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1.
Toxicol Pathol ; 46(1): 101-106, 2018 01.
Artigo em Inglês | MEDLINE | ID: mdl-28992726

RESUMO

Delivery of therapy to the cochlea is a challenge and limits the efficacy of therapies meant to treat hearing loss, reverse tinnitus, and protect hearing from chemotherapy regimens. Magnetic injection is a technique that uses magnetic fields to inject nanoparticles from the middle ear into the cochlea, where they can then elute therapy to treat hearing disorders. To evaluate the safety of this treatment in the middle ear, 30 rats were subdivided into 6 groups and treated by single or multiple intratympanic injections of saline, prednisolone, nanoparticles, or nanoparticles loaded with prednisolone. A specially designed magnet array was used to magnetically inject the particles from the middle ear to the cochlea. Treatment began at study day 0, and animals were euthanized on study day 2, 30, or 90. Temporal bones were collected and prepared for histopathological examination. Intratympanic administration of magnetic nanoparticles and/or prednisolone resulted in minimal to mild inflammatory changes in all treated groups. The incidence and severity of the inflammatory changes observed appeared slightly increased in animals administered nanoparticles, with or without prednisolone, when compared to animals administered prednisolone alone. At study day 90, there was partial reversibility of the findings noted at study day 2 and 30. Repeat administration did not appear to cause greater inflammatory changes.


Assuntos
Anti-Inflamatórios/administração & dosagem , Cóclea , Sistemas de Liberação de Medicamentos/métodos , Fenômenos Magnéticos , Nanopartículas/administração & dosagem , Prednisolona/administração & dosagem , Animais , Compostos Férricos/administração & dosagem , Masculino , Ratos , Ratos Long-Evans
2.
J Magn Magn Mater ; 393: 243-252, 2015 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-26120240

RESUMO

This article presents a method to investigate how magnetic particle characteristics affect their motion inside tissues under the influence of an applied magnetic field. Particles are placed on top of freshly excised tissue samples, a calibrated magnetic field is applied by a magnet underneath each tissue sample, and we image and quantify particle penetration depth by quantitative metrics to assess how particle sizes, their surface coatings, and tissue resistance affect particle motion. Using this method, we tested available fluorescent particles from Chemicell of four sizes (100 nm, 300 nm, 500 nm, and 1 µm diameter) with four different coatings (starch, chitosan, lipid, PEG/P) and quantified their motion through freshly excised rat liver, kidney, and brain tissues. In broad terms, we found that the applied magnetic field moved chitosan particles most effectively through all three tissue types (as compared to starch, lipid, and PEG/P coated particles). However, the relationship between particle properties and their resulting motion was found to be complex. Hence, it will likely require substantial further study to elucidate the nuances of transport mechanisms and to select and engineer optimal particle properties to enable the most effective transport through various tissue types under applied magnetic fields.

3.
Neurotherapeutics ; 10(4): 840-51, 2013 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-23963789

RESUMO

The pathogenic mechanism(s) contributing to loss of dopamine neurons in Parkinson's disease (PD) remain obscure. Leucine-rich repeat kinase 2 (LRRK2) mutations are linked, as a causative gene, to PD. LRRK2 mutations are estimated to account for 10% of familial and between 1 % and 3 % of sporadic PD. LRRK2 proximate single nucleotide polymorphisms have also been significantly associated with idiopathic/sporadic PD by genome-wide association studies. LRRK2 is a multidomain-containing protein and belongs to the protein kinase super-family. We constructed two inducible dopaminergic cell lines expressing either human-LRRK2-wild-type or human-LRRK2-mutant (G2019S). Phenotypes of these LRRK2 cell lines were examined with respect to cell viability, morphology, and protein function with or without induction of LRRK2 gene expression. The overexpression of G2019S gene promoted (1) low cellular metabolic activity without affecting cell viability, (2) blunted neurite extension, and (3) increased phosphorylation at S910 and S935. Our observations are consistent with reported general phenotypes in LRRK2 cell lines by other investigators. We used these cell lines to interrogate the biological function of LRRK2, to evaluate their potential as a drug-screening tool, and to investigate screening for small hairpin RNA-mediated LRRK2 G2019S gene knockdown as a potential therapeutic strategy. A proposed LRRK2 kinase inhibitor (i.e., IN-1) decreased LRRK2 S910 and S935 phosphorylation in our MN9DLRRK2 cell lines in a dose-dependent manner. Lentivirus-mediated transfer of LRRK2 G2019S allele-specific small hairpin RNA reversed the blunting of neurite extension caused by LRRK2 G2019S overexpression. Taken together, these inducible LRRK2 cell lines are suitable reagents for LRRK2 functional studies, and the screening of potential LRRK2 therapeutics.


