Functional processing of fertilin: evidence for a critical role of proteolysis in sperm maturation and activation.

@article{Blobel2000FunctionalPO,
  title={Functional processing of fertilin: evidence for a critical role of proteolysis in sperm maturation and activation.},
  author={Carl P. Blobel},
  journal={Reviews of reproduction},
  year={2000},
  volume={5 2},
  pages={
          75-83
        }
}
  • C. Blobel
  • Published 1 May 2000
  • Biology, Medicine
  • Reviews of reproduction
Fertilin is a sperm surface protein with an essential role in fertilization. It is required for the migration of spermatozoa through the oviduct, for binding to the zona pellucida, and for efficient binding to the egg plasma membrane. Fertilin consists of two subunits, fertilin alpha and beta, both of which belong to the metalloprotease-disintegrin protein family (ADAMs). Fertilin alpha and beta are made as larger precursors that are processed proteolytically at different stages of sperm… 
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Role of tetraspanin CD9 molecule in fertilization of mammals.
TLDR
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Post-testicular sperm environment and fertility.
TLDR
It is found that the main secreted proteins are common in different species and that enzymatic activities, capable of controlling the sperm surface changes, are present in the fluid.
Sperm Maturation in Epididymis
TLDR
The epididymal maturation of mammalian sperm is discussed, which is a unique organ that is crucial for male fertility and creates a special environment for storing mature sperm for long periods of time until ejaculation.
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References

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TLDR
It is demonstrated that one or more serine protease activities associated with testicular sperm can process fertilin beta in vitro in a fashion that closely mimics the processing pattern observed in vivo during epididymal sperm maturation.
Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis.
TLDR
Evidence is reported that a common mechanism may be used to change the localization pattern of other sperm surface molecules, shown to become localized to either the posterior or the anterior head membrane domains on sperm at the same time fertilin became localized to the posterior head.
Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence
TLDR
A protein located on the surface of guinea pig sperm (PH-30) has been implicated in the process of sperm-egg fusion and the possible role of PH-30 in mediating fusion with the egg plasma membrane is discussed.
Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion.
TLDR
Results show that the disintegrin domain of fertilin beta binds to the egg plasma membrane and that this binding is required for membrane fusion.
Cloning and sequence analysis of rat fertilin alpha and beta--developmental expression, processing and immunolocalization.
TLDR
Fertilin alpha mRNA was present at all stages of development, suggesting that it is not exclusively expressed in post-meiotic germ cells, and fertilin beta mRNA was first identified in day 19 testes, coincident with the presence of pachytene spermatocytes.
Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm-egg binding.
TLDR
The predicted extracellular domain of mouse fertilin alpha is expressed as a bacterial fusion protein with maltose-binding protein, which binds to the microvillar region of zona pellucida (ZP)-free eggs and inhibits the binding of sperm to eggs during in vitro fertilization of ZP-free eggs.
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TLDR
It is suggested that barriers to membrane protein diffusion exist at the equatorial region, the posterior ring, and the annulus and that they are responsible for maintaining a localized distribution of at least some of the surface proteins.
Testicular biosynthesis and epididymal endoproteolytic processing of rat sperm surface antigen 2B1.
TLDR
The hypothesis that sperm antigens that are important for fertilization are synthesized as precursor molecules in the testis and are then "activated' during epididymal maturation and capacitation, thereby ensuring that they only become fully functional at the site of fertilization is supported.
Rat sperm plasma membrane mannosidase: localization and evidence for proteolytic processing during epididymal maturation.
TLDR
It is demonstrated that the sperm mannosidase is an integral plasma membrane component of the rat sperm and is localized on the periacrosomal region of the sperm head, and proteolytic processing of the membrane-bound alpha-D-mannosidase during maturation of spermatozoa is demonstrated.
Surface expression of the pre-beta subunit of fertilin is regulated at a post-translational level in guinea pig spermatids.
TLDR
Results suggest that the appearance of fertilin pre-beta subunit on the spermatid surface is regulated by a post-translational mechanism.
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