Spatio-temporal organization of Vam6P and SNAP on mouse spermatozoa and their involvement in sperm-zona pellucida interactions.

نویسندگان

  • M Brahmaraju
  • Mohammed Shoeb
  • Malini Laloraya
  • Pradeep G Kumar
چکیده

Acrosomal assembly during spermatogenesis and acrosome reaction during sperm-oocyte interaction are unique events of vesicle synthesis, transport, and fusion leading to fertilization. SNARE complex formation is essential for membrane fusion, and vesicle-associated (v-) SNARE intertwines with target membrane (t-) SNARE to form a coiled coil that bridges two membranes and facilitates fusion. We detected messages of Vam6P and SNAP in mammalian testis and epididymis. Vam6P and SNAP were detected in a temporally organized fashion on the spermatozoa from testis and epididymis, which showed accumulation on the principal acrosomal domains during capacitation. Vam6P and SNAP were shed off from the principal acrosomal domain after acrosome reaction, but the equatorial and the post-acrosomal domains retained these proteins. Antibodies to VAMP and SNAP inhibited sperm-zona pellucida interaction, suggesting their possible involvement in sperm membrane vesiculation.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

I-13 Infertility with Impaired Zona Pellucida Adhesion of Spermatozoa from Mice LackingTauCstF-64

Background: Fertilization is a multistep process requiring spermatozoa with unique cellular structures and numerous germ cell-specific molecules that function in the various steps. In the highly coordinated process of male germ cell development, RNA splicing and polyadenylation help regulate gene expression to ensure formation of functional spermatozoa. Male germ cells express tauCstF-64 (Cstf2...

متن کامل

Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization.

To fuse with oocytes, spermatozoa of eutherian mammals must pass through extracellular coats, the cumulus cell layer, and the zona pellucida (ZP). It is generally believed that the acrosome reaction (AR) of spermatozoa, essential for zona penetration and fusion with oocytes, is triggered by sperm contact with the zona pellucida. Therefore, in most previous studies of sperm-oocyte interactions i...

متن کامل

Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition.

Mammalian spermatozoa undergo a series of molecular and biochemical changes collectively termed capacitation prior to acquiring the ability to fertilise the oocyte. Although phosphorylation of sperm proteins on tyrosine residues has been recognised as an important component of this process, the precise relationship between the phosphorylation status of mammalian spermatozoa and their capacity f...

متن کامل

Zonadhesin is essential for species specificity of sperm adhesion to the egg zona pellucida.

Interaction of rapidly evolving molecules imparts species specificity to sperm-egg recognition in marine invertebrates, but it is unclear whether comparable interactions occur during fertilization in any vertebrate species. In mammals, the sperm acrosomal protein zonadhesin is a rapidly evolving molecule with species-specific binding activity for the egg zona pellucida (ZP). Here we show using ...

متن کامل

O-11: Dynamics of Flagellar Force Generated by A Hyperactivated Spermatozoon

Background: To clarify the mechanism of sperm penetration through the zona pellucida, the flagellar force generated by a hyperactivated spermatozoon was evaluated using the resistive force theory applied to the hyperactivated flagellar waves that were obtained from the mammalian spermatozoa. Materials and Methods: The hydrodynamic calculation of the flagellar force of the activated (non-hyperac...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochemical and biophysical research communications

دوره 318 1  شماره 

صفحات  -

تاریخ انتشار 2004