Assuntos
Linhagem Celular , Doença de Parkinson/terapia , Proteínas Serina-Treonina Quinases/genética , Sobrevivência Celular/genética , Neurônios Dopaminérgicos/metabolismo , Humanos , Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina , Doença de Parkinson/genética , Doença de Parkinson/metabolismo , Fosforilação , Proteínas Serina-Treonina Quinases/metabolismo
4.
J Neuroimmune Pharmacol ; 8(1): 94-117, 2013 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-23054368

RESUMO

Parkinson's disease (PD) is the second most common age-related neurodegenerative disorder typified by tremor, rigidity, akinesia and postural instability due in part to the loss of dopamine within the nigrostriatal system. The pathologic features of this disorder include the loss of substantia nigra dopamine neurons and attendant striatal terminals, the presence of large protein-rich neuronal inclusions containing fibrillar α-synuclein and increased numbers of activated microglia. Evidence suggests that both misfolded α-synuclein and oxidative stress play an important role in the pathogenesis of sporadic PD. Here we review evidence that α-synuclein activates glia inducing inflammation and that Nrf2-directed phase-II antioxidant enzymes play an important role in PD. We also provide new evidence that the expression of antioxidant enzymes regulated in part by Nrf2 is increased in a mouse model of α-synuclein overexpression. We show that misfolded α-synuclein directly activates microglia inducing the production and release of the proinflammatory cytokine, TNF-α, and increasing antioxidant enzyme expression. Importantly, we demonstrate that the precise structure of α-synuclein is important for induction of this proinflammatory pathway. This complex α-synuclein-directed glial response highlights the importance of protein misfolding, oxidative stress and inflammation in PD and represents a potential locus for the development of novel therapeutics focused on induction of the Nrf2-directed antioxidant pathway and inhibition of protein misfolding.


Assuntos
Antioxidantes/farmacologia , Ativação de Macrófagos/efeitos dos fármacos , Microglia/efeitos dos fármacos , Microglia/imunologia , Doença de Parkinson/imunologia , alfa-Sinucleína/farmacologia , Fosfatase Alcalina/metabolismo , Animais , Western Blotting , Proteínas de Ligação ao Cálcio/metabolismo , Linhagem Celular , Feminino , Expressão Gênica/efeitos dos fármacos , Humanos , Imuno-Histoquímica , Camundongos , Camundongos Transgênicos , Proteínas dos Microfilamentos/metabolismo , Microscopia de Força Atômica , Fator 2 Relacionado a NF-E2/fisiologia , Estresse Oxidativo/efeitos dos fármacos , Placenta/enzimologia , Gravidez , Conformação Proteica , RNA/biossíntese , RNA/genética , Reação em Cadeia da Polimerase em Tempo Real , Fator de Necrose Tumoral alfa/metabolismo , alfa-Sinucleína/química
5.
PLoS One ; 7(11): e48243, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23133622

RESUMO

Several human diseases including neurodegenerative disorders and cancer are associated with abnormal accumulation and aggregation of misfolded proteins. Proteins with high tendency to aggregate include the p53 gene product, TAU and alpha synuclein. The potential toxicity of aberrantly folded proteins is limited via their transport into intracellular sub-compartments, the aggresomes, where misfolded proteins are stored or cleared via autophagy. We have identified a region of the acetyltransferase p300 that is highly disordered and displays similarities with prion-like domains. We show that this region is encoded as an alternative spliced variant independently of the acetyltransferase domain, and provides an interaction interface for various misfolded proteins, promoting their aggregation. p300 enhances aggregation of TAU and of p53 and is a component of cellular aggregates in both tissue culture cells and in alpha-synuclein positive Lewy bodies of patients affected by Parkinson disease. Down-regulation of p300 impairs aggresome formation and enhances cytotoxicity induced by misfolded protein stress. These data unravel a novel activity of p300, offer new insights into the function of disordered domains and implicate p300 in pathological aggregation that occurs in neurodegeneration and cancer.


