Biochemical and Biophysical Research Communications
Delivery of ferric ion to mouse spermatozoa is mediated by lipocalin internalization
Section snippets
Materials and methods
Chemicals, biochemicals, and bio-assay kits. An Enhanced Chemiluminescence plus kit (ECL) was purchased from Amersham–Pharmacia Biotech (Buckinghamshire, UK). Anti-rabbit IgG-horseradish peroxidase conjugate (HRP-conjugated anti-rabbit IgG) prepared from goats and fluorescein isothiocyanate (FITC) were obtained from Sigma (St. Louis, MO, USA). Desferrioxamine mestylate (DFO) and diethylene triamine pentaacetic acid (DTPA) were purchased from Sigma (St. Louis, MO, USA). A permeable ester form of
24p3 protein accumulation in the spermatozoa cytosol
As described previously, the epididymal caput was found to produce a large quantity of 24p3 protein in luminal fluid and was also found to be associated with caudal spermatozoa, for which the 24p3 protein had virtually vanished [14]. To test whether there was any further processing of the spermatozoa in the epididymal caput after protein association, we extracted the proteins from the different portions of the caput spermatozoa. Using Western blotting, we detected the location of 24p3 protein
Discussion
A prerequisite for understanding the physiological function of lipocalins is some knowledge pertaining to the mode of delivery of the bound ligands into the cells. Evidence suggests that lipocalin binds to certain cells and internalizes the protein into these cells [16], whereas others suggest that the lipocalin present creates a direct signal that induces various physiological processes to commence [26]. The interaction of 24p3 protein with murine spermatozoa resulting in an increase in the
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Lipocalin 2 as a link between ageing, risk factor conditions and age-related brain diseases
2021, Ageing Research ReviewsCitation Excerpt :Thirdly, it was reported that Lcn2 can bind to and partly inhibit the activity of hepatocyte growth factor (HGF), thereby reducing HGF-stimulated cell branching in kidney tubular epithelial cells (Gwira et al., 2005). Fourth, Lcn2 was found to attach to the sperm membrane by binding to membrane phosphatidylethanolamine (PE), which resulted in stimulation of lipid raft movement and cholesterol efflux (Chu et al., 2000; Elangovan et al., 2004; Watanabe et al., 2014). The mechanisms that underlie these Lcn2-mediated effects in the sperm membrane however are not clear yet (Watanabe et al., 2014).
Deficiency for Lcn8 causes epididymal sperm maturation defects in mice
2021, Biochemical and Biophysical Research CommunicationsCitation Excerpt :In the current study, normal fertility was detected in Lcn8−/− and Lcn9−/− male mice, and only sperm maturation defect was found in Lcn8−/− male mice. As mentioned before, lipocalin is a superfamily, and many homologous genes are specifically expressed in the epididymis, especially Lcn2, Lcn5, Lcn6, and Lcn10 are expressed in the caput epididymis, which is similar or adjacent to the expressed location of Lcn8 and Lcn9 [20,21,39]. These genes may have redundant functions with Lcn8 and Lcn9, which could make up for the knockout of Lcn8 or Lcn9.
Metabolism and adult neurogenesis: Towards an understanding of the role of lipocalin-2 and iron-related oxidative stress
2018, Neuroscience and Biobehavioral ReviewsCitation Excerpt :Contrastingly, apo-LCN2 internalization chelates intracellular iron and transfers it to the extracellular medium, reducing its intracellular levels (Devireddy et al., 2005). Importantly, this modulation of cell iron content was shown to impact cell proliferation and apoptosis (Devireddy et al., 2005) and was described to be relevant in kidney development (Yang et al., 2002) during acute anemia (Miharada et al., 2005), in iron delivery to spermatozoa (Elangovan et al., 2004), and in the attenuation of iron-related oxidative stress (Yamada et al., 2016). In the CNS, less is known about the processes involving LCN2, namely, by which cells it is produced/secreted, and its impact on overall brain functioning [see (Ferreira et al., 2015)].
From the periphery to the brain: Lipocalin-2, a friend or foe?
2015, Progress in NeurobiologyCitation Excerpt :With the exception of a report questioning the role of LCN2 in the modulation of iron metabolism (Correnti et al., 2012), which suggested that LCN2 does not induce cellular iron efflux, many others studies support the participation of LCN2 in cellular iron homeostasis. For instance, the delivery of iron to spermatozoa, at the caudal epididymis, was demonstrated to occur through the internalization of holo-LCN2, disclosing a physiological role for LCN2 in spermatozoa in the context of protein-ligand complex internalization (Elangovan et al., 2004). Also, LCN2 has been shown to induce apoptosis of haematopoietic cells (Devireddy et al., 2001; Lin et al., 2005; Liu et al., 2011; Miharada et al., 2005) and to inhibit the survival and differentiation of erythroid cells in vitro (Miharada et al., 2005).
The Epididymis
2015, Knobil and Neill's Physiology of Reproduction: Two-Volume SetGlycomics and proteomics analyses of mouse uterine luminal fluid revealed a predominance of Lewis Y and X epitopes on specific protein carriers
2009, Molecular and Cellular ProteomicsCitation Excerpt :The 24p3 protein has been implicated in diverse physiological processes, including apoptosis, iron transport, proinflammatory processes, and cell survival (43–46). Notably in the context of the reproductive system, functional interactions with spermatozoa have been indirectly demonstrated through its sperm motility-enhancing and acrosome reaction-suppressing activities (32, 47) as well as its internalization for ferric ion delivery (48). Here we provided evidence that 24p3 could directly bind to spermatozoa and showed by sperm motility assay that co-incubation of 24p3 with oligosaccharides containing specific fucosylated terminal epitopes in the forms of Lex, Ley, and type II H, but not terminal LacNAc or 6′-sialyl LacNAc, would attenuate its enhancer activity.