Role of a capacitation-related protein on some sperm functional parameters.
نویسندگان
چکیده
In previous studies a series of Mabs against boar capacitated sperm have been produced. One of these Mabs--4B12--was found to recognize a surface membrane-associated protein located in the acrosome portion of the spermatozoa that became accessible to antibody after capacitation. In biological experiments it was shown that Mab 4B12 significantly inhibited boar sperm-porcine ZP binding. In attempts to investigate the mechanisms by which Mab 4B12 affected sperm-ZP binding, the role of the cognate protein on some functional parameters such as sperm motility and ability of the capacitated spermatozoa to undergo AR was studied. Experimental models of premature AR and AR physiologically induced with ZP were applied to study the effect of Mab 4B12 on boar sperm AR using PSA staining to estimate the acrosome-reacted state of spermatozoa. Sperm motility characteristics were determined by the time-exposure photokinesigraphic method. The results obtained in the present study, together with previously established inhibition of sperm-ZP binding by Mab 4B12, documented the participation of the 4B12 protein in primary sperm-ZP binding. The protein is not connected with sperm motility and secondary sperm-ZP binding.
منابع مشابه
I-6: Role of Actin Cytoskeleton during Mouse Sperm Acrosomal Exocytosis
Background: Mammalian sperm must undergo a process termed capacitation to become competent to fertilize an egg. Capacitation renders the sperm competent by priming the cells to undergo a rapid exocytotic event called acrosomal exocytosis that is stimulated by the zona pellucida (ZP) of the egg or progesterone. Over the years, several biochemical events have been associated with the capacitation...
متن کاملP-57: Evaluation of HSPA2 in Fertile and Infertile Individuals
Background: Heat-shock protein A2 (HspA2) is a testisspecific member of the HSP70 family known to play a critical role in spermatogenic cell differentiation. HspA2 is correlated with sperm maturity, function and fertility, and diminished expression of HspA2 results in abnormal sperm maturity and infertility. The aim of this study was to compare expression of HspA2 in fertile and infertile indiv...
متن کاملReorganization of mouse sperm lipid rafts by capacitation.
One of the hallmarks of mammalian sperm capacitation is the loss of cholesterol from the plasma membrane. Cholesterol has been associated with the formation of detergent insoluble membrane microdomains in many cell types, and sperm from several mammalian species have been shown to contain detergent-resistant membranes (DRMs). The change in cholesterol composition of the sperm plasma membrane du...
متن کاملCalmodulin antagonists differentially affect capacitation-associated protein tyrosine phosphorylation of mouse sperm components.
Sperm capacitation in vitro is thought to be correlated with the increased protein tyrosine phosphorylation of a subset of sperm components. Our group recently used a pharmacological approach to demonstrate that calmodulin (CaM), a 17 kDa calcium sensor protein, has a role in sperm capacitation. In the present study, we have used several CaM antagonists in an attempt to characterize further the...
متن کاملImpact of Reactive Oxygen Species on Spermatozoa: ABalancing Act between Beneficial and Detrimental Effects
Reactive oxygen species (ROS)plays an important role in sperm motility. The physiological generation at low concentration induces beneficial effects on sperm functions and plays a significant role in sperm metabolism. Meanwhile, the excessive generation of reactive oxygen species can overwhelm protective mechanism and triggers changes in lipid and protein layers of sperm plasma membrane, which ...
متن کاملذخیره 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 ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Folia biologica
دوره 48 6 شماره
صفحات -
تاریخ انتشار 2002