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Angiotensin-converting enzyme inhibitors of Bothrops jararaca snake venom affect the structure of mice seminiferous epithelium J. Venom. Anim. Toxins incl. Trop. Dis.
Alberto-Silva,Carlos; Gilio,Joyce M; Portaro,Fernanda C. V.; Querobino,Samyr M.; Camargo,Antonio C. M..
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 (<ENWPHQIPP), BPP-11e (<EARPPHPPIPP), BPP-AP (<EARPPHPPIPPAP) and captopril were evaluated in the seminiferous epithelium of male mice.Methods The adult animals received either one of the synthetic peptides or captopril (120 nmol/dose per testis) via injection into the testicular parenchyma. After seven days, the mice were sacrificed, and the testes were collected for histopathological evaluation.Results BPP-10c...
Tipo: Info:eu-repo/semantics/article Palavras-chave: B. jararaca; Bradykinin-potentiating peptides; Angiotensin-converting enzyme; Seminiferous epithelium; Spermatogenesis.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100338
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Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities J. Venom. Anim. Toxins incl. Trop. Dis.
Megale,Ângela Alice Amadeu; Magnoli,Fábio Carlos; Kuniyoshi,Alexandre Kazuo; Iwai,Leo Kei; Tambourgi,Denise V.; Portaro,Fernanda C. V.; Silva,Wilmar Dias da.
Abstract Background: Bitis arietans is a venomous snake found in sub-Saharan Africa and in parts of Morocco and Saudi Arabia. The envenomation is characterized by local and systemic reactions including pain, blistering, edema and tissue damage, besides hemostatic and cardiovascular disturbances, which can cause death or permanent disabilities in its victims. However, the action mechanisms that provoke these effects remain poorly understood, especially the activities of purified venom components. Therefore, in order to elucidate the molecular mechanisms that make the Bitis arietans venom so potent and harmful to human beings, this study reports the isolation and biochemical characterization of a snake venom serine protease (SVSP). Methods: Solubilized...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bitis arietans; Venom; Antivenom; Serine protease; Fibrinogenolytic; Kinin-releasing activity.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100328
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