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1.
Zhongguo Zhong Yao Za Zhi ; 45(9): 2042-2045, 2020 May.
Artigo em Chinês | MEDLINE | ID: mdl-32495551

RESUMO

The technique of "simulative habitat cultivation" is to preserve the quality of traditional Chinese medicine by simulating the original habitat and site environment of wild Chinese medicine resources. Dendrobium nobile is the most representative variety of traditional Chinese medicine which reflects the coordinated development of medicinal material production and ecological environment. In this paper, the main technical points of the simulated cultivation model of D. nobile were summarized as follows: rapid propagation of seedling tissue technology to ensure the genetic stability of provenance; line card+fermented cow manure+live moss method to improve the survival rate; epiphytic stone cultivation to improve the quality of medicinal materials; and the integration of mycorrhizal fungi to improve the quality stability of medicinal materials. On the basis of summarizing the ecological benefits, economical and social benefits generated by the application of the technology, the paper systematically analyzes the principle of the technology for the cultivation of D. nobile to promote the excellent quality, the light, gas, heat and fertilizer resources of the undergrowth niche are in line with the wild site environment of D. nobile. The rich and complex soil microbial community in the forest laid the foundation for the species diversity needed for the growth of D. nobile.The stress effect on the growth of D. nobile resulted in the accumulation of secondary metabolites. The symbiotic relationship between the symbiotic fungi such as bryophytes and D. nobile promotes the synthesis of plant secondary metabolites. The high quality D. nobile was produced efficiently by improving and optimizing the cultivation techniques.


Assuntos
Dendrobium , Micorrizas , Animais , Bovinos , Ecossistema , Feminino , Medicina Tradicional Chinesa , Simbiose
2.
Cell Rep ; 11(8): 1305-18, 2015 May 26.
Artigo em Inglês | MEDLINE | ID: mdl-26004179

RESUMO

Motor neurons (MNs) are unique because they project their axons outside of the CNS to innervate the peripheral muscles. Limb-innervating lateral motor column MNs (LMC-MNs) travel substantially to innervate distal limb mesenchyme. How LMC-MNs fine-tune the balance between survival and apoptosis while wiring the sensorimotor circuit en route remains unclear. Here, we show that the mir-17∼92 cluster is enriched in embryonic stem cell (ESC)-derived LMC-MNs and that conditional mir-17∼92 deletion in MNs results in the death of LMC-MNs in vitro and in vivo. mir-17∼92 overexpression rescues MNs from apoptosis, which occurs spontaneously during embryonic development. PTEN is a primary target of mir-17∼92 responsible for LMC-MN degeneration. Additionally, mir-17∼92 directly targets components of E3 ubiquitin ligases, affecting PTEN subcellular localization through monoubiquitination. This miRNA-mediated regulation modulates both target expression and target subcellular localization, providing LMC-MNs with an intricate defensive mechanism that controls their survival.


Assuntos
MicroRNAs/metabolismo , Neurônios Motores/metabolismo , PTEN Fosfo-Hidrolase/metabolismo , Animais , Apoptose/fisiologia , Camundongos , Camundongos Knockout , MicroRNAs/genética , Neurônios Motores/citologia , Neurônios Motores/enzimologia , PTEN Fosfo-Hidrolase/genética , Transdução de Sinais , Ubiquitina-Proteína Ligases/genética , Ubiquitina-Proteína Ligases/metabolismo
3.
Neuron ; 69(4): 721-35, 2011 Feb 24.
Artigo em Inglês | MEDLINE | ID: mdl-21338882

RESUMO

Neural patterning relies on transcriptional cross-repressive interactions that ensure unequivocal assignment of neural progenitor identity to proliferating cells. Progenitors of spinal motor neurons (pMN) and V2 interneurons (p2) are specified by a pair of cross-repressive transcription factors, Olig2 and Irx3. Lineage tracing revealed that many p2 progenitors transiently express the pMN marker Olig2 during spinal cord development. Here we demonstrate that the repression of Olig2 in p2 domain is controlled by mir-17-3p microRNA-mediated silencing of Olig2 mRNA. Mice lacking all microRNAs or just the mir-17∼92 cluster manifest a dorsal shift in pMN/p2 boundary and impairment in the production of V2 interneurons. Our findings suggest that microRNA-mediated repression of Olig2 mRNA plays a critical role during the patterning of ventral spinal progenitor domains by shifting the balance of cross-repressive interactions between Olig2 and Irx3 transcription factors.