Assuntos
Fatores de Transcrição de p300-CBP/química , Processamento Alternativo , Sequência de Aminoácidos , Animais , Autofagia , Células COS , Chlorocebus aethiops , Regulação para Baixo , Humanos , Corpos de Lewy/metabolismo , Dados de Sequência Molecular , Neoplasias/metabolismo , Doenças Neurodegenerativas/metabolismo , Estresse Oxidativo , Doença de Parkinson/metabolismo , Príons/química , Desnaturação Proteica , Dobramento de Proteína , Estrutura Terciária de Proteína , Homologia de Sequência de Aminoácidos , alfa-Sinucleína/metabolismo , Fatores de Transcrição de p300-CBP/fisiologia
6.
J Neuroinflammation ; 7: 57, 2010 Sep 28.
Artigo em Inglês | MEDLINE | ID: mdl-20920207

RESUMO

BACKGROUND: Passive immunization with antibodies directed to Aß decreases brain Aß/amyloid burden and preserves memory in transgenic mouse models of Alzheimer's disease (AD). This therapeutic strategy is under intense scrutiny in clinical studies, but its application is limited by neuroinflammatory side effects (autoimmune encephalitis and vasogenic edema). METHODS: We intravenously administered the monoclonal Aß protofibril antibody PFA1 to aged (22 month) male and female 3 × tg AD mice with intermediate or advanced AD-like neuropathologies, respectively, and measured brain and serum Aß and CNS cytokine levels. We also examined 17 month old 3 × tg AD female mice with intermediate pathology to determine the effect of amyloid burden on responses to passive immunization. RESULTS: The 22 month old male mice immunized with PFA1 had decreased brain Aß, increased serum Aß, and no change in CNS cytokine levels. In contrast, 22 month old immunized female mice revealed no change in brain Aß, decreased serum Aß, and increased CNS cytokine levels. Identical experiments in younger (17 month old) female 3 × tg AD mice with intermediate AD-like neuropathologies revealed a trend towards decreased brain Aß and increased serum Aß accompanied by a decrease in CNS MCP-1. CONCLUSIONS: These data suggest that passive immunization with PFA1 in 3 × tg AD mice with intermediate disease burden, regardless of sex, is effective in mediating potentially therapeutic effects such as lowering brain Aß. In contrast, passive immunization of mice with a more advanced amyloid burden may result in potentially adverse effects (encephalitis and vasogenic edema) mediated by certain proinflammatory cytokines.


Assuntos
Doença de Alzheimer/imunologia , Vacinas contra Alzheimer/uso terapêutico , Peptídeos beta-Amiloides/metabolismo , Encéfalo/patologia , Imunização Passiva , Doença de Alzheimer/patologia , Doença de Alzheimer/prevenção & controle , Peptídeos beta-Amiloides/imunologia , Animais , Western Blotting , Encéfalo/imunologia , Encéfalo/metabolismo , Citocinas/imunologia , Citocinas/metabolismo , Modelos Animais de Doenças , Ensaio de Imunoadsorção Enzimática , Feminino , Masculino , Camundongos , Camundongos Transgênicos , Proteínas tau/imunologia , Proteínas tau/metabolismo
7.
Neurotox Res ; 16(3): 318-28, 2009 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-19551455

RESUMO

Except for a handful of inherited cases related to known gene defects, Parkinson's disease (PD) is a sporadic neurodegenerative disease of unknown etiology. There is increasing evidence that inflammation and proliferation of microglia may contribute to the neuronal damage seen in the nigro-striatal dopaminergic system of PD patients. Microglia events that participate in neuronal injury include the release of pro-inflammatory and neurotoxic factors. Characterizing these factors may help to prevent the exacerbation of PD symptoms or to remediate the disease progression. In rodents, the nigro-striatal system exhibits high expression of the chemokine receptor CXCR4. Its natural ligand CXCL12 can promote neuronal apoptosis. Therefore, the present study investigated the expression of CXCR4 and CXCL12 in post-mortem brains of PD and control (non-PD) individuals and in an animal model of PD. In the human substantia nigra (SN), CXCR4 immunoreactivity was high in dopaminergic neurons. Interestingly, the SN of PD subjects exhibited higher expression of CXCR4 expression and CXCL12 than control subjects despite the loss of dopamine (DA) neurons. This effect was accompanied by an increase in activated microglia. However, results from post-mortem brains may not provide indication as to whether CXCL12/CXCR4 can cause the degeneration of DA neurons. To examine the role of these chemokines, we determined the levels of CXCL12 and CXCR4 in the SN of MPTP-treated mice. MPTP produced a time-dependent up-regulation of CXCR4 that preceded the loss of DA neurons. These results suggest that CXCL12/CXCR4 may participate in the etiology of PD and indicate a new possible target molecule for PD.


