Biochemical and enzymatic characterization of two basic Asp49 phospholipase A2 isoforms from Lachesis muta muta (Surucucu) venom

D’Amico, Daniela; Lilla, Sérgio; Nucci, Gilberto De; Ponce-Soto, Luis Alberto; Winck, Flávia Vischi; Novello, José Camillo; Marangoni, Sérgio

doi:10.1016/j.bbagen.2005.05.022

Cited by 41 publications

(49 citation statements)

References 30 publications

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“…1, Table 1) display high N-terminal sequence similarity to the hemolytic and platelet aggregation inhibitory Lm-PLA 2 -I and Lm-PLA 2 -II characterized by Fully et al [47] from L. muta venom provided by Sigma or Fundação Ezequiel Dias (FUNED, Brazil), to LMPA1 (P84651) from the same source, and to two basic neurotoxic Asp49 PLA 2 molecules (LmTX-I and LmTX-II) isolated from L. muta venom purchased from Sigma [48,49] (Table 4). In particular, the N-terminal sequence of the PLA 2 isolated in fraction Lm18 (Table 1) seems to be identical to that of LM-PLA2-II, except for the striking lack of the serine residue at position 16.…”

Section: Moleculesmentioning

confidence: 99%

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Sanz

Escolano

Ferretti

et al. 2008

Journal of Proteomics

127

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This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. were identified in L. muta and L. stenophrys venoms. In addition, both venoms contained a large number of bradykinin-potentiating peptides (BPP) and a C-type natriuretic peptide (C-NP). BPPs and C-NP comprised around 15% of the total venom proteins. In both species, the most abundant proteins were Zn 2+ -metalloproteinases (32-38%) and serine proteinases (25-31%), followed by PLA 2 s (9-12%), galactose-specific C-type lectin (4-8%), L-amino acid oxidase (LAO, 3-5%), CRISP (1.8%; found in L. muta but not in L. stenophrys), and NGF (0.6%).On the other hand, only six L. muta venom-secreted proteins matched any of the previously reported 11 partial or full-length venom gland transcripts, and venom proteome and transcriptome depart in their relative abundances of different toxin families. As expected from their close phylogenetic relationship, the venoms of L. muta and L. stenophrys share (or contain highly similar) proteins, in particular BPPs, serine proteinases, a galactose-specific C-type lectin, and LAO. However, they dramatically depart in their respective PLA 2 complement. Intraspecific quantitative and qualitative differences in the expression of PLA 2 molecules were found when the venoms of five L. muta specimens (3 from Bolivia and 2 from Peru) and the venom of the same species purchased from Sigma were compared.These observations indicate that these class of toxins represents a rapidly-evolving Author's personal copy gene family, and suggests that functional differences due to structural changes in PLA 2 s molecules among these snakes may have been a hallmark during speciation and adaptation of diverging snake populations to new ecological niches, or competition for resources in existing ones. Our data may contribute to a deeper understanding of the biology and ecology of these snakes, and may also serve as a starting point for studying structure-function correlations of individual toxins.

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Section: Moleculesmentioning

confidence: 99%

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Sanz

Escolano

Ferretti

et al. 2008

Journal of Proteomics

127

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“…La enzima es de carácter ácido al ser eluída en el volumen isocrático del primer paso cromatográfico. En trabajos previos realizados en veneno de L. muta de Brasil han caracterizado cuatro isoformas de PLA 2 , siendo dos ácidas y dos básicas (Fuly et al 2002, Damico et al 2005, con características bioquímicas y biológicas distintas a las encontradas en la enzima purificada en este trabajo.…”

Section: Purificación De La Enzima Y Determinación Del Peso Molecularunclassified

Caracterización biológica y acción de inhibidores de una fosfolipasa A2 del veneno de Lachesis muta

et al. 2011

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“…Estudos detalhados da estrutura primária de peptídeos e proteí-nas com atividade farmacológica proveniente da amostra de veneno de diversas espécies animais do Brasil, incluindo Tityus serrulatus, Lonomia obliqua e Bothrops insularis, foram desenvolvidos com o auxílio da espectrometria de massas Q-TOF ("Quadrupole-Time of Flight": quadrupolo-tempo de vôo) 16,17 . A identificação da estrutura primária das proteínas com atividade farmacológica faz parte de um trabalho mais amplo que tem como objetivo final o desenvolvimento de novos fármacos.…”

Section: Proteômicaunclassified

Desafios da química analítica frente às necessidades da indústria farmacêutica

et al. 2005

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The development of liquid chromatography-mass spectrometric (LC-MS) techniques in the last few decades has made possible the analysis of trace amounts of analytes from complex matrices. With LC, the analytes of interest can be separated from each other as well as from the interfering matrix, after which they can be reliably identified thanks to the sensitivity and specificity of MS. LC-MS has become an irreplaceable tool for many applications, ranging from the analysis of proteins or pharmaceuticals in biological fluids to the analysis of toxic substances in environmental samples. In different segments of Brazilian Industry mass spectrometry has an important role, e.g. in the pharmaceutical industry in the development of generic formulations, contributing to the growth of Industry and social inclusion. However, the Brazilian chemists until this moment don't have an effective role in this new segment of the analytical chemistry in Brazil. The present paper shows the actual scenario for mass spectrometry in the pharmaceutical industry, emphasizing the need of a revision of graduation courses to attend the needs of this growing market.Keywords: generic drugs; LC-MS; pharmaceutical industry. INTRODUÇÃOAs últimas décadas do século XVIII foram palco de desenvolvimentos extraordinários que propiciaram o surgimento da quími-ca moderna. Antoine Laurent Lavoisier (1743-1794), com a publicação de seu Traité Elementaire de Chimie (1789), tornou-se o principal protagonista da época de uma nova conceituação sobre como encarar os fenômenos químicos. A partir de suas concepções qualitativas e quantitativas, a investigação química rapidamente tornou-se um ofício rigorosamente científico, com linguagem e metodologia próprias 1 . Entretanto, somente um século mais tarde, em meados de 1940, com o surgimento do espectrômetro UV-visí-vel Beckman DU, houve o início da padronização das técnicas analíticas e da difusão comercial da instrumentação analítica. Antes desse equipamento, a química analítica instrumental era restrita a poucos laboratórios de pesquisa, os quais normalmente produziam seus próprios equipamentos 2 . Nesse ínterim, a química analítica instrumental, principalmente nos campos da espectrometria e espectroscopia, evoluiu significativamente, aumentando as possibilidades analíticas em níveis de sensibilidade e seletividade impensáveis até poucos anos atrás.Uma das técnicas analíticas que ganhou extrema importância no elenco disponível para a indústria farmacêutica foi a cromatografia líquida acoplada à espectrometria de massas.A aplicação da espectrometria de massas à análise de compostos orgânicos não é novidade. Faz mais de 70 anos desde sua primeira aplicação e mais de 30 anos desde o surgimento do primeiro sistema comercial que acoplava a espectrometria de massas à cromatografia gasosa (utilizando colunas capilares) [3][4][5]

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Biochemical and enzymatic characterization of two basic Asp49 phospholipase A2 isoforms from Lachesis muta muta (Surucucu) venom

Cited by 41 publications

References 30 publications

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Caracterización biológica y acción de inhibidores de una fosfolipasa A2 del veneno de Lachesis muta

Desafios da química analítica frente às necessidades da indústria farmacêutica

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