Expression of inhibin alpha-subunit in horse testis. 1998

S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
Department of Veterinary Anatomy, Obihiro University of Agriculture and Veterinary Medicine, Japan.

Inhibin is believed to play roles in the pituitary secretion of FSH and in the paracrine regulation of testicular function. Although it has been generally accepted that inhibin is produced in Sertoli cells, there was a recent evidence for the localization of inhibin in Leydig cells of primates, rat and sheep. However, there is no report on the expression of inhibin in the adult horse testis. Therefore, using immunohistochemistry, western blotting and in situ hybridization techniques, the present study examined inhibin alpha-subunit (Ih-alpha) expression in the adult horse testis. For the detection of Ih-alpha protein, we used anti-porcine Ih-alpha antibody in immunohistochemistry and western blotting. Furthermore, digoxigenin-labeled complementary RNA probes were prepared to detect intracellular messenger RNA (mRNA) of Ih-alpha. Immunostainings for Ih-alpha were found not only in Leydig cells but also in Sertoli cells. The intensity in Leydig cells was stronger than in Sertoli cells. Immunoreactivities for Ih-alpha were found at approximately 46 kDa, 56 kDa and 90 kDa in the homogenates from testicular interstitial tissues. The bands at 56 kDa and 90 kDa agree with previous report, but not at 46 kDa. Signals for mRNA of Ih-alpha by in situ hybridization were detected in Leydig cells and in the basal region of seminiferous epithelium including Sertoli cells. These results suggest that Ih-alpha is expressed in Leydig cells and Sertoli cells of horse testis, and the expression level should be higher in Leydig cells than Sertoli cells.

UI MeSH Term Description Entries
D007150 Immunohistochemistry Histochemical localization of immunoreactive substances using labeled antibodies as reagents. Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D007265 Inhibins Glycoproteins that inhibit pituitary FOLLICLE STIMULATING HORMONE secretion. Inhibins are secreted by the Sertoli cells of the testes, the granulosa cells of the ovarian follicles, the placenta, and other tissues. Inhibins and ACTIVINS are modulators of FOLLICLE STIMULATING HORMONE secretions; both groups belong to the TGF-beta superfamily, as the TRANSFORMING GROWTH FACTOR BETA. Inhibins consist of a disulfide-linked heterodimer with a unique alpha linked to either a beta A or a beta B subunit to form inhibin A or inhibin B, respectively Female Inhibin,Inhibin,Inhibin-F,Inhibins, Female,Inhibins, Testicular,Ovarian Inhibin,Testicular Inhibin,Female Inhibins,Inhibin F,Inhibin, Female,Inhibin, Ovarian,Inhibin, Testicular,Testicular Inhibins
D008297 Male Males
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D004847 Epithelial Cells Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells. Adenomatous Epithelial Cells,Columnar Glandular Epithelial Cells,Cuboidal Glandular Epithelial Cells,Glandular Epithelial Cells,Squamous Cells,Squamous Epithelial Cells,Transitional Epithelial Cells,Adenomatous Epithelial Cell,Cell, Adenomatous Epithelial,Cell, Epithelial,Cell, Glandular Epithelial,Cell, Squamous,Cell, Squamous Epithelial,Cell, Transitional Epithelial,Cells, Adenomatous Epithelial,Cells, Epithelial,Cells, Glandular Epithelial,Cells, Squamous,Cells, Squamous Epithelial,Cells, Transitional Epithelial,Epithelial Cell,Epithelial Cell, Adenomatous,Epithelial Cell, Glandular,Epithelial Cell, Squamous,Epithelial Cell, Transitional,Epithelial Cells, Adenomatous,Epithelial Cells, Glandular,Epithelial Cells, Squamous,Epithelial Cells, Transitional,Glandular Epithelial Cell,Squamous Cell,Squamous Epithelial Cell,Transitional Epithelial Cell
D006736 Horses Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest. Equus caballus,Equus przewalskii,Horse, Domestic,Domestic Horse,Domestic Horses,Horse,Horses, Domestic
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D012621 Seasons Divisions of the year according to some regularly recurrent phenomena usually astronomical or climatic. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Seasonal Variation,Season,Seasonal Variations,Variation, Seasonal,Variations, Seasonal
D012671 Seminiferous Tubules The convoluted tubules in the TESTIS where sperm are produced (SPERMATOGENESIS) and conveyed to the RETE TESTIS. Spermatogenic tubules are composed of developing germ cells and the supporting SERTOLI CELLS. Seminiferous Tubule,Tubule, Seminiferous,Tubules, Seminiferous

Related Publications

S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
July 1990, Differentiation; research in biological diversity,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
February 2004, Molecules and cells,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
September 1989, Molecular and cellular endocrinology,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
June 2002, Reproduction (Cambridge, England),
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
August 1992, Cell and tissue research,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
April 2000, Archives of pathology & laboratory medicine,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
January 1995, Life sciences,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
February 2003, American journal of clinical pathology,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
September 2001, Applied immunohistochemistry & molecular morphology : AIMM,
S Fujimura, and E Hondo, and T Kobayashi, and K Yamanouchi, and N Inoue, and S Nagata, and G Watanabe, and K Taya, and N Kitamura, and J Yamada
April 1995, The Journal of endocrinology,
Copied contents to your clipboard!