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Foods to improve sex drive in males

If sub-fertility is a problem, making dietary adjustments can be an effective way to boost fertility, without the need for pharmaceuticals or some other form of medical intervention. Carnitine, a compound synthesised from essential amino acids lysine and methionine, is also very important for a healthy sperm count. In addition to supporting sperm production and morphology, arginine and carnitine are also important for motility. The underlying leading cause of sub-fertility in men is oxidative stress as a result of free radical damage to sperm. Research has revealed that sub-fertile males have lower concentrations of glutathione in comparison with fertile males. A diet rich in the amino acids lysine and methionine (required to produce carnitine), arginine and glutathione will help to improve fertility. Lysine and methionine rich foods: dairy, fish, red meat, legumes, whole grains, bananas, apricots, broccoli, asparagus, collard greens, pulses and seeds.
Arginine rich foods: whole grains, nuts, seeds, soy, poultry, dairy products, seafood, red meat and eggs. Glutathione rich foods: walnuts, peaches, watermelon, avocado, broccoli, peas, tomatoes, red meat, poultry, fish, eggs, garlic, onion and brussel sprouts. In addition to amino acids, there are other important compounds needed for healthy fertility.
Some good food sources for this trace element include beef, lamb, oysters, liver, pumpkin seeds, wheat germ and peanuts.
Vitamin C is important for stopping sperm agglutination (clumping or sticking together), increasing sperm count and reducing oxidative stress. The vitamin-like substance Coenzyme Q10 found within mitochondria supports healthy sperm production and motility.
Paying close attention to diet and ensuring that the body has access to vital amino acids, vitamins and minerals will naturally boost fertility.
After 5-7 months of supplementing with a sperm pill, you should experience a semen load that is 4 to 5 times your current level. Science, Technology and Medicine open access publisher.Publish, read and share novel research.
More Than a Simple Lock and Key Mechanism: Unraveling the Intricacies of Sperm-Zona Pellucida BindingKate A. This is partly because this amino acid is an important precursor for vital compounds in sperm, such as spermine, putrescine and spermidine. Studies have shown that these amino acids help with the transport of fatty acids and the conversion of glycol into energy to propel the sperm forward, increasing fertilisation potential. Boosting carnitine and glutathione concentrations can help to protect sperm from oxidative stress. Fertility studies show that glutathione supplementation enhances sperm motility and morphology. Fresh fruit and vegetables are the best sources of vitamin C, especially strawberries, oranges, papaya, kiwi fruit, brussel sprouts, broccoli, capsicum and cauliflower. Ideal food sources for coenzyme Q10 include grapeseed oil, olive oil, soybean oil, avocado, spinach, sesame seeds, beef, chicken and peanuts. Increasing the intake of amino acids lysine, methionine, arginine and glutathione can make a big difference in increasing fertility, as well as overall vitality. Collectively these proteins are believed to participate in the modification of the sperm biochemistry and surface architecture conferring the potential to engage in oocyte interactions.
More specifically, there are certain amino acids, vitamins, minerals and trace elements that support healthy fertility and improve the chances of conception. Increasing the intake of arginine will support the production of healthy sperm and enhance sperm count. Both these amino acids are important antioxidants known to improve sperm quality, especially glutathione. Good sources of selenium include brazil nuts, sunflower seeds, fish, poultry, eggs, mushrooms, onions and grains.
Cholesterol efflux during the early phases of capacitation increases plasma membrane fluidity, facilitating the entry of bicarbonate (HCO3-) and calcium ions (Ca2+) into the sperm cytosol through specific membrane channels.
For instance, female mice bearing targeted deletions of key glycosyltransferase enzymes responsible for the addition of O-linked glycans produce oocytes that display normal sperm binding characteristics (Ellies, et al., 1998). After fertilization, these residues are deglycosylated thereby preventing further sperm adhesion. Of particular importance is the process of spermiogensis, whereby spermatids undergo a process of cytodifferentiation that culminates in the production of spermatozoa.
Cholesterol is preferentially lost from non-membrane raft portions of the plasma membrane, and appears to promote a polarized redistribution of membrane rafts to the anterior region of the sperm head. CapacitationAlthough spermatozoa acquire the potential to fertilize an egg within the epididymis, the expression of this functional competence is suppressed until their release from this environment at the moment of ejaculation.
In the course of this dramatic transformation an acrosomal vesicle is formed in the anterior region of the sperm head and a flagellum develops posteriorly.
