The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition
Open Access
- 1 January 2015
- journal article
- review article
- Published by Medknow in Asian Journal of Andrology
- Vol. 17 (4), 568-573
- https://doi.org/10.4103/1008-682x.151395
Abstract
One of the most common lesions present in the spermatozoa of human infertility patients is an idiopathic failure of sperm-egg recognition. Although this unique cellular interaction can now be readily by-passed by assisted reproductive strategies such as intracytoplasmic sperm injection (ICSI), recent large-scale epidemiological studies have encouraged the cautious use of this technology and highlighted the need for further research into the mechanisms responsible for defective sperm-egg recognition. Previous work in this field has established that the sperm domains responsible for oocyte interaction are formed during spermatogenesis prior to being dynamically modified during epididymal maturation and capacitation in female reproductive tract. While the factors responsible for the regulation of these sequential maturational events are undoubtedly complex, emerging research has identified the molecular chaperone, heat shock protein A2 (HSPA2), as a key regulator of these events in human spermatozoa. HSPA2 is a testis-enriched member of the 70 kDa heat shock protein family that promotes the folding, transport, and assembly of protein complexes and has been positively correlated with in vitro fertilization (IVF) success. Furthermore, reduced expression of HSPA2 from the human sperm proteome leads to an impaired capacity for cumulus matrix dispersal, sperm-egg recognition and fertilization following both IVF and ICSI. In this review, we consider the evidence supporting the role of HSPA2 in sperm function and explore the potential mechanisms by which it is depleted in the spermatozoa of infertile patients. Such information offers novel insights into the molecular mechanisms governing sperm function.Keywords
This publication has 95 references indexed in Scilit:
- The Chaperonin Containing TCP1 Complex (CCT/TRiC) Is Involved in Mediating Sperm-Oocyte InteractionOnline Journal of Public Health Informatics, 2011
- The HSP70 chaperone machinery: J proteins as drivers of functional specificityNature Reviews Molecular Cell Biology, 2010
- MOV10L1 is necessary for protection of spermatocytes against retrotransposons by Piwi-interacting RNAsProceedings of the National Academy of Sciences of the United States of America, 2010
- Heat shock proteins on the human sperm surfaceJournal of Reproductive Immunology, 2010
- Linker Histones Stimulate HSPA2 ATPase Activity Through NASP Binding and Inhibit CDC2/Cyclin B1 Complex Formation During Meiosis in the Mouse1Biology of Reproduction, 2009
- Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesisThe Journal of cell biology, 2008
- Guidelines for the nomenclature of the human heat shock proteinsCell Stress and Chaperones, 2008
- Post-meiotic Shifts in HSPA2/HSP70.2 Chaperone Activity during Mouse SpermatogenesisOnline Journal of Public Health Informatics, 2006
- Expression profiling reveals meiotic male germ cell mRNAs that are translationally up- and down-regulatedProceedings of the National Academy of Sciences of the United States of America, 2006
- Molecular Chaperones and Protein Quality ControlCell, 2006