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| Veloso,D.. |
| Low and high molecular weight kininogens (LK and HK), containing 409 and 626 amino acids with masses of ~65 and 120 kDa after glycosylation, respectively, are coded by a single gene mapped to the human chromosome 3 by alternative splicing of the transcribed mRNA. The NH2-termini Glu1-Thr383 region, identical in LK and HK, contains bradykinin (BK) moieties Arg363-Arg371. LK, HK and their kinin products Lys-BK and BK are involved in several biologic processes. They are evolutionarily conserved and only 7 patients, all apparently normal, have been reported to lack them. In one of these patients (Williams' trait), a codon mutation (Arg178 <FONT FACE="Symbol">®</FONT> stop) has been blamed for the absence of LK and HK. However, using Western blots... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Kininogen deficiency; Kinins; Antibodies; Plasma; Kininogen-like species; Human and nonhuman primates. |
| Ano: 1998 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1998000700004 |
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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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| 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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| BAGCHI,S.; DESHPANDE,S. B.. |
| The mechanisms underlying the action of Indian red scorpion Buthus tamulus (BT) venom-induced augmentation of cardiopulmonary reflexes elicited by intravenous injection of 5-HT were examined in urethane anaesthetized rats. The 5-HT produced a concentration-dependent increase in time-response area of bradycardiac response, with the responses at submaximal concentrations shifted to the left after exposure to BT venom (20 µg/kg, IV). Aprotinin (6000 kallikrein inactivating unit, IV) as such had no effect on 5-HT reflex responses (bradycardia, hypotension, and apnea), but blocked the venom-induced reflex augmentation. While ondansetron (10 µg/kg, IV) completely blocked the 5-HT reflex responses, these reappeared partially after venom exposure (20 µg/kg).... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bezold-Jarisch reflex; Aprotinin; Bradykinin; Indian red scorpion; Ondansetron; Buthus tamulus; Kinins; 5-HT3 receptors; Cardiopulmonary reflexes. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302001000100003 |
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| LEIVA-SALCEDO,ELIAS; PEREZ,VIVIANA; ACUÑA-CASTILLO,CLAUDIO; WALTER,ROBIN; SIERRA,FELIPE. |
| Serum levels of T-kininogen increase dramatically as rats approach the end of their lifespan. Stable expression of the protein in Balb/c 3T3 fibroblasts leads to a dramatic inhibition of cell proliferation, as well as inhibition of the ERK signaling pathway. T-kininogen is a potent inhibitor of cysteine proteinases, and we have described that the inhibition of ERK activity occurs, at least in part, via stabilization of the MAP kinase phosphatase, MKP-1. Since fibroblasts are not a physiological target of T-kininogen, we have now purified the protein from rat serum, and used it to assess the effect of T-kininogen on endothelial cells. Adding purified T-kininogen to EAhy 926 hybridoma cells resulted in inhibition of basal ERK activity levels, as estimated... |
| Tipo: Journal article |
Palavras-chave: Aging; Endothelial cells; ERK pathway; Kininogen; Kinins. |
| Ano: 2002 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602002000200020 |
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