Bradykinin Potentiating Peptides
Mostrando 1-9 de 9 artigos, teses e dissertações.
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1. Subproteome of Lachesis muta rhombeata venom and preliminary studies on LmrSP-4, a novel snake venom serine proteinase
Abstract Background: Lachesis muta rhombeata is one of the venomous snakes of medical importance in Brazil whose envenoming is characterized by local and systemic effects which may produce even shock and death. Its venom is mainly comprised of serine and metalloproteinases, phospholipases A2 and bradykinin-potentiating peptides. Based on a previously report
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 15/04/2019
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2. Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
Abstract Background: Venoms represent a still underexplored reservoir of bioactive components that might mitigate or cure diseases in conditions in which conventional therapy is ineffective. The bradykinin-potentiating peptides (BPPs) comprise a class of angiotensin-I converting enzyme (ACE) inhibitors. The BPPs usually consist of oligopeptides with 5 to 13
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 08/02/2018
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3. The modular nature of bradykinin-potentiating peptides isolated from snake venoms
Abstract Bradykinin-potentiating peptides (BPPs) are molecules discovered by Sergio Ferreira – who found them in the venom of Bothrops jararaca in the 1960s – that literally potentiate the action of bradykinin in vivo by, allegedly, inhibiting the angiotensin-converting enzymes. After administration, the global physiological effect of BPP is the decrease
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 21/11/2017
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4. Angiotensin-converting enzyme inhibitors of Bothrops jararaca snake venom affect the structure of mice seminiferous epithelium
Background Considering the similarity between the testis-specific isoform of angiotensin-converting enzyme and the C-terminal catalytic domain of somatic ACE as well as the structural and functional variability of its natural inhibitors, known as bradykinin-potentiating peptides (BPPs), the effects of different synthetic peptides, BPP-10c (
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 29/09/2015
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5. A bradykinin-potentiating peptide (BPP-10c) from Bothrops jararaca induces changes in seminiferous tubules
Background The testis-specific isoform of angiotensin-converting enzyme (tACE) is exclusively expressed in germ cells during spermatogenesis. Although the exact role of tACE in male fertility is unknown, it clearly plays a critical function in spermatogenesis. The dipeptidase domain of tACE is identical to the C-terminal catalytic domain of somatic ACE (sAC
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 06/11/2013
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6. A diversidade estrutural de peptídeos potenciadores da bradicinina da Bothrops jararaca (Bj-BPPs) proporciona ações sinérgicas no sistema cardiovascular. / The structural diversity of the proline-rich oligopeptides from Bothrops jararaca (Bj-BPPs) provides synergistic cardiovascular actions.
Nosso laboratório mostrou que um único gene codifica um precursor protêico, cujo processamento gera o peptídeo natriurético tipo C (CNP) e uma variedade de peptídeos ricos em prolina, conhecidos como peptideos potenciadores da bradicinina ou BPPs. Com pequenas diferenças, esse precursor é expresso na glândula do veneno e na região neuro-endócrina
Publicado em: 2010
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7. Minimização da estrutura primária do peptídeo TsHpt-I: Identificação dos resíduos de aminoácidos cruciais e da estrutura peptídica mínima para a manutenção de seus efeitos anti-hipertensivos
Using a proteomic approach, a new structural family of peptides was put in evidence in the venom of the yellow scorpion Tityus serrulatus. T. serrulatus Hypotensins (TsHpt) are random-coiled linear peptides that act as bradykinin potentiating peptides (PPBs). Aiming to better understand the relationship between the primary structure of TsHpt-I (AEIDFSGIPEDII
Publicado em: 2009
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8. The central nervous system as target for anti-hypertensive actions of a proline-rich peptide from Bothrops jararaca venom / O sistema nervoso central como alvo das ações anti-hipertensivas de um peptídeo rico em resíduo de prolina do veneno da Bothrops jararaca
Os peptídeos potenciadores da bradicinina (BPPs) presentes no veneno da serpente Bothrops jararaca são oligopeptídeos ricos em prolinas. Eles foram os primeiros inibidores naturais da enzima conversora de angiotensina (ECA) descritos. As propriedades bioquímicas e farmacológicas desses peptídeos foram essenciais para o desenvolvimento do captopril, o p
Publicado em: 2009
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9. Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide
A 1.8-kb cDNA clone was isolated from a Bothrops jararaca venom gland cDNA library that encodes a 256-aa precursor for bradykinin-potentiating peptides (angiotensin-converting enzyme inhibitors) and a C-type natriuretic peptide (CNP). The seven bradykinin-potentiating peptides are aligned tandemly after the hydrophobic signal peptide sequence, followed by a
The National Academy of Sciences of the USA.