Indeed they must first spend a period of time within the female reproductive tract (Austin, 1952, Chang, 1951) during which they undergo the final phase of post-testicular maturation, a process known as capacitation. Following fertilization, ZP2 is processed in such a way that it prevents further sperm adhesion. The plasma membrane is also remodeled to produce zona pellucida (ZP) and hyaluronic acid (HA) binding sites. There is compelling evidence that such dramatic membrane remodeling events may be augmented by the action of molecular chaperones that are themselves activated during capacitation.
Females from these transgenic lines were shown to retain their fertility both in vitro and in vivo, and their oocytes maintained the ability to bind the same number of sperm as wild type mice, strongly suggesting that neither Ser332 nor Ser334 are critical for sperm- zona pellucida recognition. Capacitation is characterized by a series of biochemical and biophysical alterations to the cell including changes in intracellular pH, remodeling of the cell surface architecture, changes in motility patterns and initiation of complex signal transduction pathways. This activation appears to be underpinned by a complex signaling cascade involving cross-talk between several pathways.
The latter findings are perhaps best explained by detailed glycoproteomic analyses that have revealed Ser332 and Ser334 are in fact unlikely to be glycosylated in mouse ZP3 (Boja et al. These events have been correlated with a dramatic global up-regulation of tyrosine phosphorylation across a number of key proteins. In the most well characterized of these, a sperm specific form of soluble adenylyl cyclase (SACY) is activated by increases in intracellular bicarbonate, calcium and pH, leading to the production of the second messenger cyclic AMP (cAMP).
The ensuing activation of these target proteins has, in turn, been causally linked to the initiation of hyperactivated motility, ability to recognize and adhere to the zona pellucida, and the ability to undergo acrosomal exocytosis (Nixon, et al., 2007).
Furthermore, the modification of ZP2 that accompanies fertilization renders these O-glycans inaccessible to sperm.

For the purpose of this review, focus will be placed on the molecular mechanisms that culminate in the ability of the sperm to interact with the zona matrix. This dual regulation results in a global increase in protein tyrosine phosphorylation across a myriad of proteins, including a subset of molecular chaperones, and culminates in the functional activation of the cell. These collective findings have led to the proposal of a number of alternative models of sperm- zona pellucida adhesion (Fig. Furthermore, as this is a cell-surface mediated event, discussion will be centered on the capacitation-associated pathways that mediate sperm surface remodeling. Calcium regulated adenylyl cyclases, phosphodiesterases (PDE), tyrosine kinases and tyrosine phosphatases have also been implicated in various aspects of capacitation associated cell signaling in the spermatozoa of a number of mammalian species. One of the more widely accepted sequences for mammalian capacitation begins with the loss of surface-inhibitory factors, known as decapacitation factors. These factors mostly originate in the epididymis and accessory organs, and their removal from non-capacitated spermatozoa results in a rapid increase in their fertilizing ability (Fraser, 1984). Summary of specific biochemical- and biophysical-changes that occur during mammalian sperm maturation. What is clear from these studies is that the initiation of gamete interaction is not mediated by a simple lock and key mechanism involving a single receptor-ligand interaction. Furthermore, as capacitation is a reversible process, addition of these decapacitation factors into a population of capacitating spermatozoa potently suppress their ability to recognize and fertilize an oocyte (Fraser, et al., 1990). Rather it is likely that sperm engage in multiple binding events with a variety of ligands within the zona pellucida matrix.
