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College of Veterinary Medicine, Yangzhou University, Yangzhou, People’s Republic of China
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stimulate the proliferation of porcine Leydig cells. Pigs play not only an important role in animal husbandry but are also one of the most commonly used animals experimental studies, especially as an application-appropriate model for studies related to
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–epididymal compartment as the predominant source of SE in boars. In vitro experiments using purified Leydig cells suggested that they are the main producers of SE in the adult porcine testis ( Raeside & Renaud 1983 ). However, in our previous study, estrogen
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porcine testis is widely unclear, and it is still elusive why the porcine testis inactivates bioactive steroids (estrogens, steroidal pheromones) immediately after their production in Leydig cells and why it removes important intermediates of
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ABSTRACT
The LH/hCG receptor is a G protein-coupled receptor with an N-terminal extracellular domain involved in hormone—receptor interaction. The recombinant porcine receptor, stably expressed in Chinese hamster ovary (CHO) cells, has the same characteristics (K d and cAMP production) as in Leydig cells. Six synthetic peptides derived from the receptor ectodomain and two polyclonal anti-peptide sera were tested in the homologous system porcine LH and porcine LH receptor. Their ability to inhibit hormone binding and signal transduction on CHO cells expressing the recombinant receptor was evaluated. Peptides 25–40 and 107–121 exhibited a high transduction inhibition as compared with hormone binding, peptides 21–36, 102–111, and 102–121 inhibited hormone binding more efficiently than signal transduction, and peptide 7–24 exhibited inhibition of both hormone binding and hormone-induced cAMP production. Immuno-globulins against peptides 21–36 and 102–111 inhibited both hormone binding and receptor activation suggesting that these sequences are located on the receptor surface.
The data suggest that multiple, discontinuous regions of the extracellular domain of porcine LH receptor are involved in hormone binding and signal transduction. Two minimum critical sequences, 21–24 and 102–107, are involved in hormone binding and vicinal segments may be implicated in signal transduction.
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ABSTRACT
The testicular feminized (Tfm) mouse lacks functional androgen receptors and develops with a female external phenotype and internal testes. The testes of these animals contain normal, or close to normal, numbers of Leydig cells but secrete very low amounts of androgen due to a lack of 17α-hydroxylase activity. To determine whether this loss of activity is due to a lack of enzyme synthesis or a change in catalytic activity we have examined 17α-hydroxylase cytochrome P-450 (P-45017α) protein and mRNA levels in the testes of Tfm mice.
Levels of P-45017α protein were measured by immunoblotting, while mRNA was measured following reverse transcription (RT) and amplification by the polymerase chain reaction (PCR). Conditions for RT-PCR were determined which allowed semiquantification of P-45017α mRNA relative to β-actin mRNA. In extracts of Tfm testes P-45017α protein was undetectable using antiserum against porcine P-45017α. In contrast, a protein of around 54 kDa was clearly detectable in extracts of control cryptorchid testes. Using RT-PCR, P-45017α mRNA was detectable in both control and [ill] testes but, expressed in terms of β-actin mRNA, levels of P-45017α mRNA in control testes were 40-fold higher than those in [ill] testes. If the total amount of RNA extracted from each testis is taken into account then P-45017α mRNA levels per testis were up to 400-fold higher in control testes. These results show that the reduced level of 17α-hydroxylase activity in [ill] testes is related to reduced protein synthesis. Previous results have shown that androgens reduce P-45017α mRNA levels in cultured Leydig cells. Results from this study suggest, however, that androgens are required to induce normal levels of P-45017α mRNA in Leydig cells.
Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA
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Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA
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Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA
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Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA
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Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA
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Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA
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Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA
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RI being responsible for signal transduction ( Dinarello et al. 1989 ). Both of these receptors are expressed by the Leydig cells, Sertoli cells and macrophages in the testis ( Petersen et al. 2002 , Svechnikov et al. 2003 ). Recently
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Reproduction, Department of Obstetrics, Mother and Child Health, Centre de Recherche du Centre Hospitalier Universitaire de Québec, CHUL Room T3-67, 2705 Laurier Boulevard, Québec, City, Québec, Canada G1V 4G2
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Structural organization of the porcine and human genes coding for a Leydig cell-specific insulin-like peptide (LEY I-L) and chromosomal localization of the human gene (INSL3) . Genomics 20 13 – 19 . ( doi:10.1006/geno.1994.1121 ). Cederroth CR Schaad
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Centre for Research in Reproduction, Development and Intergenerational Health, Department of Obstetrics, Gynecology, and Reproduction, Faculty of Medicine, Université Laval, Québec City, Québec, Canada
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, Pusch et al. 1996 ). During development, INSL3 is expressed in a sexually dimorphic pattern and produced almost exclusively by Leydig cells. During foetal life, INSL3 was found to be a critical regulator of testicular descent. Insl3- deficient mice
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Introduction The desensitization of lutropin (LH)/chorionic gonadotropin (CG)-induced responses has been studied in some detail in rodent granulosa and Leydig cells. Some of the hormone-induced effects that contribute to this
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activity in porcine Leydig cells. Primary porcine Leydig cells were isolated from mature Yorkshire boars and the SULT2A1 activity was determined. Leydig cells were cultured in the presence of CITCO (1 μM), TCPOBOP (250 nM), phenobarbital (2 mM), phenytoin