Assuntos
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo , Regulação da Expressão Gênica no Desenvolvimento/fisiologia , Proteínas de Homeodomínio/metabolismo , MicroRNAs/fisiologia , Proteínas do Tecido Nervoso/metabolismo , Células-Tronco Neurais/fisiologia , Medula Espinal/citologia , Fatores de Transcrição/metabolismo , Animais , Animais Recém-Nascidos , Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética , RNA Helicases DEAD-box/genética , RNA Helicases DEAD-box/metabolismo , Relação Dose-Resposta a Droga , Doxiciclina/farmacologia , Embrião de Mamíferos , Endorribonucleases/genética , Endorribonucleases/metabolismo , Antagonistas de Estrogênios/farmacologia , Regulação da Expressão Gênica no Desenvolvimento/efeitos dos fármacos , Regulação da Expressão Gênica no Desenvolvimento/genética , Proteínas de Homeodomínio/genética , Interneurônios/metabolismo , Proteínas Luminescentes/genética , Substâncias Macromoleculares/metabolismo , Camundongos , Camundongos Transgênicos , Modelos Biológicos , Neurônios Motores/metabolismo , Proteínas do Tecido Nervoso/genética , Células-Tronco Neurais/efeitos dos fármacos , Fator de Transcrição 2 de Oligodendrócitos , Proteínas/genética , RNA não Traduzido , Ribonuclease III , Relação Estrutura-Atividade , Tamoxifeno/análogos & derivados , Tamoxifeno/farmacologia , Fatores de Transcrição/genética , Transfecção/métodos
4.
Mol Cell ; 27(5): 701-16, 2007 Sep 07.
Artigo em Inglês | MEDLINE | ID: mdl-17803936

RESUMO

Death-associated protein kinase (DAPK) is a calmodulin-regulated serine/threonine kinase and elicits tumor suppression function through inhibiting cell adhesion/migration and promoting apoptosis. Despite these biological functions, the signaling mechanisms through which DAPK is regulated remain largely elusive. Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation. Upon EGF stimulation, a rapid Src activation leads to subsequent LAR downregulation, and these two events act in synergism to inactivate DAPK, thereby facilitating tumor cell migration and invasion toward EGF. Finally, DAPK Y491/492 hyperphosphorylation is found in human cancers in which Src activity is aberrantly elevated. These results identify LAR and Src as a DAPK regulator through their reciprocal modification of DAPK Y491/492 residues and establish a functional link of this DAPK-regulatory circuit to tumor progression.


Assuntos
Proteínas Reguladoras de Apoptose/metabolismo , Proteínas Quinases Dependentes de Cálcio-Calmodulina/metabolismo , Proteínas do Tecido Nervoso/fisiologia , Proteínas Tirosina Fosfatases/fisiologia , Proteínas Proto-Oncogênicas pp60(c-src)/fisiologia , Receptores de Superfície Celular/fisiologia , Proteínas Supressoras de Tumor/metabolismo , Proteínas Reguladoras de Apoptose/química , Proteínas Quinases Dependentes de Cálcio-Calmodulina/química , Linhagem Celular Tumoral , Proteínas Quinases Associadas com Morte Celular , Fator de Crescimento Epidérmico/metabolismo , Humanos , Neoplasias/metabolismo , Proteínas do Tecido Nervoso/metabolismo , Fosforilação , Proteínas Tirosina Fosfatases/metabolismo , Proteínas Proto-Oncogênicas pp60(c-src)/metabolismo , Proteínas Tirosina Fosfatases Classe 2 Semelhantes a Receptores , Receptores de Superfície Celular/metabolismo , Transdução de Sinais , Proteínas Supressoras de Tumor/química
5.
Exp Eye Res ; 84(3): 486-92, 2007 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-17178414

