Galectin-3 is associated with prostasomes in human semen.
Galectin-3 is associated with prostasomes in human semen.
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DOI：
10.1007/s10719-009-9262-9
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发表时间：
2010-02
影响因子：
3
通讯作者：
Diekman, Alan B.
中科院分区：
文献类型：
--
作者：
Jones, Jennifer L.;Saraswati, Sarika;Block, Ashley S.;Lichti, Cheryl F.;Mahadevan, Maha;Diekman, Alan B.
半乳糖凝集素-3是一种β-半乳糖苷结合蛋白，参与免疫调节、细胞相互作用、癌症进展和感染性生物体的发病机制。我们报告了人精液中半乳糖凝集素-3的鉴定和表征。在雄性生殖道中，在睾丸、附睾、输精管、前列腺、精囊和精子蛋白提取物中鉴定出~30 kDa半乳糖凝集素-3蛋白。在精浆中，半乳糖凝集素-3在可溶性部分和前列腺体中被鉴定，前列腺体是由前列腺分泌并在射精期间并入精浆的富含胆固醇的膜状囊泡。纯化的前列腺体的二维免疫印迹分析确定了5个半乳糖凝集素-3等电变体，pI范围为7.0至9.2。来自前列腺体的β-半乳糖苷结合蛋白的亲和纯化和串联质谱证实了前列腺体中半乳糖凝集素-3的存在，并鉴定了截短的半乳糖凝集素-3变体。完整的半乳糖凝集素-3分子含有碳水化合物识别结构域和与蛋白质和脂质部分相互作用的非凝集素结构域。具有保守的碳水化合物结合活性的单价半乳糖凝集素-3片段的鉴定表明这种截短的功能相关性，并表明半乳糖凝集素-3在前列腺体中的调节机制。表面生物素化研究表明半乳糖凝集素-3和截短的半乳糖凝集素-3变体定位于前列腺体表面。前列腺体被认为在女性生殖道中具有免疫抑制和精子功能调节的功能，涉及促进性传播感染，并且指示前列腺癌进展。鉴于功能意义的重叠，在前列腺体中鉴定半乳糖凝集素-3为将来研究前列腺体在生殖、疾病传播和癌症进展中的作用奠定了基础。
Galectin-3 is a β-galactoside-binding protein involved in immunomodulation, cell interactions, cancer progression, and pathogenesis of infectious organisms. We report the identification and characterization of galectin-3 in human semen. In the male reproductive tract, the ~30 kDa galectin-3 protein was identified in testis, epididymis, vas deferens, prostate, seminal vesicle, and sperm protein extracts. In seminal plasma, galectin-3 was identified in the soluble fraction and in prostasomes, cholesterol-rich, membranous vesicles that are secreted by the prostate and incorporated into seminal plasma during ejaculation. Two-dimensional immunoblot analysis of purified prostasomes identified five galectin-3 isoelectric variants with a pI range of 7.0 to 9.2. Affinity purification and tandem mass spectrometry of β-galactoside-binding proteins from prostasomes confirmed the presence of galectin-3 in prostasomes and identified a truncated galectin-3 variant. The intact galectin-3 molecule contains a carbohydrate recognition domain and a non-lectin domain that interacts with protein and lipid moieties. The identification of a monovalent galectin-3 fragment with conserved carbohydrate-binding activity indicates the functional relevance of this truncation and suggests a regulatory mechanism for galectin-3 in prostasomes. Surface biotinylation studies suggested that galectin-3 and the truncated galectin-3 variant are localized to the prostasome surface. Prostasomes are proposed to function in immunosuppression and regulation of sperm function in the female reproductive tract, are implicated in facilitating sexually-transmitted infections, and are indicated in prostate cancer progression. Given the overlap in functional significance, the identification of galectin-3 in prostasomes lays the groundwork for future studies of prostasomes in reproduction, disease transmission, and cancer progression.
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影响因子：
13.3
作者：
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通讯作者：
Whittington, K
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Ellerhorst, J;Troncoso, P;Lotan, R
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Lotan, R