Assuntos
Quimiocina CXCL12/metabolismo , Corpo Estriado/metabolismo , Regulação da Expressão Gênica/fisiologia , Doença de Parkinson/patologia , Receptores CXCR4/metabolismo , Substância Negra/metabolismo , Análise de Variância , Animais , Proteínas de Ligação ao Cálcio , Quimiocina CXCL12/genética , Proteínas de Ligação a DNA/metabolismo , Modelos Animais de Doenças , Ensaio de Imunoadsorção Enzimática/métodos , Regulação da Expressão Gênica/efeitos dos fármacos , Humanos , Intoxicação por MPTP/induzido quimicamente , Intoxicação por MPTP/patologia , Camundongos , Proteínas dos Microfilamentos , Microglia/patologia , Doença de Parkinson/etiologia , Fosfopiruvato Hidratase/metabolismo , Mudanças Depois da Morte , Receptores CXCR4/genética , Fatores de Tempo , Tirosina 3-Mono-Oxigenase/metabolismo
8.
Neurobiol Dis ; 29(3): 505-14, 2008 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-18187333

RESUMO

Loss-of-function mutations in the DJ-1 gene account for an autosomal recessive form of Parkinson's disease (PD). To investigate the physiological functions of DJ-1 in vivo, we generated DJ-1 knockout (DJ-1(-/-)) mice. Younger (<1 year) DJ-1(-/-) mice were hypoactive and had mild gait abnormalities. Older DJ-1(-/-), however, showed decreased body weight and grip strength and more severe gait irregularities compared to wild-type littermates. The basal level of extracellular dopamine, evoked dopamine release and dopamine receptor D2 sensitivity appeared normal in the striatum of DJ-1(-/-) mice, which was consistent with similar results between DJ-1(-/-) and controls in behavioral paradigms specific for the dopaminergic system. An examination of spinal cord, nerve and muscle tissues failed to identify any pathological changes that were consistent with the noted motor deficits. Taken together, our findings suggest that loss of DJ-1 leads to progressive behavioral changes without significant alterations in nigrostriatal dopaminergic and spinal motor systems.


Assuntos
Comportamento Animal/fisiologia , Corpo Estriado/fisiologia , Proteínas Associadas aos Microtúbulos/deficiência , Proteínas Associadas aos Microtúbulos/genética , Substância Negra/fisiologia , Animais , Progressão da Doença , Aprendizagem em Labirinto/fisiologia , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Knockout , Atividade Motora/fisiologia
9.
J Neurosci ; 26(45): 11798-806, 2006 Nov 08.
Artigo em Inglês | MEDLINE | ID: mdl-17093100

RESUMO

Amyotrophic lateral sclerosis (ALS), the most common adult-onset motor neuron disease is caused by a selective loss of motor neurons. One form of juvenile onset autosomal recessive ALS (ALS2) has been linked to the loss of function of the ALS2 gene. The pathogenic mechanism of ALS2-deficiency, however, remains unclear. To further understand the function of alsin that is encoded by the full-length ALS2 gene, we screened proteins interacting with alsin. Here, we report that alsin interacted with glutamate receptor interacting protein 1 (GRIP1) both in vitro and in vivo, and colocalized with GRIP1 in neurons. In support of the physiological interaction between alsin and GRIP1, the subcellular distribution of GRIP1 was altered in ALS2(-/-) spinal motor neurons, which correlates with a significant reduction of AMPA-type glutamate receptor subunit 2 (GluR2) at the synaptic/cell surface of ALS2(-/-) neurons. The decrease of calcium-impermeable GluR2-containing AMPA receptors at the cell/synaptic surface rendered ALS2(-/-) neurons more susceptible to glutamate receptor-mediated neurotoxicity. Our findings reveal a novel function of alsin in AMPA receptor trafficking and provide a novel pathogenic link between ALS2-deficiency and motor neuron degeneration, suggesting a protective role of alsin in maintaining the survival of motor neurons.


