摩登7平台合作客户/
拜耳公司 |
同济大学 |
联合大学 |
美国保洁 |
美国强生 |
瑞士罗氏 |
相关新闻Info
推荐新闻Info
-
> 磺酸基团修饰水滑石LB复合薄膜自组装机理及酸致变色特性(二)
> 磺酸基团修饰水滑石LB复合薄膜自组装机理及酸致变色特性(一)
> LDH/染料复合LB膜组装过程的多样化和化学气体传感机理研究
> 矿井瓦斯防治:表面活性剂溶液表面张力、泡沫特性及对甲烷缓释效应(三)
> 矿井瓦斯防治:表面活性剂溶液表面张力、泡沫特性及对甲烷缓释效应(二)
> 矿井瓦斯防治:表面活性剂溶液表面张力、泡沫特性及对甲烷缓释效应(一)
> 连铸结晶器内渣钢两相表面张力和界面张力的演变行为与机制
> St与MMA在无皂乳液聚合过程中的动态表面张力变化——结果与讨论、结论
> St与MMA在无皂乳液聚合过程中的动态表面张力变化——摘要、实验部分
> 低分子热塑性树脂体系CBT500/DBTL的界面张力与温度的关联性(二)
应用不同组装的磷脂酰胆碱对牛精浆蛋白的隔离:一种新的技术方法——结论、致谢!
来源:上海谓载 浏览 911 次 发布时间:2021-12-20
5.结论
首先,表面张力测量证明牛精浆具有很好的表面活性,可能与BSP蛋白有关。其次,Langmuir膜法(先前被证明是公牛精子外细胞膜的相关脂质单层模型[35])有助于表征BSP蛋白对脂质膜的亲和力。BSP蛋白能够到达被磷脂覆盖的牛精子细胞表面,这得益于它们与磷脂酰胆碱的相互作用和自身的表面活性。我们的假设是,由于它们自身的表面活性,它们首先穿透精子的外小叶,然后由于与磷脂酰胆碱的强烈相互作用而留在那里。最后,利用Langmuir膜法对已知的BSP蛋白螯合剂如ldl和脂质体的作用进行了筛选。脂质体与低密度脂蛋白一样有效地阻止BSP蛋白插入磷脂层。低密度脂蛋白和脂质体的比例相同:0.16–0.17 mg磷脂酰胆碱/mg BSP。我们还不知道在冷冻保存的时间尺度上脂质体的非常微弱的插入是否有一些生物学后果。需要进一步研究分析每种BSP蛋白的表面性质及其在膜上的作用。此外,可以测试Langmuir膜,以检测BSP与膜的亲和力随温度的变化[20]。最后,Langmuir膜法是一种有效的筛选BSP蛋白质新螯合剂的方法。该方法可适用于其他动物物种。
致谢
作者感谢IMV Technologies(法国)的财务支持,Gérard Chatagnon负责精浆蛋白质定量,Véronique Solé负责凝胶电泳,Maureen Collobert负责英语校正,Alain Sire和Patrice Papineau负责手套箱的构思和实现,允许在受控大气中使用朗缪尔槽。
附录A.补充数据
与本文相关的补充数据可在在线版本中找到,网址为http://dx.doi.org/10.1016/j.colsurfb.2015.11.34
工具书类
[1]F.Ardon,S.S.Suarez,Cryopreservation increases coating of bull sperm by seminal plasma binder of sperm proteins BSP1,BSP3,and BSP5,Reproduction 146(2013)111–117,http://dx.doi.org/10.1530/rep-12-0468.
[2]P.Manjunath,J.Lefebvre,P.S.Jois,J.Fan,M.W.Wright,New nomenclature for mammalian BSP genes,Biol.Reprod.80(2009)394–397,http://dx.doi.org/10.1095/biolreprod.108.074088.
[3]V.Nauc,P.Manjunath,Radioimmunoassays for bull seminal plasma proteins(BSP-A1/-A2,BSP-A3,and BSP-30-Kilodaltons),and their quantification in seminal plasma and sperm,Biol.Reprod.63(2000)1058–1066,http://dx.doi.org/10.1095/biolreprod63.4.1058.
[4]F.S.Esch,N.C.Ling,P.Böhlen,S.Y.Ying,R.Guillemin,Primary structure of PDC-109,a major protein constituent of bovine seminal plasma,Biochem.Biophys.Res.Commun.113(1983)861–867,http://dx.doi.org/10.1016/0006-291x(83)91078-1.
