| Registro completo |
| Provedor de dados: |
Arq. Bras. Med. Vet. Zootec.
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| País: |
Brazil
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| Título: |
Binding patterns of seminal plasma plasma proteins on bovine epididymal and ejaculated sperm membrane
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| Autores: |
Souza,C.E.A.
Moura,A.A.
Lima-Souza,A.C.
Killian,G.J.
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| Data: |
2011-06-01
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| Ano: |
2011
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| Palavras-chave: |
Sperm
Seminal plasma proteins
Immunocytochemistry
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| Resumo: |
The present study was designed to investigate the topographical distribution of seminal plasma (SP) proteins on epididymal and ejaculated bovine sperm. Using immunocytochemistry and confocal microscopy the binding patterns of bovine SP proteins BSP-A3, albumin, transferrin, prostaglandin D-synthase (PGDS) and nucleobindin in ejaculated and cauda epididymal sperm from adult bulls were evaluated. Experiments were performed using sperm from 5 males. Data showed a positive signal, only detected for anti-PGDS, in the acrosomal cap of epididymal and ejaculated sperm. In ejaculated sperm, a very weak signal for nucleobindin 2 in the midpiece and equatorial regions was detected, using the anti-rat nucleobindin. BSP-A3 was detected on all sperm regions studied, with a more evidenced signal in acrosome and midpiece. However, no binding was detected for albumin or transferrin in neither epididymal nor ejaculated sperm. In conclusion, PGDS, BSP-A3 and nucleobindin interact directly with bovine sperm, with specific topographic distribution. These findings may add to the knowledge of how these proteins modulate sperm functions, thus providing fundamental support for studies designed to evaluate how they influence sperm functions.
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0102-09352011000300001
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| Editor: |
Universidade Federal de Minas Gerais, Escola de Veterinária
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| Relação: |
10.1590/S0102-09352011000300001
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| Formato: |
text/html
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| Fonte: |
Arquivo Brasileiro de Medicina Veterinária e Zootecnia v.63 n.3 2011
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| Direitos: |
info:eu-repo/semantics/openAccess
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