A quantitative study of the effect of heat on germinal epithelium of rat testes

Chowdhury, A. K.; Steinberger, Emil

doi:10.1002/aja.1001150307

Cited by 161 publications

(84 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This study indicates that hsp70 can be induced during stages of spermatogenesis that are sensitive to elevations in temperature and suggests that hsp70 does not protect male germ cells from heat stress (9). These results support the hypothesis that heat shock proteins have a developmental role during spermatogenesis.…”

Section: Discussionsupporting

confidence: 76%

“…We have shown that a cell-specific hsp7o-like protein (P70) and products of the hsp70 gene family are abundant in mixed preparations of mouse spermatogenic cells and that hsp70 is induced in mixed germ cells following heat stress (1). However, the process of spermatogenesis is sensitive to even slight elevations of temperature and to many toxic agents (9,29). One possibility is that heat shock proteins have a developmental role during spermatogenesis and do not protect germ cells against adverse environmental effects.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Expression of heat shock proteins by isolated mouse spermatogenic cells.

et al. 1988

View full text Add to dashboard Cite

Proteins of the hsp70 family are abundant in mouse spermatogenic cells. These cells also synthesize relatively large amounts of a 70,000-molecular-weight protein (P70) that appears to be a cell-specific isoform of hsp70, the major heat-inducible protein (R. L. Allen, D. A. O'Brien, and E. M. Eddy, Mol. Cell. Biol. 8:828-832, 1988). In this study, proteins of unstressed and heat-stressed spermatogenic cells consisting of purified preparations of preleptotene, leptotene-zygotene, pachytene spermatocytes, and round spermatids were analyzed by two-dimensional polyacrylamide gel electrophoresis. Unstressed preleptotene and leptotenezygotene spermatocytes contained little P70, whereas relatively large amounts of P70 were present in pachytene spermatocytes and round spermatids. Labeling studies showed that P70 was synthesized primarily in pachytene spermatocytes and that little synthesis occurred in round spermatids or in preleptotene and leptotene-zygotene stages of spermatogenesis. Synthesis of hsp70 was not detectable in unstressed cells but was induced in all stages of isolated germ cells following heat stress. These results indicate that P70 is expressed in a stage-specific manner during cell differentiation, whereas hsp70 is synthesized in response to stress in all populations of isolated spermatogenic cells examined.

show abstract

Section: Discussionsupporting

confidence: 76%

mentioning

confidence: 99%

Expression of heat shock proteins by isolated mouse spermatogenic cells.

et al. 1988

View full text Add to dashboard Cite

show abstract

“…The testis in most mammals must be maintained a few degrees below ambient body temperature because of the low tolerance of certain stages of spermatogenesis to elevated temperature (6,37). The seminiferous epithelium is also a target for many toxic agents (25).…”

Section: Discussionmentioning

confidence: 99%

A novel hsp70-like protein (P70) is present in mouse spermatogenic cells.

1988

View full text Add to dashboard Cite

Mouse spermatogenic cells contain relatively large amounts of a 70-kilodalton protein (P70) that is closely related to hsp70, the major inducible heat shock protein. When hsp70 from spermatogenic cells is heat induced, it migrates to the same location as does P70 on two-dimensional polyacrylamide gels, indicating that it has an apparently identical mass and isoelectric point. P70 reacts strongly and specifically with an anti-Drosophila hsp70 monoclonal antibody that is specific for products of the hsp70 gene family. Both P70 and hsp70 are also ATP-binding proteins and are purified by using ATP-affinity chromatography. However, P70 and hsp70 are unique proteins on the basis of peptide map analysis and are regulated differently in germ cells. P70 appears to be a novel heat shock protein of spermatogenic cells which is synthesized in association with germ cell differentiation.Cells respond to elevated temperature by synthesizing a small number of heat shock proteins. The same proteins are synthesized in cells exposed to other stresses, such as heavy metal ions, anoxia, or toxic agents (8,23,34). This response is universal and has been observed in organisms as diverse as bacteria and humans (34). Although the specific functions of heat shock proteins are unclear, one role is to protect cells against the effects of adverse environmental conditions (22,31,32).A 70-kilodalton (kDa) protein is the most prominent and highly conserved heat shock protein (hsp70) in all organisms. In eucaryotic cells, the gene for hsp7O has been shown to be a member of a multigene family (9, 14). In the mouse, this multigene family includes genes for two heat shock cognate proteins of approximately 71 (hsc7l) and 74 kDa (hsc74) which are synthesized in unstressed cells (24,30). Members of this gene family are expressed developmentally during yeast cell sporulation and Drosophila oogenesis and in mouse embryos before implantation, which suggests that they may serve a role in cell differentiation as well as in the response to stress (2,3,11,19,41).Spermatogenic cells are sensitive to heat and to many toxic agents. In most mammals, germ cell development is affected adversely if the temperature of the testis is raised even to body temperature. In this study, we have examined heat shock proteins of mouse spermatogenic cells and detected the presence of a unique hsp70-like protein (P70) synthesized during germ cell differentiation. MATERIALS AND METHODSCell preparation and culture. Mixed germ cell suspensions were prepared from mature CD-1 mice by enzymatic dissociation of testes as previously described (28). Purified pachytene spermatocytes and round spermatids were isolated from mixed cell suspensions by unit gravity sedimentation (1, 33). Germ cells were collected for electrophoretic analysis by centrifugation, or 2 x 107 germ cells were cultured at 32°C with 5% CO2 in 60-mm petri dishes containing 5 ml of methionine-free minimal essential medium supplemented with 6 mM sodium L-lactate, 1 mM sodium pyruvate, 100 U * Corresponding author. of pe...