An advantage of this complex adhesion system is that it would enhance the opportunities of sperm to bind to the oocyte and thus maximize the chance of fertilization. Following the release of these decapacitation factors, spermatozoa experience a dramatic efflux of cholesterol from the plasma membrane (Davis, 1981). Bovine serum albumin is commonly used within in vitro capacitating media as a cholesterol acceptor, although analogous acceptor(s) are believed to be present within the female reproductive tract. Acquisition of the ability to engage in sperm-zona pellucida interactionsPrior to interaction with the egg, the sperm cell must undergo a complex, multifaceted process of functional maturation (Fig. Indeed, studies of human follicular fluid have identified the presence high concentrations of albumin and other cholesterol sinks (Langlais, et al., 1988). This process begins in the testes where spermatogonial stem cells are dramatically remodeled during spermatogenesis to produce one of the most highly differentiated and specialized cells in the body, the spermatozoon. In addition to its key role in initiation of critical signal transduction cascades, HCO3- has itself been shown to have a more direct role in sperm surface remodeling via stimulation of phospholipid scramblase activity (Gadella and Harrison, 2000, Gadella and Harrison, 2002). After their initial morphological differentiation, these cells are released from the germinal epithelium of the testes in a functionally immature state, incapable of movement or any of the complex array of cellular interactions that are required for fertilization (Hermo, et al., 2010a). The ensuing random translocation of phospholipids between the outer and inner leaflets of the bilayer serves to disrupt the characteristic membrane asymmetry, (Flesch, et al., 2001a). In all mammalian species, the acquisition of functional competence occurs progressively during the cells descent through the epididymis, a long convoluted tubule that connects the testis to the vas deferens (Fig. This redistribution of phospholipids has been suggested to prime the sperm plasma membrane for cholesterol efflux, thus rendering the cell more ‘fusogenic’ and responsive to zona pellucida glycoproteins (Harrison and Gadella, 2005). A remarkable feature of epididymal maturation is that this process is driven entirely by extrinsic factors in the complete absence of nuclear gene transcription and significant protein translation within the spermatozoa (Engel, et al., 1973).
The surface and intracellular changes associated with epididymal maturation prepare the spermatozoa for their final phase of maturation within the female reproductive tract, whereby they realize their potential to bind to the zona pellucida and ultimately fertilize the egg (Bailey, 2010, Fraser, 2010, Yanagimachi, 1994a).
Membrane rafts are generally defined as small, heterogeneous domains that serve to compartmentalize cellular processes (Pike, 2006), and regulate the distribution of membrane proteins, the activation of receptors and initiation of signaling cascades (Brown and London, 1998, Brown and London, 2000, Simons and Ikonen, 1997, Simons and Toomre, 2000).
SpermatogenesisSpermatogenesis describes the process by which spermatozoa develop from undifferentiated germ cells within the seminiferous tubules of the testis.
However despite their stability, rafts remain highly dynamic entities and have been observed to display considerable lateral movement in various cell types as a response to physical stimuli or cellular activation events (Simons and Vaz, 2004). During the proliferation phase, spermatogonial germ cells undergo several mitotic divisions in order to renew themselves in addition to producing spermatocytes (Brinster, 2002, de Rooij, 2001, Dym, 1994, Oatley and Brinster, 2006).
Notably, the spatial distribution of membrane rafts within the sperm membrane is dramatically influenced by the capacitation status of the cells. The latter then develop into spermatozoa via an extremely complex process of cytodifferentiation and metamorphosis. This includes structural modifications to the shape of their nucleus, compaction of the nuclear chromatin, formation of an acrosomal vesicle and establishment of a flagellum allowing for the subsequent Figure 2.Acquisition of spermatozoa’s ability to engage in interaction with the oocyte. This particularly interesting finding raises the possibility that membrane rafts are of significance in coordinating the functional competence of spermatozoa (Bou Khalil, et al., 2006). Consistent with this notion, elegant real time tracking studies have demonstrated that cholesterol efflux initiates diffusion (and possibly formation) of novel membrane raft-like structures containing zona-binding molecules over the acrosome of live spermatozoa.
The importance of SACY has been demonstrated by the fact that sperm from Sacy-null male mice display limited motility (Esposito, et al., 2004).
Furthermore, inhibition of SACY activity in wildtype mice results in the obstruction of capacitation-associated tyrosine phosphorylation and in vitro fertilization (Hess, et al., 2005). The latter series of modifications that produce terminally differentiated spermatozoa from spermatids is referred to as spermiogenesis. Of particular importance to fertilization, is the formation of the acrosome during this stage. As seen by light microscopy, acrosomal development begins with the production of small proacrosome granules derived from the Golgi apparatus that lies adjacent to the early spermatid nucleus. These subsequently fuse together to form the acrosome, a large secretory vesicle that overlies the nucleus (Leblond and Clermont, 1952). There is also evidence to suggest that, in addition to the Golgi apparatus, the plasma membrane of the cell and endocytotic trafficking may also play a fundamental role in the formation of the this exocytotic vesicle (Ramalho-Santos, et al., 2001, West and Willison, 1996). Once formed, the acrosome remains associated with the nucleus of the spermatid, and subsequently the spermatozoa for the remainder of its life, and is of critical importance during fertilization due to its ability to aid in the penetration of the zona pellucida surrounding the ovulated oocyte. This function is, in turn, attributed to the hydrolytic enzymes enclosed within the acrosome. Notwithstanding recent evidence to the contrary, it is widely held that the release of these enzymes occurs upon engagement of sperm binding to the zona pellucida and facilitates localized digestion of the zona matrix, thereby facilitating sperm penetration through this barrier and providing access to the oocyte.