Assuntos
Esclerose Lateral Amiotrófica/complicações , Esclerose Lateral Amiotrófica/metabolismo , Fatores de Troca do Nucleotídeo Guanina/deficiência , Degeneração Neural/etiologia , Receptores de AMPA/metabolismo , Proteínas Adaptadoras de Transdução de Sinal/metabolismo , Animais , Biotinilação/métodos , Linhagem Celular , Membrana Celular/fisiologia , Sobrevivência Celular/efeitos dos fármacos , Córtex Cerebral/citologia , Modelos Animais de Doenças , Agonistas de Aminoácidos Excitatórios/farmacologia , Fatores de Troca do Nucleotídeo Guanina/genética , Humanos , Imunoprecipitação/métodos , Técnicas In Vitro , Camundongos , Camundongos Knockout , Proteínas do Tecido Nervoso/metabolismo , Neurônios/efeitos dos fármacos , Neurônios/fisiologia , Transporte Proteico/efeitos dos fármacos , Medula Espinal/citologia , Frações Subcelulares/efeitos dos fármacos , Frações Subcelulares/metabolismo , Transfecção/métodos , Ácido alfa-Amino-3-hidroxi-5-metil-4-isoxazol Propiônico/farmacologia
10.
Hum Mol Genet ; 14(14): 2063-73, 2005 Jul 15.
Artigo em Inglês | MEDLINE | ID: mdl-15944198

RESUMO

Both homozygous (L166P, M26I, deletion) and heterozygous mutations (D149A, A104T) in the DJ-1 gene have been identified in Parkinson's disease (PD) patients. The biochemical function and subcellular localization of DJ-1 protein have not been clarified. To date the localization of DJ-1 protein has largely been described in studies over-expressing tagged DJ-1 protein in vitro. It is not known whether the subcellular localization of over-expressed DJ-1 protein is identical to that of endogenously expressed DJ-1 protein both in vitro and in vivo. To clarify the subcellular localization and function of DJ-1, we generated three highly specific antibodies to DJ-1 protein and investigated the subcellular localization of endogenous DJ-1 protein in both mouse brain tissues and human neuroblastoma cells. We have found that DJ-1 is widely distributed and is highly expressed in the brain. By cell fractionation and immunogold electron microscopy, we have identified an endogenous pool of DJ-1 in mitochondrial matrix and inter-membrane space. To further investigate whether pathogenic mutations might prevent the distribution of DJ-1 to mitochondria, we generated human neuroblastoma cells stably transfected with wild-type (WT) or mutant (M26I, L166P, A104T, D149A) DJ-1 and performed mitochondrial fractionation and confocal co-localization imaging studies. When compared with WT and other mutants, L166P mutant exhibits largely reduced protein level. However, the pathogenic mutations do not alter the distribution of DJ-1 to mitochondria. Thus, DJ-1 is an integral mitochondrial protein that may have important functions in regulating mitochondrial physiology. Our findings of DJ-1's mitochondrial localization may have important implications for understanding the pathogenesis of PD.


Assuntos
Proteínas Oncogênicas/metabolismo , Doença de Parkinson/metabolismo , Western Blotting , Núcleo Celular/metabolismo , Eletroforese em Gel de Poliacrilamida , Heterozigoto , Humanos , Imuno-Histoquímica , Peptídeos e Proteínas de Sinalização Intracelular , Microscopia Eletrônica , Mitocôndrias/metabolismo , Mutação , Proteínas Oncogênicas/genética , Proteína Desglicase DJ-1 , Frações Subcelulares/metabolismo
11.
Brain Res Mol Brain Res ; 134(1): 103-8, 2005 Mar 24.
Artigo em Inglês | MEDLINE | ID: mdl-15790534

RESUMO

Formation of alpha-synuclein aggregation and Lewy bodies (LBs) are hallmarks of Parkinson's disease (PD) and other related diseases. The dopaminergic neurotoxin, MPTP, replicates many of the pathological signs and motoric features of PD in primates and rodents by selective destruction of dopamine (DA) neurons of the substantia nigra. In this study, groups of adult wild-type C57BL6 mice were treated with MPTP either acutely (20 mg/kg, every 2 h x 4 for 1 day), semi-chronically (30 mg/kg/day for 5 days), or chronically (25 mg/kg MPTP with 250 mg/kg probenecid 2 times/week for 5 weeks). Mice brains were collected and processed at various time points for immunohistochemistry and HPLC assays. Our data showed that although there is a significant decrease in DA content and its metabolites and tyrosine hydroxylase immunoreactivity, there is no inclusion body formation following the various MPTP treatment regimens.


