Influence of pentoxifylline in severe male factor infertility

Yovich, Jeanne M.; Edirisinghe, W. Rohini; Cummins, James M.; Yovich, John L.

doi:10.1016/s0015-0282(16)53470-0

Cited by 203 publications

(87 citation statements)

References 20 publications

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“…Pentoxifylline has been used extensively as a sperm motility enhancer in fresh ejaculates, post-thaw semen samples and testicular sperm [10,13,14]. The clinical experience with pentoxifylline has contradictory reports in the literature.…”

Section: Discussionmentioning

confidence: 99%

“…The clinical experience with pentoxifylline has contradictory reports in the literature. Even though a majority of the studies found a significant improvement in the motility after pentoxifylline treatment [10,[13][14][15], few have observed either no Fig. 1 The total motility pattern in frozen-thawed semen samples processed in media supplemented with biotin (10 nM) and pentoxifylline (1 mM) (n0105) at different hours after incubation in vitro.…”

Section: Discussionmentioning

confidence: 99%

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Supplementation of biotin to sperm preparation medium increases the motility and longevity in cryopreserved human spermatozoa

Kalthur¹,

Salian²,

Keyvanifard³

et al. 2012

J Assist Reprod Genet

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Purpose To study the effect of supplementing biotin to sperm preparation medium on the motility of frozen-thawed spermatozoa. Methods Semen samples of men attending the University infertility clinic (n0105) were cryopreserved using glycerolegg yolk-citrate buffered cryoprotective medium in liquid nitrogen. After a period of two weeks, the semen samples were thawed and the motile spermatozoa were extracted by swim-up technique using Earle's balanced salt solution (EBSS) medium supplemented with either biotin (10 nM) or pentoxifylline (1 mM). The post-wash motility was observed up to 4 h after incubation. Results Both biotin and pentoxifylline supplementation resulted in significant increase in total motility (p<0.05), progressive motility (p<0.001) and rapid progressive motility (p<0.05 v/s biotin and p<0.01 v/s pentoxifylline) compared to the control at 1 h post-incubation period. Significantly higher percentage of total (p<0.01, p<0.05 in biotin and pentoxifylline respectively), progressive (p<0.001) and rapid progressive motilities (p<0.01) were observed in these two groups even at 2 h compared to the control. In the control group at 4 h after incubation,~11% decline in total motility and 8% decline in progressive motility was observed. However, in both biotin and pentoxifylline group the motility was significantly higher than control (p<0.001). No significant difference in the motility was observed between biotin and pentoxifylline groups at any of the time intervals studied. Conclusions Biotin can enhance the sperm motility and prolong the survival of frozen-thawed semen samples which may have potential benefit in assisted reproductive technology field.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Supplementation of biotin to sperm preparation medium increases the motility and longevity in cryopreserved human spermatozoa

Kalthur¹,

Salian²,

Keyvanifard³

et al. 2012

J Assist Reprod Genet

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“…Pharmacological stimulants that elevate intracellular cAMP, such as the phosphodiesterase inhibitors, caffeine, and pentoxifylline, enhance hyperactivated motility of sperm (13). cAMP agonists can accelerate protein tyrosine phosphorylation in sperm, whereas antagonists of PKA inhibit tyrosine phosphorylation and capacitation (14).…”

mentioning

confidence: 99%

FSCB, a Novel Protein Kinase A-phosphorylated Calcium-binding Protein, Is a CABYR-binding Partner Involved in Late Steps of Fibrous Sheath Biogenesis

