Highly Specific Testicular Adenosine 3',5'*–Monophosphate Phosphodiesterase Associated with Sexual Maturation

Monn, E; Desautel, Marcia; Christiansen, Robert O.

doi:10.1210/endo-91-3-716

Cited by 60 publications

(14 citation statements)

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“…The testes from both immature (18 days) and adult (75 days) rats contained qualitatively the same soluble enzyme activities, although there were significant quantitative differences. Our results are in contradiction with those of Monn et al [7], who failed to detect the high affinity cAMP phosphodiesterase activity in the testes of immature rats of the same age. This observation led them to speculate that this enzyme represented a germ cell-specific form that appeared at the more advanced stages of spermatogenesis.…”

Section: Discussioncontrasting

confidence: 99%

“…However, this group has concentrated their efforts on the Sertoli cell enriched testis (obtained by prenatal irradiation) and not on the normal rat testis. There was detected in rat testes a high affinity CAMP-phosphodiesterase whose activity paralleled the appearance of the mature germ cells [7]. This enzyme was not found in immature animals (20 days).…”

Section: Introductionmentioning

confidence: 86%

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Testicular Cyclic Nucleotide Phosphodiesterase in the Rat. Kinetic Properties and Changes with Age

Purvis

Olsen

Barry

et al. 1981

Archives of Andrology

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The assay for cyclic nucleotide phosphodiesterase has been applied, with certain modifications, to the measurement of the soluble forms of these enzymes in the rat testis. The homogenization and incubation conditions were adjusted to achieve linear product formation as a function of time and protein concentrations and the resulting products were isolated by ion exchange chromatography using 5 mM HCl as the eluting agent. Phosphodiesterase activities were present in the testicular cytosol(lO5,OOO g supernatant) of adult rats which were capable of hydrolyzing cAMP with a high ( K , 2 pM) and low ( K , 20 pM) affinity and GMP with a relatively high affinity ( K , 3 pM). The low affinity cAMP enzyme activity could be stimulated with divalent ions such as calcium, magnesium, and manganese. At 18 days of age, all three enzyme activities were present in the testis, although both the high and low affinity cAMP phosphodiesterase displayed maximal rates (Vmax) that were only one third of the adult testis (when expressed per mg protein).

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Section: Discussioncontrasting

confidence: 99%

Section: Introductionmentioning

confidence: 86%

Testicular Cyclic Nucleotide Phosphodiesterase in the Rat. Kinetic Properties and Changes with Age

Purvis

Olsen

Barry

et al. 1981

Archives of Andrology

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“…The highest enzyme specific activity is found in early spermatids in which the lowest cAMP levels are detectable. This enzyme activity probably corresponds to the enzyme activity described in developing rat testis (Monn, Desautel & Christiansen, 1972) and in mature spermatozoa (Tash, 1976). Even though it is not possible to speculate on the role of these enzyme activities in spermatogenesis, the finding that these phosphodiesterase forms are present in different species is of interest.…”

Section: Phosphodiesterase Forms In Epididymal Spermatozoasupporting

confidence: 62%

Cyclic nucleotide phosphodiesterases in somatic and germ cells of mouse seminiferous tubules

Rossi¹,

Pezzotti²,

Conti³

et al. 1985

Reproduction

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Summary. The distribution of phosphodiesterase forms in somatic and germ cells, and their variations during testicular development and germ cell differentiation have been investigated. Seminiferous tubules from immature mice and Sertoli cells in culture possessed two enzyme activities which were comparable to forms described for different tissues and species: (a) a calcium\p=n-\calmodulin-dependentenzyme with high affinity for guanosine 3',5'-(cyclic)-monophosphate (cGMP), and (b) a calcium\p=n-\ calmodulin-independent enzyme with high affinity for adenosine 3' ,5' -(cyclic)\x=req-\ monophosphate (cAMP) the activity of which increased in cultured Sertoli cells after treatment with FSH or dibutyryl cAMP. Seminiferous tubules from adult animals and germ cells at the meiotic and post-meiotic stage of differentiation possessed two enzyme forms that could be distinguished from those present in somatic cells of the seminiferous tubules: (a) a calcium\p=n-\calmodulin-dependent form with high affinity for both cAMP and cGMP, similar to forms described in other tissues from different species, and (b) a calcium\p=n-\calmodulin-independentphosphodiesterase with high affinity for cAMP and present only in post-meiotic cells, previously identified also in germ cells of the rat.

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“…However, cultured mouse Sertoli cells have been shown to produce IL-1ra under basal conditions, and endogenous production of this cytokine in the cultures might obscure small responses to exogenous IL-1ra (Zeyse et al 2000). It also should be noted that adult Sertoli cells are less responsive to FSH stimulation than immature Sertoli cells (Monn et al 1972, Steinberger et al 1978, Lampa et al 1999. In both immature and adult Sertoli cells, however, dbcAMP and FSH mostly inhibited the action of IL-1 on activin A secretion.…”

Section: Discussionmentioning

confidence: 99%

Regulation of activin A and inhibin B secretion by inflammatory mediators in adult rat Sertoli cell cultures

Okuma¹,

O’Connor²,

Muir³

et al. 2005

Journal of Endocrinology

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The regulation of Sertoli cell activin A and inhibin B secretion during inflammation was investigated in vitro. Adult rat Sertoli cells were incubated with the inflammatory mediators, lipopolysaccharide (LPS), interleukin-1 (IL-1 ), IL-6 and the IL-1 receptor antagonist (IL-1ra) over 48 h in culture. Activin A, inhibin B and IL-1 were measured in the culture medium by specific two-site ELISAs. Both IL-1 -and LPS-stimulated activin A and inhibited inhibin B secretion. LPS also stimulated the production of IL-1 in the cultures. In contrast to IL-1 , IL-6 had no effect on activin A, although it did have a significant inhibitory effect on inhibin B secretion. Ovine follicle-stimulating hormone (FSH) and the cAMP analogue dibutyryl cAMP opposed the actions of IL-1 and LPS by suppressing activin A and IL-1 secretion and by stimulating inhibin B. Blocking IL-1 activity in the cultures by addition of an excess of IL-1ra completely prevented the response of activin A to exogenous IL-1 , and reduced the response to LPS by 50%. In the presence of IL-1ra, basal secretion of inhibin B was increased, but IL-1ra was unable to reverse the suppression of inhibin B by LPS. These data indicate the importance of both IL-1 isoforms in regulating secretion of activin A and inhibin B by mature Sertoli cells during inflammation. The data also establish that inflammation exerts its effects on activin A and inhibin B secretion via other pathways in addition to those mediated by IL-1, and that hormonal stimulation by FSH and cAMP moderates the Sertoli cell response to inflammation. Interference with the complex interactions between these cytokines and hormones may contribute to the disruption of reproductive function that can accompany infection and illness in men.

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Highly Specific Testicular Adenosine 3',5'*–Monophosphate Phosphodiesterase Associated with Sexual Maturation

Cited by 60 publications

References 0 publications

Testicular Cyclic Nucleotide Phosphodiesterase in the Rat. Kinetic Properties and Changes with Age

Testicular Cyclic Nucleotide Phosphodiesterase in the Rat. Kinetic Properties and Changes with Age

Cyclic nucleotide phosphodiesterases in somatic and germ cells of mouse seminiferous tubules

Regulation of activin A and inhibin B secretion by inflammatory mediators in adult rat Sertoli cell cultures

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