Assuntos
1-Metil-4-Fenil-1,2,3,6-Tetra-Hidropiridina , Modelos Animais de Doenças , Corpos de Inclusão/metabolismo , Intoxicação por MPTP/metabolismo , Substância Negra/efeitos dos fármacos , Ácido 3,4-Di-Hidroxifenilacético/metabolismo , Animais , Cromatografia Líquida de Alta Pressão/métodos , Dopamina/metabolismo , Relação Dose-Resposta a Droga , Esquema de Medicação , Ácido Homovanílico/metabolismo , Humanos , Imuno-Histoquímica/métodos , Masculino , Camundongos , Camundongos Endogâmicos C57BL , Proteínas do Tecido Nervoso/metabolismo , Neurônios/efeitos dos fármacos , Substância Negra/metabolismo , Substância Negra/patologia , Sinucleínas , Tirosina 3-Mono-Oxigenase/metabolismo , Ubiquitina/metabolismo , alfa-Sinucleína
12.
Ann N Y Acad Sci ; 991: 132-9, 2003 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-12846982

RESUMO

Experimental intoxication models are used to study the more common sporadic form of Parkinson's disease (PD). 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyrimidine (MPTP) animal models of PD provide a valuable and predictive tool to probe the molecular mechanisms of dopamine neuronal cell death in PD. MPTP is a powerful neurotoxin that induces neuronal degeneration in the substantia nigra pars compacta and produces PD-like symptoms in several mammalian species tested, a feat not yet accomplished in genetically engineered mice expressing human genetic mutations. The mechanisms of MPTP-induced neurotoxicity are not yet fully understood but involve activation of N-methyl-D-aspartate (NMDA) receptors by glutamate, production of NO by nNOS and iNOS, oxidative injury to DNA, and activation of the DNA damage-sensing enzyme poly (ADP-ribose) polymerase (PARP). Recent experiments indicate that translocation of a mitochondrial protein apoptosis inducing factor (AIF) from mitochondria to the nucleus depends on PARP activation and plays an important role in excitotoxicity-induced cell death. This article briefly reviews the experimental findings regarding excitotoxicity, PARP activation, and AIF translocation in MPTP toxicity and dopaminergic neuronal cell death.


Assuntos
Flavoproteínas/metabolismo , Intoxicação por MPTP/metabolismo , Proteínas de Membrana/metabolismo , Poli(ADP-Ribose) Polimerases/metabolismo , Proteínas/metabolismo , Animais , Fator de Indução de Apoptose , Morte Celular/fisiologia , Dano ao DNA , Modelos Animais de Doenças , Haplorrinos , Humanos , Intoxicação por MPTP/induzido quimicamente , Intoxicação por MPTP/fisiopatologia , Óxido Nítrico/metabolismo , Poli(ADP-Ribose) Polimerase-1 , Poli(ADP-Ribose) Polimerases/genética , Processamento de Proteína Pós-Traducional/efeitos dos fármacos , Proteínas/genética
13.
J Comp Psychol ; 109(4): 368-383, 1995 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-7497695

RESUMO

The authors tested the effects of varying cage size on the behavior of 10 female and 10 male Macaca fascicularis by singly caging them for 2 weeks in each of 5 cage sizes, ranging from approximately 20% to 148% of regulation size. Behavior in the regulation cage size, a size 23% smaller, and a size 48% larger did not differ in any analysis. Locomotion was significantly less in the 2 smallest cage sizes. Abnormal behavior occurred only 5% of the time, did not increase as cage size decreased, and did not change significantly over nearly 3 years. Disruption of the normal activity budget in the laboratory environment proved to be a useful indicator of psychological well-being. Moving to a new room and, to a lesser extent, moving into a new, clean cage, regardless of size, was associated with disrupted sleep the 1st night and suppressed activity, especially self-grooming, the next day.


Assuntos
Abrigo para Animais , Macaca fascicularis/psicologia , Atividade Motora , Percepção de Tamanho , Meio Social , Adaptação Psicológica , Bem-Estar do Animal , Animais , Feminino , Asseio Animal , Habituação Psicofisiológica , Masculino , Fases do Sono
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