| Summary: | CoordenaÃÃo de AperfeÃoamento de Pessoal de NÃvel Superior === O presente estudo foi realizado com o objetivo de identificar o perfil das principais proteÃnas do plasma seminal suÃno e suas associaÃÃes com parÃmetros seminais. Amostras de sÃmen foram coletadas de 12 cachaÃos adultos e submetidas à avaliaÃÃo dos parÃmetros seminais (motilidade total, morfologia, vitalidade e porcentagem de cÃlulas com acrossoma intacto). O plasma seminal foi obtido por centrifugaÃÃo e as proteÃnas seminais foram analisadas por eletroforese 2-D e espectrometria de massa. Foram testados modelos de regressÃo usando a soma das intensidades dos spots referentes Ãs mesmas proteÃnas como variÃveis independentes e parÃmetros seminais como variÃveis dependentes (p < 0,05). Cento e doze spots foram identificados nos gÃis do plasma seminal, equivalentes a 39 proteÃnas diferentes. As espermadesinas PSP-I, PSP-II, AQN1, AQN3 e AWN1 representaram 45,2  8 % do total da intensidade de todos os spots detectados nos geis. Outras proteÃnas expressas no plasma seminal suÃno incluem a albumina, proteÃnas do complemento (complement factor H precursor, complement C3 precursor e adipsin/complement factor D), imunoglobulinas (IgG heavy chain precursor, imunoglobulina delta heavy chain membrane bound form, imunoglobulina gamma-chain, Ig lambda chain V-C region PLC3 e CH4 and secreted domain of swine IgM), IgG-binding proteins, epididymal specific lipocalin-5, epididymal secretory protein E1 precursor, epididymal glutathione peroxidase precursor, transferrin, lactotransferrin e fibronectin tipo 1 (FN1). Em funÃÃo das anÃlises de regressÃo, o percentual de espermatozoides com defeito na peÃa intermediÃria foi relacionado com a quantidade de âCH4 and secreted domain of swine IgMâ e FN1 (R2 = 0,58), a proteÃna IgG-binding (R2 = 0,61), o fator H do complemento (R2 = 0,61) e lactaderina (R2 = 0,45). Porcentagem percentual de defeitos de cauda tambÃm foi relacionado com âCH4 and secreted domain of swine IgMâ e FN1 (R2 =0,40), a proteÃna IgG-binding (R2 = 0,34), e lactaderina (R2 = 0,74). A motilidade espermÃtica, por sua vez, teve associaÃÃo com a intensidade dos spots identificados como lactaderina (R2 = 0,48). Em conclusÃo, descreve-se, neste trabalho, o proteoma do plasma seminal suÃno e associaÃÃes significativas entre proteÃnas especÃficas do plasma seminal e parÃmetros seminais. Tais relaÃÃes servirÃo como base para a determinaÃÃo de marcadores moleculares da funÃÃo espermÃtica na espÃcie suÃna. === The present study was conducted to identify the major seminal plasma protein profile of boars and its associations with semen criteria. Semen samples were collected from 12 adult boars and subjected to evaluation of sperm parameters (motility, morphology, vitality and percent of cells with intact acrosome). Seminal plasma was obtained by centrifugation, analyzed by 2-D SDS-PAGE and proteins identified by mass spectrometry (electrospray ionization quadrupole-time-of-flight). We tested regression models using spot intensities related to the same proteins as independent variables and semen parameters as dependent variables (p < 0,05). One hundred and twelve spots were indentified in the boar seminal plasma gels, equivalent to 39 different proteins. Spermadhesins PSP-I, PSP-II, AQN1, AQN3 and AWN1 represented 45,2  8 % of the total intensity of all spots. Other proteins expressed in the boar seminal plasma include albumin, complement proteins (complement factor H precursor, complement C3 precursor and adipsin/complement factor D), immunoglobulins (IgG heavy chain precursor, immunoglobulin delta heavy chain membrane bound form, immunoglobulin gamma-chain, Ig lambda chain V-C region PLC3 and CH4 and secreted domain of swine IgM), IgG-binding proteins, epididymal specific lipocalin-5, epididymal secretory protein E1 precursor, epididymal secretory glutathione peroxidase precursor, transferrin, lactotransferrin and fibronectin type 1 (FN1). Based on regression analysis, the percentage of sperm with midpiece defects was related to the amount of CH4 and secreted domains of swine IgM and FN1 (R = 0,58), IgG-binding protein (R = 0,61), complement factor H precursor (R = 0,61) and lactadherin (R = 0.45). The percentage of sperm with tail defects was also related to CH4 and secreted domains of swine IgM and FN1 (R = 0,40), IgG-binding protein (R = 0,34) and lactadherin (R = 0,74). Sperm motility, in turn, had association with the intensities of spots identified as lactadherin (R = 0,48). In conclusion, we presently describe the major proteome of boar seminal plasma and significant associations between specific seminal plasma proteins and semen parameters. Such relationships will serve as the basis for determination of molecular markers of sperm function in the swine species.
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