PATRICK JACK SPENCER
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Possui graduação em Ciências Biológicas pela Universidade Presbiteriana Mackenzie (1991), mestrado em Tecnologia Nuclear pela Universidade de São Paulo (1995) e doutorado em Tecnologia Nuclear pela Universidade de São Paulo (2000) tendo sido bolsista sandwich no US Army Medical Research Institute for Infeccious Diseases (98-99). É responsável pelo Biotério de criação e manutenção de animais de laboratório do IPEN. Tem experiência na área de Bioquímica, com ênfase em Proteínas, atuando principalmente nos seguintes temas: veneno, proteínas, bothrops, irradiação e miotoxina.(Texto extraído do Currículo Lattes em 22 dez. 2021)
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Resumo IPEN-doc 27445 Hypanus americanus mucus2020 - COELHO, GUILHERME R.; PREZOTTO NETO, JOSE P.; BARBOSA, FERNANDA C.; SANTOS, RAFAEL S.; BRIGATTE, PATRICIA; SPENCER, PATRICK J.; SAMPAIO, SANDRA C.; D'AMELIO, FERNANDA; PIMENTA, DANIEL C.; SCIANI, JULIANA M.Fish skin plays important biological roles, such as the control of the osmotic pressure gradient, protection against mechanical forces and microorganism infections. The mucus, on the other hand, is a rich and complex fluid, important for the fish acting as innate immunity system, swimming and nutrition. The elasmobranch epidermis is characterized mainly by mucus secretory cells, and marine stingrays have already been described to present secretory glands spread throughout the body. Little is known about the biochemical composition of the stingray mucus, but recent studies denoted the importance of mucus in the envenomation process. Stingrays venom are largely studied due the human medical importance of envenoming caused by sting puncture, that evolve with local inflammation and necrosis, and these toxic events can be correlated to the chemical composition of the sting skin, according to the literature. Aiming to analyse the mucus composition, a new non-invasive mucus collection method was developed that focused on peptides and proteins, and biological assays were performed to analyze preliminary toxic and immune activities of the Hypanus americanus mucus. Pathophysiological characterization showed the presence of peptidases on mucus, as well that the induction of edema and leukocyte recruitment in mice. The fractionated mucus improved phagocytosis on macrophages and showed antimicrobial activity against T. rubrum, C. neoformans and C. albicans in vitro. The proteomic analyses showed the presence of immune-related proteins like actin, histones, hemoglobin, and ribosomal proteins. This protein pattern is similar to those reported for other fish mucus and stingray venom. This is the first report depicting the Hypanus stingray mucus composition, highlighting its biochemical composition and importance for the stingray immune system and the possible role on the envenomation process.Artigo IPEN-doc 23046 Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros2017 - FUCASE, TAMARA M.; SCIANI, JULIANA M.; CAVALCANTE, INGRID; VIALA, VINCENT L.; CHAGAS, BRUNO B.; PIMENTA, DANIEL C.; SPENCER, PATRICK J.