Análise proteômica do coágulo seminal de Sapajus apella
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Data
2024-05-06
Autores
Guilharducci, Raquel Lozano [UNIFESP]
Orientadores
Bertolla, Ricardo Pimenta [UNIFESP]
Tipo
Dissertação de mestrado
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Objetivo: O presente trabalho objetivou a caracterização do proteoma do coágulo seminal de macaco-prego (Sapajus apella), visando a elucidação dos mecanismos biomoleculares que direcionam a coagulação seminal na espécie. Métodos: Foram incluídos nesse estudo três indivíduos de S. apella mantidos aos cuidados humanos. As colheitas seminais foram realizadas via eletroestimulação retal, e as frações coaguladas foram submetidas à análise proteômica através da cromatografia líquida acoplada à espectrometria de massas. Posteriormente à identificação e quantificação dos peptídeos, análises de ontologia gênica e de enriquecimento funcional das vias foram realizadas. Resultados: Foram identificadas ao todo 249 proteínas únicas, com destaque para SEMG1 e TGM4, que atuam na formação do coágulo, e inibidores de proteases como A2M e membros da família das serpinas. A análise ontológica destacou como principal termo para processo biológico a atividade antioxidante, e para função molecular, os termos reportados com maior frequência foram a atividade de peptidases e endopeptidases, expressivamente reportados pelos inibidores de proteases, como A2M, SERPINA1, SERPINA5 e SPINK5. Além das proteínas amplamente conhecidas, chamou a atenção entre as mais abundantes a proteína Ovomucoid-like, cuja correspondente ortóloga em humanos consiste em um membro da família Kazal denominado SPINK9, também com atividade inibitória sobre proteases. Conclusões: Analisando as proteínas identificadas e a frequência dos termos reportados, o presente trabalho sugere que o ponto chave a respeito do coágulo seminal de S. apella não se relaciona principalmente às proteínas que promovem a coagulação seminal, mas sim aos mecanismos que impedem, ou pelo menos dificultam, o processo de liquefação, dando destaque às diferentes classes de inibidores de proteases presentes entre as amostras.
Objective: This study aimed to characterize the seminal clot proteome of tufted capuchin monkey (Sapajus apella) to elucidate the biomolecular mechanisms directing seminal coagulation in the species. Methods: Three individuals of S. apella under human care were included in this study. Seminal samplings were obtained via rectal electrostimulation, and the coagulated fractions underwent proteomic analysis using liquid chromatography coupled to mass spectrometry. Following peptide identification and quantification, gene ontology and functional pathway enrichment analyses were conducted. Results: A total of 249 unique proteins were identified, with notable mentions including SEMG1 and TGM4, implicated in coagulum formation, alongside protease inhibitors such as A2M and members of the serpin family. Ontological analysis highlighted antioxidant activity as the primary biological process term, while peptidase and endopeptidase activity emerged as the most frequent molecular function terms, prominently reported by protease inhibitors like A2M, SERPINA1, SERPINA5, and SPINK5. Additionally, among the most abundant proteins, Ovomucoidlike protein drew attention, whose orthologous counterpart in humans is a member of the Kazal family termed SPINK9, also exhibiting protease inhibitory activity. Conclusions: Analyzing the identified proteins and the frequency of reported terms, this study suggests that the pivotal aspect concerning the seminal coagulum of S. apella lies not primarily in proteins promoting seminal coagulation but rather in mechanisms impeding, or at least hindering, the liquefaction process, with emphasis on the various classes of protease inhibitors present among the samples.
Objective: This study aimed to characterize the seminal clot proteome of tufted capuchin monkey (Sapajus apella) to elucidate the biomolecular mechanisms directing seminal coagulation in the species. Methods: Three individuals of S. apella under human care were included in this study. Seminal samplings were obtained via rectal electrostimulation, and the coagulated fractions underwent proteomic analysis using liquid chromatography coupled to mass spectrometry. Following peptide identification and quantification, gene ontology and functional pathway enrichment analyses were conducted. Results: A total of 249 unique proteins were identified, with notable mentions including SEMG1 and TGM4, implicated in coagulum formation, alongside protease inhibitors such as A2M and members of the serpin family. Ontological analysis highlighted antioxidant activity as the primary biological process term, while peptidase and endopeptidase activity emerged as the most frequent molecular function terms, prominently reported by protease inhibitors like A2M, SERPINA1, SERPINA5, and SPINK5. Additionally, among the most abundant proteins, Ovomucoidlike protein drew attention, whose orthologous counterpart in humans is a member of the Kazal family termed SPINK9, also exhibiting protease inhibitory activity. Conclusions: Analyzing the identified proteins and the frequency of reported terms, this study suggests that the pivotal aspect concerning the seminal coagulum of S. apella lies not primarily in proteins promoting seminal coagulation but rather in mechanisms impeding, or at least hindering, the liquefaction process, with emphasis on the various classes of protease inhibitors present among the samples.
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Citação
GUILHARDUCCI, Raquel Lozano. Análise proteômica do coágulo seminal de Sapajus apella. 2024. 83 f. Dissertação (Mestrado em Urologia) - Escola Paulista de Medicina, Universidade Federal de São Paulo (UNIFESP). São Paulo, 2024.