[5]N.G.Seidah,P.Manjunath,J.Rochemont,M.R.Sairam,M.Chrétien,Complete amino acid sequence of BSP-A3 from bovine seminal plasma.Homology to PDC-109 and to the collagen-binding domain of fibronectin,Biochem.J.243(1987)195–203.
[6]J.J.Calvete,K.Mann,L.Sanz,M.Raida,E.Töpfer-Petersen,The primary structure of BSP-30K,a major lipid-,gelatin-,and heparin-binding glycoprotein of bovine seminal plasma,FEBS Lett.399(1996)147–152,http://dx.doi.org/10.1016/s0014-5793(96)1310-5.
[7]D.Salois,M.Ménard,Y.Paquette,P.Manjunath,Complementary deoxyribonucleic acid cloning and tissue expression of BSP-A3 and BSP-30-kDa:phosphatidylcholine and heparin-binding proteins of bovine seminal plasma,Biol.Reprod.61(1999)288–297,http://dx.doi.org/10.1095/biolreprod61.1.288.
[8]P.Manjunath,M.R.Sairam,J.Uma,Purification of four gelatin-binding proteins from bovine seminal plasma by affinity chromatography,Biosci.Rep.7(1987)231–238,http://dx.doi.org/10.1007/bf01124794.
[9]L.Desnoyers,P.Manjunath,Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid,J.Biol.Chem.267(1992)10149–10155.
[10]L.Desnoyers,P.Manjunath,Interaction of a novel class of phospholipid-binding proteins of bovine seminal fluid with different affinity matrices,Arch.Biochem.Biophys.305(1993)341–349,http://dx.doi.org/10.1006/abbi.1993.1431.
[11]P.Müller,K.-R.Erlemann,K.Müller,J.J.Calvete,E.Töpfer-Petersen,K.Marienfeld,et al.,Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles,Eur.Biophys.J.27(1998)33–41,http://dx.doi.org/10.1007/s002490050108.
[12]P.Manjunath,I.Thérien,Role of seminal plasma phospholipid-binding proteins in sperm membrane lipid modification that occurs during capacitation,J.Reprod.Immunol.53(2002)109–119,http://dx.doi.org/10.1016/s0165-0378(01)98-5.
[13]M.Ramakrishnan,V.Anbazhagan,T.V.Pratap,D.Marsh,M.J.Swamy,Membrane insertion and lipid-protein interactions of bovine seminal plasma protein PDC-109 investigated by spin-label electron spin resonance spectroscopy,Biophys.J.81(2001)2215–2225,http://dx.doi.org/10.1016/S0006-3495(01)75869-9.
[14]D.A.Wah,C.Fernández-Tornero,L.Sanz,A.Romero,J.J.Calvete,Sperm coating mechanism from the 1.8Åcrystal structure of PDC-109-phosphorylcholine complex,Structure 10(2002)505–514,http://dx.doi.org/10.1016/s0969-2126(02)751-7.
[15]P.Manjunath,M.R.Sairam,Purification and biochemical characterization of three major acidic proteins(BSP-A1,BSP-A2 and BSP-A3)from bovine seminal plasma,Biochem.J.241(1987)685–692.
[16]R.S.Damai,V.Anbazhagan,K.B.Rao,M.J.Swamy,Fluorescence studies on the interaction of choline-binding domain B of the major bovine seminal plasma protein,PDC-109 with phospholipid membranes,Biochim.Biophys.Acta:Proteins Proteomics.1794(2009)1725–1733,http://dx.doi.org/10.1016/j.bbapap.2009.08.010.
[17]A.Bergeron,M.-H.Crête,Y.Brindle,P.Manjunath,Low-density lipoprotein fraction from hen's egg yolk decreases the binding of the major proteins of bovine seminal plasma to sperm and prevents lipid efflux from the sperm membrane,Biol.Reprod.70(2004)708–717,http://dx.doi.org/10.1095/biolreprod.103.022996.
[18]A.Tannert,E.Töpfer-Petersen,A.Herrmann,K.Müller,P.Müller,The lipid composition modulates the influence of the bovine seminal plasma protein PDC-109 on membrane stability,Biochemistry 46(2007)11621–11629,http://dx.doi.org/10.1021/bi7011299.
[19]I.Thérien,G.Bleau,P.Manjunath,Phosphatidylcholine-binding proteins of bovine seminal plasma modulate capacitation of spermatozoa by heparin,Biol.Reprod.52(1995)1372–1379,http://dx.doi.org/10.1095/biolreprod52.6.1372.
[20]D.Lassiseraye,L.Courtemanche,A.Bergeron,P.Manjunath,M.Lafleur,Binding of bovine seminal plasma protein BSP-A1/-A2 to model membranes:lipid specificity and effect of the temperature,Biochim.Biophys.Acta:Biomembr.1778(2008)502–513,http://dx.doi.org/10.1016/j.bbamem.2007.10.025.
[21]I.Thérien,R.Moreau,P.Manjunath,Major proteins of bovine seminal plasma and high-density lipoprotein induce cholesterol efflux from epididymal sperm,Biol.Reprod.59(1998)768–776,http://dx.doi.org/10.1095/biolreprod59.4.768.
[22]I.Thérien,R.Moreau,P.Manjunath,Bovine seminal plasma phospholipid-binding proteins stimulate phospholipid efflux from epididymal sperm,Biol.Reprod.61(1999)590–598,http://dx.doi.org/10.1095/biolreprod61.3.590.
[23]A.Bergeron,P.Manjunath,New insights towards understanding the mechanisms of sperm protection by egg yolk and milk,Mol.Reprod.Dev.73(2006)1338–1344,http://dx.doi.org/10.1002/mrd.20565.
[24]P.Müller,A.Greube,E.Töpfer-Petersen,A.Herrmann,Influence of the bovine seminal plasma protein PDC-109 on cholesterol in the presence of phospholipids,Eur.Biophys.J.31(2002)438–447,http://dx.doi.org/10.1007/s00249-002-0234-2.
[25]T.S.Witte,S.Schäfer-Somi,Involvement of cholesterol,calcium and progesterone in the induction of capacitation and acrosome reaction of mammalian spermatozoa,Anim.Reprod.Sci.102(2007)181–193,http://dx.doi.org/10.1016/j.anireprosci.2007.07.007.
[26]P.Manjunath,V.Nauc,A.Bergeron,M.Ménard,Major proteins of bovine seminal plasma bind to the low-density lipoprotein fraction of hen's egg yolk,Biol.Reprod.67(2002)1250–1258,http://dx.doi.org/10.1095/biolreprod67.4.1250.
[27]M.-F.Lusignan,A.Bergeron,M.Lafleur,P.Manjunath,The major proteins of bovine seminal plasma interact with caseins and whey proteins of milk extender,Biol.Reprod.85(2011)457–464,http://dx.doi.org/10.1095/biolreprod.110.089961.
[28]L.Amirat,D.Tainturier,L.Jeanneau,C.Thorin,O.Gerard,J.L.Courtens,et al.,Bull semen in vitro fertility after cryopreservation using egg yolk LDL:a comparison with Optidyl®,a commercial egg yolk extender,Theriogenology 61(2004)895–907.
[29]J.A.Foulkes,D.L.Stewart,Fertility of dairy-cattle after artificial-insemination with semen frozen in a lipoprotein diluent,J.Reprod.Fertil.51(1977)175–177.
[30]J.A.Foulkes,Separation of lipoproteins from egg-yolk and their effect on motility and integrity of bovine spermatozoa,J.Reprod.Fertil.49(1977)277–284.
[31]M.Moussa,V.Martinet,A.Trimeche,D.Tainturier,M.Anton,Low density lipoproteins extracted from hen egg yolk by an easy method:cryoprotective effect on frozen-thawed bull semen,Theriogenology 57(2002)1695–1706.
[32]M.M.Pace,E.F.Graham,Components in egg yolk which protect bovine spermatozoa during freezing,J.Anim.Sci.39(1974)1144–1149.
[33]M.Anton,V.Martinet,M.Dalgalarrondo,V.Beaumal,E.David-Briand,H.Rabesona,Chemical and structural characterisation of low-density lipoproteins purified from hen egg yolk,Food Chem.83(2003)175–183,http://dx.doi.org/10.1016/s0308-8146(03)60-8.
[34]M.-F.Lusignan,P.Manjunath,M.Lafleur,Thermodynamics of the interaction between bovine binder of sperm BSP1 and low-density lipoprotein from hen's egg yolk,Thermochim.Acta 516(2011)88–90,http://dx.doi.org/10.1016/j.tca.2011.01.003.
[35]J.Le Guillou,M.H.Ropers,C.Gaillard,E.David-Briand,S.Desherces,E.Schmitt,et al.,Organization of lipids in the artificial outer membrane of bull spermatozoa reconstructed at the air–water interface,Colloids Surfaces B:Biointerfaces 108(2013)246–254,http://dx.doi.org/10.1016/j.colsurfb.2013.02.040.
[36]A.Seelig,Local anesthetics and pressure:a comparison of dibucaine binding to lipid monolayers and bilayers,Biochim.Biophys.Acta 899(1987)196–204,http://dx.doi.org/10.1016/0005-2736(87)90400-7.
[37]P.Manjunath,L.Chandonnet,E.Leblond,L.Desnoyers,Major proteins of bovine seminal vesicles bind to spermatozoa,Biol.Reprod.50(1994)27–37,http://dx.doi.org/10.1095/biolreprod50.1.27.
[38]A.Berthold,H.Schubert,N.Brandes,L.Kroh,R.Miller,Behaviour of BSA and of BSA-derivatives at the air/water interface,Colloids Surfaces A:Physicochem.Eng.Aspects 301(2007)16–22,http://dx.doi.org/10.1016/j.colsurfa.2006.11.054.
[39]V.S.Alahverdjieva,D.O.Grigoriev,J.K.Ferri,V.B.Fainerman,E.V.Aksenenko,M.E.Leser,et al.,Adsorption behaviour of hen egg-white lysozyme at the air/water interface,Colloids Surfaces A:Physicochem.Eng.Aspects 323(2008)167–174,http://dx.doi.org/10.1016/j.colsurfa.2007.12.031.
[40]H.M.Mansour,G.Zografi,Relationships between equilibrium spreading pressure and phase equilibria of phospholipid bilayers and monolayers at the air–water interface,Langmuir 23(2007)3809–3819,http://dx.doi.org/10.1021/la063053o.
[41]L.E.Palacios,T.Wang,Egg-yolk lipid fractionation and lecithin characterization,JAOCS,J.Am.Oil Chem.Soc.82(2005)571–578,http://dx.doi.org/10.1007/s11746-005-1111-4.
[42]C.J.Thomas,V.Anbazhagan,M.Ramakrishnan,N.Sultan,I.Surolia,M.J.Swamy,Mechanism of membrane binding by the bovine seminal plasma protein,PDC-109:a surface plasmon resonance study,Biophys.J.84(2003)3037–3044,http://dx.doi.org/10.1016/s0006-3495(03)70029-0.
[43]U.Dahmen-Levison,G.Brezesinski,H.Möhwald,Specific adsorption of PLA2 at monolayers,Thin Solid Films 327–329(1998)616–620,http://dx.doi.org/10.1016/s0040-6090(98)725-1.
[44]V.Anbazhagan,R.S.Damai,A.Paul,M.J.Swamy,Interaction of the major protein from bovine seminal plasma,PDC-109 with phospholipid membranes and soluble ligands investigated by fluorescence approaches,Biochim.Biophys.Acta:Proteins Proteomics.1784(2008)891–899,http://dx.doi.org/10.1016/j.bbapap.2008.03.002.
[45]V.Anbazhagan,M.J.Swamy,Thermodynamics of phosphorylcholine and lysophosphatidylcholine binding to the major protein of bovine seminal plasma,PDC-109,FEBS Lett.579(2005)2933–2938,http://dx.doi.org/10.1016/j.febslet.2005.04.046.
[46]P.Manjunath,New insights into the understanding of the mechanism of sperm protection by extender components,Anim.Reprod.9(2012)809–815.
[47]M.Gasset,L.Magdaleno,J.J.Calvete,Biophysical study of the perturbation of model membrane structure caused by seminal plasma protein PDC-109,Arch.Biochem.Biophys.374(2000)241–247,10.1006/abbi.1999.1593rS000398619991593X[pii].
[48]A.Greube,K.Müller,E.Töpfer-Petersen,A.Herrmann,P.Müller,Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes,Biochemistry 40(2001)8326–8334,http://dx.doi.org/10.1021/bi010552+.
[49]I.Thérien,S.Soubeyrand,P.Manjunath,Major proteins of bovine seminal plasma modulate sperm capacitation by high-density lipoprotein,Biol.Reprod.57(1997)1080–1088,http://dx.doi.org/10.1095/biolreprod57.5.1080.
[50]M.Lafleur,L.Courtemanche,G.Karlsson,K.Edwards,J.L.Schwartz,P.Manjunath,Bovine binder-of-sperm protein BSP1 promotes protrusion and nanotube formation from liposomes,Biochem.Biophys.Res.Commun.399(2010)406–411,http://dx.doi.org/10.1016/j.bbrc.2010.07.088.