RESUMO

Retinal ischemia is a common cause of visual impairment for humans and animals. Herein, the neuroprotective effects of phenylbutyrate (PBA) upon retinal ischemic injury were investigated using a rat model. Retinal ganglion cells (RGCs) were retrograde labeled with the fluorescent tracer fluorogold (FG) applied to the superior collicoli of test Sprague-Dawley rats. High intraocular pressure and retinal ischemia were induced seven days subsequent to such FG labeling. A dose of either 100 or 400 mg/kg PBA was administered intraperitoneally to test rats at two time points, namely 30 min prior to the induction of retinal ischemia and 1 h subsequent to the cessation of the procedure inducing retinal ischemia. The test-rat retinas were collected seven days subsequent to the induction of retinal ischemia, and densities of surviving RGCs were estimated by counting FG-labeled RGCs within the retina. Histological analysis revealed that ischemic injury caused the loss of retinal RGCs and a net decrease in retinal thickness. For PBA-treated groups, almost 100% of the RGCs were preserved by a pre-ischemia treatment with PBA (at a dose of either 100 or 400 mg/kg), while post-ischemia treatment of RGCs with PBA did not lead to the preservation of RGCs from ischemic injury by PBA as determined by the counting of whole-mount retinas. Pre-ischemia treatment of RGCs with PBA (at a dose of either 100 or 400 mg/kg) significantly reduced the level of ischemia-associated loss of thickness of the total retina, especially the inner retina, and the inner plexiform layer of retina. Besides, PBA treatment significantly reduced the ischemia-induced loss of cells in the ganglion-cell layer of the retina. Taken together, these results suggest that PBA demonstrates a marked neuroprotective effect upon high intraocular pressure-induced retinal ischemia when the PBA is administered prior to ischemia induction.


Assuntos
Fenilbutiratos/uso terapêutico , Traumatismo por Reperfusão/prevenção & controle , Doenças Retinianas/tratamento farmacológico , Animais , Contagem de Células , Morte Celular , Relação Dose-Resposta a Droga , Glaucoma/complicações , Glaucoma/tratamento farmacológico , Isquemia/tratamento farmacológico , Isquemia/patologia , Masculino , Microscopia de Fluorescência , Modelos Animais , Ratos , Ratos Sprague-Dawley , Traumatismo por Reperfusão/etiologia , Doenças Retinianas/etiologia , Células Ganglionares da Retina/patologia , Vasos Retinianos/patologia
6.
Mol Cell Biol ; 24(24): 10558-72, 2004 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-15572663

RESUMO

Brk (for breast tumor kinase) is a nonreceptor tyrosine kinase containing SH3, SH2, and tyrosine kinase catalytic domains. Brk was originally identified from a human metastatic breast tumor, and its overexpression is frequently observed in breast cancer and several other cancer types. However, the molecular mechanism by which this kinase participates in tumorigenesis remains poorly characterized. In the present study, we not only identified paxillin as the binding partner and substrate of Brk but also discovered a novel signaling pathway by which Brk mediates epidermal growth factor (EGF)-induced paxillin phosphorylation. We show that EGF stimulation activates the catalytic activity of Brk, which in turn phosphorylates paxillin at Y31 and Y118. These phosphorylation events promote the activation of small GTPase Rac1 via the function of CrkII. Through this pathway, Brk is capable of promoting cell motility and invasion and functions as a mediator of EGF-induced migration and invasion. In accordance with these functional roles, Brk translocates to membrane ruffles, where it colocalizes with paxillin during cell migration. Together, our findings identify novel signaling and biological roles of Brk and indicate the first potential link between Brk and metastatic malignancy.


Assuntos
Moléculas de Adesão Celular/metabolismo , Proteínas do Citoesqueleto/metabolismo , Fosfoproteínas/metabolismo , Proteínas Tirosina Quinases/metabolismo , Proteínas rac1 de Ligação ao GTP/metabolismo , Animais , Células COS , Domínio Catalítico , Linhagem Celular , Linhagem Celular Tumoral , Movimento Celular , Quimiotaxia/efeitos dos fármacos , Chlorocebus aethiops , Ativação Enzimática , Fator de Crescimento Epidérmico/metabolismo , Glutationa Transferase/metabolismo , Proteínas de Fluorescência Verde/metabolismo , Proteínas de Fluorescência Verde/farmacologia , Células HeLa , Humanos , Cinética , Microscopia de Fluorescência , Modelos Biológicos , Proteínas de Neoplasias , Paxilina , Fosforilação , Testes de Precipitina , Estrutura Terciária de Proteína , Proteínas Tirosina Quinases/análise , Proteínas Tirosina Quinases/química , Proteínas Proto-Oncogênicas/metabolismo , Proteínas Proto-Oncogênicas c-crk , RNA Interferente Pequeno/metabolismo , Proteínas Recombinantes de Fusão/metabolismo , Transdução de Sinais , Especificidade por Substrato , Proteínas rac1 de Ligação ao GTP/análise
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