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| Pesquero,J.B.; Bader,M.. |
| The participation of the kallikrein-kinin system, comprising the serine proteases kallikreins, the protein substrates kininogens and the effective peptides kinins, in some pathological processes like hypertension and cardiovascular diseases is still a matter of controversy. The use of different experimental set-ups in concert with the development of potent and specific inhibitors and antagonists for the system has highlighted its importance but the results still lack conclusivity. Over the last few years, transgenic and gene-targeting technologies associated with molecular biology tools have provided specific information about the elusive role of the kallikrein-kinin system in the control of blood pressure and electrolyte homeostasis. cDNA and genomic... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Kallikrein; Kinins; Bradykinin; Molecular biology; Transgenics. |
| Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998000900013 |
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| Craveiro,R.B.; Ramalho,J.D.; Chagas,J.R.; Wang,P.H.M.; Casarini,D.E.; Pesquero,J.L.; Araújo,R.C.; Pesquero,J.B.. |
| Carboxypeptidase M (CPM) is an extracellular glycosylphosphatidyl-inositol-anchored membrane glycoprotein, which removes the C-terminal basic residues, lysine and arginine, from peptides and proteins at neutral pH. CPM plays an important role in the control of peptide hormones and growth factor activity on the cell surface. The present study was carried out to clone and express human CPM in the yeast Pichia pastoris in order to evaluate the importance of this enzyme in physiological and pathological processes. The cDNA for the enzyme was amplified from total placental RNA by RT-PCR and cloned in the vector pPIC9, which uses the methanol oxidase promoter and drives the expression of high levels of heterologous proteins in P. pastoris. The cpm gene, after... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Kinins; Human carboxypeptidase M; Recombinant protein; Pichia pastoris. |
| Ano: 2006 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2006000200007 |
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