Wang

Jha

et al. 2007

Journal of Biological Chemistry

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We report characterization of a novel testis-and sperm-specific protein, FSCB (fibrous sheath CABYR binding), that is expressed post-meiotically and localized in mouse sperm flagella. FSCB was identified as a binding partner of CABYR, a calcium-binding protein that is tyrosine-phosphorylated during capacitation. Orthologous genes of FSCB are present in other mammals, including rat and human, and conserved motifs in FSCB include PXXP, proline-rich and extensin-like regions. FSCB is phosphorylated by protein kinase A as shown by in vitro phosphorylation assay and also by determining phosphorylation sites in native FSCB from mouse sperm. Calcium overlay assay showed that FSCB is a calcium-binding protein from sperm. FSCB is a post meiotic protein first expressed at step 11 of mouse spermatogenesis in the elongating spermatids, and it subsequently incorporates into the flagellar principal piece of the sperm. Ultrastructurally, FSCB localized to a cortical layer of intermediate electron density at the surface of the ribs and longitudinal columns of the fibrous sheath. Due to its temporal appearance during spermiogenesis and location at the cortex of the fibrous sheath, FSCB is postulated to be involved in the later stages of fibrous sheath assembly.Hyperactivated motility along with changes in the sperm head that confer the capacity to fertilize an oocyte result from a series of time-dependent processes collectively referred to as capacitation (1, 2). Although the molecular mechanisms underlying capacitation, including hyperactivation, are incompletely understood, some fundamental processes related to capacitation have been elucidated.The presence of a protein source such as albumin, bicarbonate, and Ca 2ϩ and an energy substrate such as glucose, pyruvate, or lactate are essential to achieve in vitro capacitation (3). Capacitation is also marked by an increase in tyrosine phosphorylation through a unique signal transduction cascade involving a sperm-specific soluble adenylyl cyclase, protein kinase A (PKA), 3 and tyrosine kinase(s). A variety of factors, including Ca 2ϩ, HCO 3 Ϫ , and H 2 O 2 stimulate soluble adenylyl cyclase leading to increased cytosolic levels of cAMP (4). This increase in cAMP then activates PKA, and the consequence is a significant increase in tyrosine phosphorylation of protein substrates localized in the flagellum such as AKAP3, AKAP4, CABYR, hsp-90, ODF2, and tubulin (3,(5)(6)(7)(8)(9)(10)(11)(12).The fact that PKA is a key regulator of capacitation-associated changes such as protein phosphorylation and hyperactivation has been well established. Pharmacological stimulants that elevate intracellular cAMP, such as the phosphodiesterase inhibitors, caffeine, and pentoxifylline, enhance hyperactivated motility of sperm (13). cAMP agonists can accelerate protein tyrosine phosphorylation in sperm, whereas antagonists of PKA inhibit tyrosine phosphorylation and capacitation (14). Mice in which sperm-specific PKA ␣ is knocked out are infertile, owing to the complete absence of normal sperm movement...

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“…Pentoxifylline improves the success rates of in vitro fertilization in oligo-or asthenozoospermic patients [27]. However, the mutagenic effects of methylxanthines, especially of metabolites of caffeine, have been under debate [ 151.…”

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confidence: 99%

Effect of Pentoxifylline on Sperm Motion

Fuse

Sakamoto

Katayama

1993

Archives of Andrology

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The ability of pentoxifylline to stimulate sperm motility characteristics was assessed. The effect of pentoxifylline was immediate and lasted for 240 min. The percent motility was increased 1.5-fold when compared with the control at 120, 180, and 240 min after pentoxifylline treatment. Significant increases in velocity and amplitude of lateral head displacement by the agent were observed at 120 min after the start of incubation. Conversely, linearity was reduced by pentoxifylline. Beat-cross frequency did not show any significant change by the agent at any time point. Sperm swelling was not influenced by pentoxifylline throughout the experiment. It would appear that pentoxifylline stimulates sperm motion in vibo with no change ofthe sperm membrane.

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Influence of pentoxifylline in severe male factor infertility

Cited by 203 publications

References 20 publications

Supplementation of biotin to sperm preparation medium increases the motility and longevity in cryopreserved human spermatozoa

Supplementation of biotin to sperm preparation medium increases the motility and longevity in cryopreserved human spermatozoa

FSCB, a Novel Protein Kinase A-phosphorylated Calcium-binding Protein, Is a CABYR-binding Partner Involved in Late Steps of Fibrous Sheath Biogenesis

Effect of Pentoxifylline on Sperm Motion

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