The acrosomal enzymes are mostly derived from the lysosome, although several are unique to this organelle (Tulsiani, et al., 1998).
In general terms, the acrosome can be divided into compartments, the first of which contains soluble proteins such as didpetididyl peptidase II and cystein-rich secretory protein 2 (Hardy, et al., 1991). In addition to the formation of the acrosome during spermiogenesis, the sperm develop a cytoplasmic droplet as well as undergoing plasma membrane remodeling events.
The cytoplasmic droplet was first described by Retzius in 1909 as being a portion of germ cell cytoplasm that remains attached to the neck region of elongating spermatids. The precise function of this residual cytoplasm remains elusive although its retention beyond ejaculation is associated with poor sperm function.

In addition, sperm from Src-null mice contained similar levels of capacitation-associated tyrosine phosphorylation as wild-type sperm. These data indicate that SRC is not directly involved in capacitation-associated changes in tyrosine phosphorylation in mouse spermatozoa. The plasma membrane remodeling event involves the formation of zona pellucida binding sites via protein transport, which is thought to be mediated by the molecular chaperone, HSPA2. In agreement with the observations discussed above, immature human sperm that fail to express HSPA2 display cytoplasmic retention and reduced zona pellucida binding (Huszar, et al., 2000).
It is important to note, that while the above canonical pathway is the primary pathway thought to induce capacitation, there is evidence to suggest that there is significant cross-talk with other signaling pathways. The sperm also develop the machinery necessary for functional motility during spermiogenesis. For instance, it has been demonstrated that a subset of the targets for capacitation associated protein tyrosine phosphorylation are activated by the extracellular signal-regulated kinase (ERK) module of the mitogen-activated protein kinase (MAPK) pathway. As the acrosome grows at one pole of the nuclear surface of round spermatids, paired centrioles migrate to the opposite pole where they initiate the formation of the flagellum.
Interestingly, inhibition of several elements of this pathway results in suppression of sperm surface phosphotyrosine expression and a concomitant reduction in sperm-zona pellucida interactions (Nixon, et al., 2010).
The flagellum consists of a neck piece, a mid piece, a principle piece and an endpiece (Fawcett, 1975, Katz, 1991).
The motility apparatus of the flagellum consists of a central axoneme of nine microtubular doublets arranges to form a cylinder around a central pair of single microtubules (Fawcett, 1975). The diversity of functions regulated by phosphorylation is consistent with the demonstration that this process occurs in a specific sequence within different compartments of the sperm cell, and is altered again upon binding to the zona pellucida (Sakkas, et al., 2003). In combination, these fundamental changes in structure and biochemisty result in terminally differentiated, highly polarized and morphologically mature spermatozoa. In mouse spermatozoa, overt capacitation-associated increases in protein tyrosine phosphorylation have been documented in the flagellum, with principal piece phosphorylation preceding that of the midpiece. However, despite this level of specialization the spermatozoa that leave the testis are functionally incompetent, as yet unable to move forward progressively, nor interact with the zona pellucida and fertilize the oocyte. Several targets have been identified including aldolase A, NADH dehydrogenase, acrosin binding protein (sp32), proteasome subunit alpha type 6B, and voltage-dependent anion channel 2 among others (Arcelay, et al., 2008). They must first traverse the epididymis, a highly convoluted tubule adjacent to the testis, during which time they undergo further biochemical and biophysical changes. The tyrosine phosphorylation of proteins in the sperm flagellum has been causally related to the induction of hyperactivated motility (Mahony and Gwathmey, 1999, Nassar, et al., 1999, Si and Okuno, 1999), a vigorous pattern of motility that is required for spermatozoa to penetrate through the cumulus cell layer and the zona pellucida in order to reach the inner membrane of the oocyte. Epididymal maturationUpon leaving the testes, the first region of the epididymis that immature sperm encounter is that of the caput (head). In addition, to the increased phosphorylation, hyperactivation requires the alkalinization of the sperm and is also calcium-dependent. As they leave this environment and enter the corpus (body) epididymis, sperm begin to acquire their motility and fertilizing ability. These attributes continue to develop as the sperm move through the corpus, and reach an optimum level as they reach the cauda (tail) region where they are stored in a quiescent state prior to ejaculation (Fig. Ground breaking research performed in the 1960’s and 1970’s provided the first evidence that the epididymis played an active role for the epididymis in sperm development (Bedford, 1963, Bedford, 1965, Bedford, 1967, Bedford, 1968, Orgebin-Crist, 1967 a, Orgebin-Crist, 1967b, Orgebin-Crist, 1968, Orgebin-Crist, 1969). Furthermore, these phosphoproteins are present on virtually all sperm that are competent to adhere to the zona pellucida opposed to less than one quarter of sperm in the free swimming population. Most importantly, it was discovered that if sperm were held in the testis via ligation of the epididymal duct, they were unable to develop the ability to fertilize an ovum, and as such their maturation is not an intrinsic property (Cooper and Orgebin-Crist, 1975, Cooper and Orgebin-Crist, 1977).Consistent with this notion, sperm maturation within the epididymis is not under genomic control, since the cells enter the ductal system in a transcriptionally inactive state with limited biosynthetic capacity (Eddy, 2002).
