tailieunhanh - Báo cáo khoa học: Purification and characterization of pheromaxein, the porcine steroid-binding protein A member of the secretoglobin superfamily

Low molecular mass proteins are implicated in chemical communication throughout mammalian species, being involved in both perception and delivery of pheromonal compounds. In boars, pheromones are secreted in saliva to cause oestrous sows to take up the mating stance. These pheromones are the 16-androstene steroids, 5a-androsten-3a-ol and 5a-androsten-3-one. The submaxillary glands of boars contain a low molecular mass protein, pheromaxein, which is capable of binding these 16-androstene phero-mones. . | Eur. J. Biochem. 271 2593-2606 2004 FEBS 2004 doi Purification and characterization of pheromaxein the porcine steroid-binding protein A member of the secretoglobin superfamily Corrine J. Austin1 Louise Emberson2 and Peter Nicholls2 1Life Science Unilever R D Colworth Sharnbrook Bedfordshire UK department of Biosciences University of Kent Canterbury Kent UK Low molecular mass proteins are implicated in chemical communication throughout mammalian species being involved in both perception and delivery of pheromonal compounds. In boars pheromones are secreted in saliva to cause oestrous sows to take up the mating stance. These pheromones are the 16-androstene steroids 5a-androsten-3a-ol and 5a-androsten-3-one. The submaxillary glands of boars contain a low molecular mass protein pheromaxein which is capable of binding these 16-androstene pheromones. Pheromaxein was purified cloned and characterized. It was found to be a nonglycosylated heterodimeric protein belonging to the secretoglobin superfamily and the major 16-androstene-binding protein present in submaxillary salivary glands of the boar. One subunit pheromaxein A was found to be homologous to prostatein peptides C1 and C2 and lipophilin A and B whereas the other subunit pheromaxein C was homologous to prostatein peptide C3 and lipophilin C. Transcription of pheromaxein A was limited to the prostate and submaxillary salivary glands from both the boar and sow whereas transcription of the other subunit pheromaxein C was more widespread. This is similar to the transcription distribution of lipophilin in humans. Many isoforms of pheromaxein were found to exist with a molecular mass range of 17 415-18 159 Da these are probably products of a multigene family. Post-translational modifications to generate mature pheromaxein isoforms probably include C-terminal cleavage of pheromaxein A followed by additional modifications. Keywords androstenone lipocalin pheromaxein secreto-globin .