AI Article Synopsis
- Many species’ eggs have extracellular coats that release signals (ligands) to attract sperm, prompting them to move toward the egg and prepare for fertilization.
- Recent studies have highlighted a specific protein called allurin, which is part of the Cysteine-Rich Secretory Protein (CRISP) family and attracts both amphibian and mammalian sperm.
- Understanding allurin's expression and function could provide valuable insights into how CRISP proteins influence sperm behavior and reproductive processes.
Article Abstract
Eggs of many species are surrounded by extracellular coats that emit ligands to which conspecific sperm respond by undergoing chemotaxis and changes in metabolism, motility, and acrosomal status in preparation for fertilization. Here we review methods used to measure sperm chemotaxis and focus on recent studies of allurin, a 21-kDa protein belonging to the Cysteine-RIch Secretory Protein (CRISP) family that has chemoattraction activity for both amphibian and mammalian sperm. Allurin is unique in being the first extensively characterized Crisp protein found in the female reproductive tract and is the product of a newly discovered amphibian gene within a gene cluster that has been largely conserved in mammals. Study of its expression, function, and tertiary structure could lead to new insights in the role of Crisp proteins in sperm physiology.
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| http://dx.doi.org/10.1016/B978-0-12-394306-4.00007-1 | DOI Listing |
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