Valproic acid changes the expression of tyrosine‐phosphorylated proteins in rat seminal vesicle

Abstract

Previous studies reported the effects of valproic acid (VPA) on tyrosine‐phosphorylated (TyrPho) protein expression in the testis and epididymis, but its effects on that in the seminal vesicle (SV) have never been demonstrated. This study attempted to investigate the expressions of TyrPho proteins in SV treated with VPA. Sixteen rats were divided into control and VPA‐treated groups. The control rats were injected with normal saline, whereas the treated animals were intraperitoneally injected with VPA (500 mg/kg BW) for 10 consecutive days (n = 8/each). The biochemical parameters in blood plasma and SV fluid were analysed. The SV tissues and fluid were investigated for the presence and expression of TyrPho proteins, androgen receptor (AR) proteins and heat shock protein 70 (Hsp70). Significantly, VPA caused SV atrophy and reductions in secretion and biochemical parameter levels. There were significant increases in many TyrPho proteins in the plasma (a 95 kDa) and SV tissue (a 40 kDa) of the VPA rats. However, the expressions of seminal AR, Hsp70 and TyrPho proteins (50 and 48 kDa) were significantly lower in VPA rats. Recent results have indicated that VPA affected SV morphology and decreased biochemical fluid substances including TyrPho proteins associated with decreased expressions of AR and Hsp70.

Effect of ethanol on the changes in testicular protein expression in adult male rats

“…Tyrosine phosphorylation is a post-translational process recently known to be associated with male fertility especially involved in sperm capacitation and acrosome reaction. Interestingly, many tyrosine-phosphorylated (TyrPho) proteins have been localised and identified in testis, epididymis and seminal vesicle of rats (Chaichun, Arun, Burawat, Kanla, & Iamsaard, 2017;Sawatpanich et al, 2018;Tongpan, Sukhorum, Arun, Sawatphanich, & Iamsaard, 2019). Indeed, the alteration of TyrPho proteins is associated with male infertile conditions such as animals induced with anti-cancer drugs (Burawat, Uabandit, Arun, Nualkaew, & Iamsaard, 2018;Chaichun et al, 2019;Iamsaard et al, 2014Iamsaard et al, , 2018Sukhorum & Iamsaard, 2017;Tongpan et al, 2019), type 1 and 2 diabetes (Sampannang, Arun, Burawat, Sukhorum, & Iamsaard, 2019;Yannasithinon & Iamsaard, 2019), and acute and chronic stresses (Arun, Burawat, Sukhorum, Sampannang, Maneenin, et al, 2016;Arun, Burawat, Sukhorum, Sampannang, Uabundit, et al, 2016).…”

Alterations of morphology and phosphorylated protein expression in the seminal vesicles of diabetic mice

“…Moreover, such proteins have been shown to be present in the epithelium of the epididymis and seminal vesicle(Tarinee et al, 2018;Tongpan, Sukhorum, Arun, Sawatphanich, & Iamsaard, 2019). Moreover, such proteins have been shown to be present in the epithelium of the epididymis and seminal vesicle(Tarinee et al, 2018;Tongpan, Sukhorum, Arun, Sawatphanich, & Iamsaard, 2019).…”

Localization (and profiles) of tyrosinephosphorylated proteins in female reproductive organs of adult rats

“…Tyrosine phosphorylation is known to play important roles in the internal fertilization processes of mammals, especially in capacitation and the acrosome reaction. Additionally, TyrPho proteins have been shown to be localized in the testis [9][10][11][12][13][14][15], epididymis [7], and seminal vesicle [8] by using anti-TyrPho antibodies (clone 4G10; catalog no. 05-321; MilliporeSigma).…”

“…Tyrosine phosphorylation is a post-transcriptional process that is essential to the regulation of cell proliferation, division, growth, and differentiation [1][2][3][4]. In the male reproductive system, tyrosine-phosphorylated (TyrPho) proteins have been found to be localized in the Sertoli cells [5,6], spermatogonia, spermatocytes, and Leydig cells, as well as the spermatids of rat testes [6], the epididymis epithelium [7], and the seminal epithelium and fluid [8]. Previous reports have demonstrated that the patterns of expression of testicular TyrPho proteins can be altered by drugs or other chemical agents [9][10][11][12][13][14][15].…”

“…Previous reports have demonstrated that the patterns of expression of testicular TyrPho proteins can be altered by drugs or other chemical agents [9][10][11][12][13][14][15]. Recently, Tongpan et al [8] showed that TyrPho proteins were localized in the seminal epithelium and present in the seminal fluid and blood plasma. Moreover, it was recently demonstrated that the expression of a TyrPho protein was altered in the seminal vesicles of diabetic mice [16].…”