Galectin-3 is associated with prostasomes in human semen
Autor: | Sarika Saraswati, Ashley S. Block, Maha M. Mahadevan, Jennifer L. Jones, Alan B. Diekman, Cheryl F. Lichti |
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Rok vydání: | 2009 |
Předmět: |
Male
medicine.medical_specialty animal structures Surface Properties Galectin 3 Immunoblotting Molecular Sequence Data Semen Plasma protein binding Genitalia Male Biology Biochemistry Article Seminal vesicle Tandem Mass Spectrometry Internal medicine Centrifugation Density Gradient otorhinolaryngologic diseases medicine Humans Biotinylation Amino Acid Sequence Molecular Biology Membranes Secretory Vesicles Vas deferens Antibodies Monoclonal Galactosides Cell Biology Epididymis Sperm Protein Structure Tertiary stomatognathic diseases medicine.anatomical_structure Endocrinology Chromatography Gel Prostasomes Ultracentrifugation Protein Binding Subcellular Fractions |
Zdroj: | Glycoconjugate Journal. 27:227-236 |
ISSN: | 1573-4986 0282-0080 |
Popis: | Galectin-3 is a beta-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 approximately 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 beta-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 galectin-3 and prostasomes in reproduction, disease transmission, and cancer progression. |
Databáze: | OpenAIRE |
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