Although such findings invite speculation that a subset of proteins targeted for phosphotyrosine residues may directly participate sperm-zona pellucida adhesion, this conclusion is at odds with the fact that pre-incubation of sperm with anti-phosphotyrosine antibodies has no discernible effect on their subsequent fertilizing ability (Asquith, et al., 2004). Any subsequent molecular changes must therefore be driven by the dynamic intraluminal milieu in which they are bathed as they transit the length of the epididymal tubule (Cooper, 1986). Rather it has been suggested that, following their activation via phosphorylation, these proteins play an indirect role by mediating sperm surface remodeling to render cells competent to engage in zona pellucida adhesion (Fig. The unique physiological compartments established by this activity are thought to have evolved to not only to support the maturation of spermatozoa, but to also to provide protection for the vulnerable cells during their transport and prolonged storage. In agreement with this proposal, a subset of phosphorylated proteins have been identified in the mouse as the molecular chaperone proteins heat shock protein (HSP) 60 (HSPD1) and endoplasmin (HSP90B1) (Asquith, et al., 2004). This progressive motion not only allows the sperm to negotiate the female reproductive tract, but has also been suggested to play a role in penetration of the oocytes outer protective barriers, including the cumulus oophorous and the zone pellucida. To date, the mechanisms underlying the acquisition of forward motility by cauda epididymal sperm have not been completely elucidated.
On a biochemical level, proteins from caput epididymal sperm contain a greater number of sulfhydryl groups than disulfide bonds. Additionally, there is also recent evidence to suggest that sperm isolated from the caput epididymis possess the ability to become motile, but that this activity is suppressed through the action of the cannaboid receptor CNR1, which upon engagement with its ligand, t ennocanaboid 2-arachidonoylglcerol, suppresses the capacity for motility (Cobellis, et al., 2010).
Furthermore, changes in the luminal environment, as well as specific post-translational modification to sperm proteins have been shown to affect the motility status of these cells during their transit through the epididymis. In relation to the former, acidification of the luminal contents of the epididymis work to maintain sperm in an immotile state. In terms of post-translational modifications, proteomic analyses of sperm proteins within the epididymis have identified a number of potential targets affected by changes in expression, disulfide bond status, proteolysis and alterations such as phosphorylation (Baker, et al., 2005). Finally, glycolysis plays an essential role as an energy pathway to fuel forward progressive movement in mouse spermatozoa. In part this can be explained by significantly decreased levels of ATP production (4 to 10-times lower than wildtype sperm) resulting in poor, or sluggish motility. Furthermore, the spermatogenic cell-specific type 7 hexokinase that is present in mouse spermatozoa undergoes cleavage of dilsulfide bonds during epididymal transit, resulting in increased hexokinase activity which, in turn, has been causally associated with the initiation of sperm motility (Nakamura, et al., 2008). This indicates that specific structural changes to proteins during epididymal maturation have functional consequences, improving sperm competence for motility, and subsequently their ability to engage in fertilization. This is in keeping with the demonstration that biotinylated proteins are able to be transferred between epididymosomes and the sperm surface (Saez, et al., 2003). At present it remains to be determined how this transfer is mediated and the number of cargo proteins that are delivered to the maturing spermatozoa in this manner. Nevertheless, a number of proteins have been shown to be acquired by the sperm during epididymal transit.

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