEASE; IDENTIFICATION; NEUROPEPTIDES; DELETIONS; MUTATIONS;
Keywords:
aldehyde fixatives; evolution; antigen retrieval; Drosophila; dopamine; Parkinson's disease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Torres, G SUNY Buffalo, Behav Neurosci Program, Dept Psychol, Pk Hall Box 604110, Buffalo, NY 14260 USA SUNY Buffalo Pk Hall Box 604110 Buffalo NY USA 14260 Y 14260 USA
Citazione:
J.M. Horowitz et al., "Immunodetection of Parkin protein in vertebrate and invertebrate brains: acomparative study using specific antibodies", J CHEM NEUR, 21(1), 2001, pp. 75-93

Abstract

Parkin is an intracellular protein that plays a significant role in the etiopathogenesis of autosomal recessive juvenile parkinsonism. Using immunoblot methods, we found Parkin isoforms varying from 54 to 58 kDa in rat, mouse, bird, frog and fruit-fly brains. Immunocytochemical studies carried out in rats, mice and birds demonstrated multiple cell types bearing the phenotype for Parkin throughout telencephalic, diencephalic, mesencephalic and metencephalic brain structures. While in some instances Parkin-containing neurons tended to be grouped into clusters, the majority of these labeled nerve cells were widely scattered throughout the neuraxis. The topographical distribution and organizational pattern of Parkin within major functional brain circuits was comparable in both rats and mice. However, the subcellular localization of Parkin was found to vary significantly as a function of antibody reactivity. A consistent cytoplasmic labeling for Parkin was observedin rodent tissue incubated with a polyclonal antibody raised against the human Parkin protein and having an identical amino-acid sequence with that of the rat. In contrast, rodent tissue alternately incubated with a polyclonal antibody raised against a different region of the same human Parkin protein but having 10 mismatched amino-acid sequence changes with those of the rat and mouse, resulted in nuclear labeling for Parkin in rat but not mouseneurons. This difference in epitope recognition, however, was reversed when mouse brain tissue was heated at 80 degreesC, apparently unmasking targetepitopes against which the antisera were directed. Collectively, these results show a high degree of conservation in the cellular identity of Parkin in animals as different as drosophilids and mammals and points to the possibility that the biochemical specificities of Parkin, including analogous functional roles, may have been conserved during the course of evolution. (C)2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 20/06/19 alle ore 17:26:26