https://nova.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:51128 6,000 proteins, encompassing the selective loss and gain of several hundred proteins. Further, we demonstrate epididymal-driven activation of RHOA-mediated signaling pathways is an important component of sperm maturation. These data contribute molecular insights into the complexity of proteomic changes associated with epididymal sperm maturation.]]> Tue 22 Aug 2023 15:52:22 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:34014 Thu 30 May 2019 15:41:20 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:3007 Sat 24 Mar 2018 08:33:06 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:1595 Sat 24 Mar 2018 08:30:41 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:17300 Sat 24 Mar 2018 08:01:46 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:59 Sat 24 Mar 2018 07:42:05 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:27976 50 = 6.7 nM) led to a significant reduction in dynamin phosphorylation (10.3% vs. 27.3%; P < 0.001), acrosomal exocytosis (9.7% vs. 25.7%; P < 0.01), and in vitro fertilization (53% vs. 100%; P < 0.01). GSK3 was shown to be present in developing germ cells where it colocalized with dynamin in the peri-acrosomal domain. However, additional GSK3 was acquired by maturing mouse spermatozoa within the male reproductive tract, via a novel mechanism involving direct interaction of sperm heads with extracellular structures known as epididymal dense bodies. These data reveal a novel mode for the cellular acquisition of a protein kinase and identify a key role for GSK3 in the regulation of sperm maturation and acrosomal exocytosis.—Reid, A. T., Anderson, A. L., Roman, S. D., McLaughlin, E. A., McCluskey, A., Robinson, P. J., Aitken, R. J., Nixon, B. Glycogen synthase kinase 3 regulates acrosomal exocytosis in mouse spermatozoa via dynamin phosphorylation.]]> Sat 24 Mar 2018 07:38:43 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:30077 Sat 24 Mar 2018 07:31:16 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:22263 in vitro induction of acrosomal exocytosis by progesterone, but not by the calcium ionophore A23187, and elicited a concomitant reduction of in vitro fertilization. In vivo treatment with these inhibitors also resulted in spermatozoa displaying reduced acrosome reaction potential. Dynamin 1 and 2 phosphorylation increased on progesterone treatment, and this was also selectively blocked by dynasore. On the basis of our collective data, we propose that dynamin could regulate specific membrane fusion events necessary for acrosomal exocytosis in mouse spermatozoa.]]> Sat 24 Mar 2018 07:17:38 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:24127 Sat 24 Mar 2018 07:16:32 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:22056 Fri 28 Sep 2018 16:15:17 AEST ]]>