show abstract

“…In most mammalian species, the testis is kept approximately 4-5 C below body temperature. This lower temperature has been shown to be important for normal germ cell development and testicular function [2,3]. A slight increase in testicular temperature for a short period results in a rapid loss of mature germ cells [4,5], and the number of primary spermatocytes and spermatids drops rapidly [6].…”

mentioning

confidence: 99%

Effects of Experimental Cryptorchidism on Sperm Motility and Testicular Endocrinology in Adult Male Rats

Ren

Medan

Ozu

et al. 2006

Journal of Reproduction and Development

View full text Add to dashboard Cite

Abstract. The effect of induced cryptorchidism on testicular function and sperm motility was investigated. Bilateral cryptorchidism was created surgically in adult male rats (treated group), and sham-operated rats were used as a control group. Five rats from each group were sacrificed on days 1, 3, 5, and 7 after surgery. The percentage of motile spermatozoa began to decrease 1 day after the operation, followed by an abrupt decline 3 and 5 days later in cryptorchid rats. Furthermore, there were significant decreases in the other sperm motility parameters 5 days after inducement of cryptorchidism. In cryptorchid rats, plasma concentrations of LH, FSH, testosterone, and inhibin B were significantly lower than in the control group 1 day after the operation. Thereafter, plasma concentrations of LH, FSH, and testosterone gradually increased in the cryptorchid rats. On the other hand, plasma concentrations of inhibin B showed a further decline from day 3 after the operation onward. Concentrations of immunoreactive (ir)-inhibin, but not testosterone, in testicular interstitial fluid were remarkably increased until 3 days after surgery in the cryptorchid rats, and declined thereafter. Testicular response to human chorionic gonadotropin (hCG) for testosterone release was decreased in the cryptorchid rats compared with the control rats, indicating that heat stress to testes resulted in a reduction of the activity of Leydig cells and Sertoli cells. These results clearly indicate that heat stress to the testes resulted in a significant reduction of sperm activity within 3 days, and this was followed by changes in testicular endocrine function. Key words: Cryptorchidism, Heat stress, Inhibin B, Sperm motility, Testosterone (J. Reprod. Dev. 52: [219][220][221][222][223][224][225][226][227][228] 2006) ormal testicular descent is dependent on a series of complex endocrine and mechanical interactions [1]. In most mammalian species, the testis is kept approximately 4-5 C below body temperature. This lower temperature has been shown to be important for normal germ cell development and testicular function [2,3]. A slight increase in testicular temperature for a short period results in a rapid loss of mature germ cells [4,5], and the number of primary spermatocytes and spermatids drops rapidly [6]. In the field of animal production, summer sterility is a serious problem especially in male domestic animals, such as pigs, cattle, and stallions. In the rat, testicular damage caused by cryptorchidism is reversible, if the

show abstract

A quantitative study of the effect of heat on germinal epithelium of rat testes

Cited by 161 publications

References 6 publications

Expression of heat shock proteins by isolated mouse spermatogenic cells.

Expression of heat shock proteins by isolated mouse spermatogenic cells.

A novel hsp70-like protein (P70) is present in mouse spermatogenic cells.

Effects of Experimental Cryptorchidism on Sperm Motility and Testicular Endocrinology in Adult Male Rats

Contact Info

Product

Resources

About