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| Mesquita-Ferrari,RA; Moraes,CK de; Micocci,KC; Selistre-de-Araújo,HS. |
| ALT-C, an ECD motif (glutamic acid, cysteine, aspartic acid) disintegrin from Bothrops alternatus snake venom, induces α2β1 integrin-mediated signaling and neutrophil chemotaxis. In vitro, in human umbilical vein endothelial cells (HUVEC), ALT-C induces cell proliferation, thus showing an interesting potential for tissue regeneration studies. This work aimed to evaluate the influence of ALT-C in myoblast viability and differentiation. Myoblasts were obtained from hind limb muscles of 3 to 4-day old Wistar rats. The cells were incubated with ALT-C at different concentrations and incubation periods were followed by total RNA isolation. cDNA synthesis and real time polymerase chain reaction (PCR) were performed with primers of myoD as well as of both (slow... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Viability; Myosin heavy chain; Myoblast; Disintegrin; Skeletal muscle; Bothrops alternatus. |
| Ano: 2009 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992009000200013 |
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| Selistre-de-Araujo,H.S.; Cominetti,M.R.; Terruggi,C.H.B.; Mariano-Oliveira,A.; De Freitas,M.S.; Crepin,M.; Figueiredo,C.C.; Morandi,V.. |
| The alpha2ß1 integrin is a major collagen receptor that plays an essential role in the adhesion of normal and tumor cells to the extracellular matrix. Alternagin-C (ALT-C), a disintegrin-like protein purified from the venom of the Brazilian snake Bothrops alternatus, competitively interacts with the alpha2ß1 integrin, thereby inhibiting collagen binding. When immobilized in plate wells, ALT-C supports the adhesion of fibroblasts as well as of human vein endothelial cells (HUVEC) and does not detach cells previously bound to collagen I. ALT-C is a strong inducer of HUVEC proliferation in vitro. Gene expression analysis was done using an Affimetrix HU-95A probe array with probe sets of ~10,000 human genes. In human fibroblasts growing on collagen-coated... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Alpha2ß1 integrin; Disintegrin; Snake venom; Adhesion; Gene expression; Extracellular matrix. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001000007 |
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| Barja-Fidalgo,C.; Coelho,A.L.J.; Saldanha-Gama,R.; Helal-Neto,E.; Mariano-Oliveira,A.; Freitas,M.S. de. |
| Extracellular matrix proteins and cell adhesion receptors (integrins) play essential roles in the regulation of cell adhesion and migration. Interactions of integrins with the extracellular matrix proteins lead to phosphorylation of several intracellular proteins such as focal adhesion kinase, activating different signaling pathways responsible for the regulation of a variety of cell functions, including cytoskeleton mobilization. Once leukocytes are guided to sites of infection, inflammation, or antigen presentation, integrins can participate in the initiation, maintenance, or termination of the immune and inflammatory responses. The modulation of neutrophil activation through integrin-mediated pathways is important in the homeostatic control of the... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Integrin; Disintegrin; Leukocytes; Activation; Proliferation; Signal transduction. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001000008 |
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| Rádis-Baptista,G.. |
| Integrins encompass a family of transmembrane heterodimeric proteins of adhesion that maintain cells attached to other cells and to the extracellular matrix (ECM). Integrins work as bi-directional mechanotransducers, conveying mechanical signal from outside to inside the cell through a cascade of phosphorylation signals. On the other hand, the signal from inside to outside controls the strength and affinity of integrin adhesion. As proteins of focal contact, integrins are involved in diverse cell functions, such as cell activation, migration, growth, and survival. In the development of neoplastic disease and metastatic tumor, integrins can influence cancer invasiveness and progression, as well as mediate the formation of new blood vessels (angiogenesis).... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Integrin; Angiogenesis; Cancer; Apoptosis; Snake toxin; Snake venom C-type lectin; Metalloprotease; Disintegrin. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992005000300002 |
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| 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 |
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