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 residues with a high number of proline residues and the tripeptide Ile-Pro-Pro (IPP-tripeptide) in the C-terminus region and have a conserved N-terminal pyroglutamate residue. As a whole, the action of the BPPs on prey and snakebite victims results in the decrease of the blood pressure. The aim of this work was to isolate and characterize novel BPPs from the venom of Bitis gabonica rhinoceros. Methods: The crude venom of B. g. rhinoceros was fractionated by size exclusion chromatography and the peptide fraction (<7 kDa) was separated by reverse phase chromatography (RP-HPLC) and analyzed by ESI-IT-TOF-MS/MS. One new BPP was identified, synthetized and assayed for ACE inhibition and, in vivo, for edema potentiation. Results: Typical BPP signatures were identified in three RP-HPLC fractions. CID fragmentation presented the usual y-ion of the terminal P-P fragment as a predominant signal at m/z 213.1. De novo peptide sequencing identified one Bothrops-like BPP and one new BPP sequence. The new BPP was synthesized and showed poor inhibition over ACE, but displayed significant bradykinin-induced edema potentiation. Conclusions: So far, few BPPs are described in Viperinae, and based on the sequenced peptides, two non-canonical sequences were detected. The possible clinical role of this new peptides remains unclear.Artigo IPEN-doc 21761 Isolation and characterization of bradykinin potentiating peptides from Agkistrodon bilineatus venom2016 - MUNAWAR, AISHA; ZAHID, ANUM; NEGM, AMR; AKREM, AHMED; SPENCER, PATRICK; BETZEL, CHRISTIANArtigo IPEN-doc 21327 Venomics of the Australian eastern brown snake (Pseudonaja textilis): Detection of new venom proteins and splicing variants2015 - VIALA, VINCENT L.; HILDEBRAND, DIANA; TRUSCH, MARIA; FUCASE, TAMARA M.; SCIANI, JULIANA M.; PIMENTA, DANIEL C.; ARNI, RAGHUVIR K.; SCHLUTER, HARTMUT; BETZEL, CHRISTIAN; MIRTSCHIM, PETER; DUNSTAN, NATHAN; SPENCER, PATRICK J.Artigo IPEN-doc 21288 Proteomic analysis of the rare Uracoan rattlesnake Crotalus vegrandis venom: Evidence of a broad arsenal of toxins2015 - VIALA, VINCENT L.; HILDEBRAND, DIANA; FUCASE, TAMARA M.; SCIANI, JULIANA M.; PREZOTTO NETO, JOSE P.; RIEDNER, MARIA; SANCHES, LEONARDO; NISHIMURA, PAULA J.; OGUIURA, NANCY; PIMENTA, DANIEL C.; SCHLUTER, HARTMUT; BETZEL, CHRISTIAN; ARNI, RAGHUVIR K.; SPENCER, PATRICK J.Artigo IPEN-doc 20025 Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis2014 - MUNAWAR, AISHA; TRUSCH, MARIA; GEORGIEVA, DESSISLAVA; HILDEBRAND, DIANA; KWIATKOWSKI, MARCEL; BEHNKEN, HENNING; HARDER, SONKE; ARNI, RAGHUVIR; SPENCER, PATRICK; SCHLUTER, HARTMUT; BETZEL, CHRISTIANArtigo IPEN-doc 19552 Rapid purification of serine proteinases from Bothrops alternatus and Bothrops moojeni venoms2013 - OLIVEIRA, LILIANE M.F. de; ULLAH, ANWAR; MASOOD, REHANA; ZELANIS, ANDRE; SPENCER, PATRICK J.; SERRANO, SOLANGE M.T.; ARNI, RAGHUVIR K.Artigo IPEN-doc 12952 Natterins, a new class of proteins with kininogenase activity characterized from Thalassophryne nattereri fish venom2005 - MAGALHAES, G.S.; LOPES-FERREIRA, M.; JUNQUEIRA de AZEVEDO, I.L.M.; SPENCER, P.J.; ARAUJO, M.S.; PORTARO, F.C.V.; MA, L.; VALENTE, R.H.; JULIANO, L.; FOX, J.W.; HO, P.L.; SILVA, A.M.M. daArtigo IPEN-doc 12918 sup(60)Co gamma irradiation prevents Bothrops jararacussu venom neurotoxicity and myotoxicity in isolated mouse neuromuscular junction2002 - SOUZA, FABIO A.D.; SPENCER, PATRICK J.; ROGERO, JOSE R.; NASCIMENTO, NANCI; PAI SILVA, MAELI D.; GALLACCI, MARCIAArtigo IPEN-doc 12919 Phylogenetic conservation of a snake venom metalloproteinase epitope recognized by a monoclonal antobody that netralizes hemorrhagic activity2003 - TANJONI, ISABELLE; BUTERA, DIEGO; SPENCER, PATRICK J.; TAKEHARA, HARUMI A.; FERNANDES, IRENE; SILVA, ANA M.M. da