Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados BJMBR (2) Biol. Res. (1) ArchiMer (1) Genet. Mol. Biol. (1) Autor An,N. (1) Avarre, Jean-christophe (1) Boulo, Viviane (1) De Lorgeril, Julien (1) Escoubas, Jean-michel (1) Guo,L. (1) Hao,R.H. (1) Kamiguti,A.S. (1) Lagos-Cabré,Raúl (1) Lizama,Carlos (1) Luo,L. (1) Montagnani, Caroline (1) Moreno,Ricardo D (1) Portela,Valerio M. (1) Price,Christopher A. (1) Quiquand, M (1) Reyes,Juan G (1) Theakston,R.D.G. (1) Tian,F.D. (1) Urriola-Muñoz,Paulina (1) Mais... Palavra-chave Metalloproteinase (5) Apoptosis (1) Chondrocyte (1) Crassostrea gigas (1) Damage associated molecular pattern (1) Disintegrin (1) Gonadotropin (1) Granulosa (1) Growth factor (1) Integrin (1) Knee-joint (1) Mollusk immunity (1) Naringenin (1) Osteoarthritis (1) Oyster (1) Paracrine (1) Platelet (1) Rat MIA model (1) Signaling (1) Spermatogenesis (1) Mais... Tipo do documento Info:eu-repo/semantics/article (3) Journal article (1) Text (1) Ano 2017 (1) 2014 (1) 2009 (1) 2007 (1) 1998 (1) País Brazil (3) Chile (1) France (1) Idioma Inglês (5)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 5 Primeira ... 1 ... Última Differential expression and localization of ADAM10 and ADAM17 during rat spermatogenesis suggest a role in germ cell differentiation Biol. Res. Urriola-Muñoz,Paulina; Lizama,Carlos; Lagos-Cabré,Raúl; Reyes,Juan G; Moreno,Ricardo D. BACKGROUND: Extracellular metolloproteases have been implied in different process such as cell death, differentiation and migration. Membrane-bound metalloproteases of the ADAM family shed the extracellular domain of many cytokines and receptor controlling auto and para/juxtacrine cell signaling in different tissues. ADAM17 and ADAM10 are two members of this family surface metalloproteases involved in germ cell apoptosis during the first wave of spermatogenesis in the rat, but they have other signaling functions in somatic tissues. RESULTS: In an attempt to further study these two enzymes, we describe the presence and localization in adult male rats. Results showed that both enzymes are detected in germ and Sertoli cells during all the stages of... Tipo: Journal article Palavras-chave: Testis; Spermatogenesis; Apoptosis; Paracrine; Metalloproteinase. Ano: 2014 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602014000100031 First evidence of the activation of Cg-timp, an immune response component of pacific oysters, through a damage-associated molecular pattern pathway ArchiMer Montagnani, Caroline; Avarre, Jean-christophe; De Lorgeril, Julien; Quiquand, M; Boulo, Viviane; Escoubas, Jean-michel. In a previous work, we characterized a Crassostrea gigas cPNA (Cg-timp) encoding a protein which presents all the features of vertebrate tissue inhibitor of metalloproteinase (TIMP). The expression pattern of this gene led us to propose that Cg-timp is an important factor in oyster wound heating and defense mechanisms. Here we describe the analysis of Cg-timp expression in oysters challenged by live or dead bacteria as well as by bacterial secretory/excretory products and metalloproteinase. Surprisingly, bacterial secretory/excretory products activate Cg-timp gene expression whereas heat-inactivated ones do not. To address the question of the signal transduction pathway involved in Cg-timp gene activation, we isolated and sequenced Cg-timp promoter and... Tipo: Text Palavras-chave: Damage associated molecular pattern; Tissue inhibitor of metalloproteinase; Metalloproteinase; Mollusk immunity; Crassostrea gigas; Oyster. Ano: 2007 URL: http://archimer.ifremer.fr/doc/2007/publication-2094.pdf Naringenin regulates production of matrix metalloproteinases in the knee-joint and primary cultured articular chondrocytes and alleviates pain in rat osteoarthritis model BJMBR Wang,C.C.; Guo,L.; Tian,F.D.; An,N.; Luo,L.; Hao,R.H.; Wang,B.; Zhou,Z.H.. Inflammation of cartilage is a primary symptom for knee-joint osteoarthritis. Matrix metalloproteinases (MMPs) are known to play an important role in the articular cartilage destruction related to osteoarthritis. Naringenin is a plant-derived flavonoid known for its anti-inflammatory properties. We studied the effect of naringenin on the transcriptional expression, secretion and enzymatic activity of MMP-3 in vivo in the murine monosodium iodoacetate (MIA) osteoarthritis model. The assessment of pain behavior was also performed in the MIA rats. The destruction of knee-joint tissues was analyzed microscopically. Moreover, the effect of naringenin was also studied in vitro in IL-1β activated articular chondrocytes. The transcriptional expression of MMP-3,... Tipo: Info:eu-repo/semantics/article Palavras-chave: Metalloproteinase; Osteoarthritis; Naringenin; Chondrocyte; Knee-joint; Rat MIA model. Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2017000400603 Regulation of MMP2 and MMP9 metalloproteinases by FSH and growth factors in bovine granulosa cells Genet. Mol. Biol. Portela,Valerio M.; Veiga,Angela; Price,Christopher A.. Matrix metalloproteinases (MMP) are key enzymes involved in tissue remodeling. Within the ovary, they are believed to play a major role in ovulation, and have been linked to follicle atresia. To gain insight into the regulation of MMPs, we measured the effect of hormones and growth factors on MMP2 and MMP9 mRNA levels in non-luteinizing granulosa cells in serum-free culture. FSH and IGF1 both stimulated estradiol secretion and inhibited MMP2 and MMP9 mRNA abundance. In contrast, EGF and FGF2 both inhibited estradiol secretion but had no effect on MMP expression. At physiological doses, none of these hormones altered the proportion of dead cells. Although we cannot link MMP expression with apoptosis, the specific down regulation by the gonadotropic hormones... Tipo: Info:eu-repo/semantics/article Palavras-chave: Metalloproteinase; Gonadotropin; Growth factor; Granulosa. Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572009000300014 Snake venom metalloproteinases and disintegrins: interactions with cells BJMBR Kamiguti,A.S.; Zuzel,M.; Theakston,R.D.G.. Metalloproteinases and disintegrins are important components of most viperid and crotalid venoms. Large metalloproteinases referred to as MDC enzymes are composed of an N-terminal Metalloproteinase domain, a Disintegrin-like domain and a Cys-rich C-terminus. In contrast, disintegrins are small non-enzymatic RGD-containing cysteine-rich polypeptides. However, the disintegrin region of MDC enzymes bears a high degree of structural homology to that of the disintegrins, although it lacks the RGD motif. Despite these differences, both components share the property of being able to recognize integrin cell surface receptors and thereby to inhibit integrin-dependent cell reactions. Recently, several membrane-bound MDC enzymes, closely related to soluble venom MDC... Tipo: Info:eu-repo/semantics/article Palavras-chave: Venom; Metalloproteinase; Disintegrin; Platelet; Integrin; Signaling. Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998000700001 Registros recuperados: 5 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco