Oligomerization of Polymorphic protein CABYR in human sperm fibrous sheath
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Oligomerization of Polymorphic protein CABYR in human sperm fibrous sheath
Journal of Army Medical UniversityVol. 32, Issue 21, Pages: 2263-2268(2010)
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DOI:
CLC:R321.1;R394-33;R394.3
Published:2010
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李彦锋,何畏,梁培禾,张军,孙中义,张勇,王洛夫,靳风烁,Charles J Flickinger,John C Herr.人精子纤维鞘多态性蛋白CABYR的寡聚化作用[J].陆军军医大学学报(原第三军医大学学报),2010,32(21):2263-2268.
Li Yanfeng,He Wei,Liang Peihe,Zhang Jun,Sun Zhongyi,Zhang Yong,Wang Luofu,Jin Fengshuo,Charles J. Flickinger,John C. Herr.Oligomerization of Polymorphic protein CABYR in human sperm fibrous sheath[J].J Amry Med Univ (J Third Mil Med Univ),2010,32(21):2263-2268.
李彦锋,何畏,梁培禾,张军,孙中义,张勇,王洛夫,靳风烁,Charles J Flickinger,John C Herr.人精子纤维鞘多态性蛋白CABYR的寡聚化作用[J].陆军军医大学学报(原第三军医大学学报),2010,32(21):2263-2268.DOI:
Li Yanfeng,He Wei,Liang Peihe,Zhang Jun,Sun Zhongyi,Zhang Yong,Wang Luofu,Jin Fengshuo,Charles J. Flickinger,John C. Herr.Oligomerization of Polymorphic protein CABYR in human sperm fibrous sheath[J].J Amry Med Univ (J Third Mil Med Univ),2010,32(21):2263-2268.DOI:
Oligomerization of Polymorphic protein CABYR in human sperm fibrous sheath
Objective To confirm the formation of oligomers by different isomers of CABYR
a calcium-binding tyrosine phosphorylation-regulated protein. Methods Different human sperm extracts were analyzed by SDS-PAGE
2D IEF/SDS-PAGE
2D diagonal gel electrophoresis
2D blue native/SDS-PAGE and Western blotting
respectively
in native or non-reducing condition and reducing condition. Results The most abundant and
predominant subtype of CABYR in human sperms was CABYR-A with a 86×10
3
variant. Some variants contained both CABYR-A and CABYR-B. CABYR isomers were oligomerized by binding through disulfide bond. A 130×10
3
heterodimer was composed of a 86×10
3
CABYR-A variant and a 50×10
3
variant containing both CABYR-A and CABYR-B. A (200-220)×10
3
isomer contained 86×10
3
variant and a 50×10
3
variant
as well as a 35×10
3
variant (may containing both CABYR-A and CABYR-B) and a 30×10
3
variant (CABYR-A only). Conclusion CABYR isomers can form oligomers mainly by 86×10
3
and 50×10
3
variants
and form large oligomers by binding to other CABYR isomers. CABYR isomers participate in assembly and formation of supra molecular structure of fibrous sheath in human sperms.