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Endocrinology, Vol 128, 2805-2814, Copyright © 1991 by Endocrine Society
ARTICLES |
MS Stahler, P Schlegel, CW Bardin, B Silvestrini and CY Cheng
Population Council, New York, New York 10021.
Earlier studies from this laboratory have shown that Sertoli cells actively synthesize and secrete a nonspecific protease inhibitor in vitro; N-terminal sequence analysis, subunit structural analysis, and other biological studies revealed that this protein is the homolog of serum alpha 2-macroglobulin. We have now quantified the relative distribution of alpha 2-macroglobulin in the reproductive compartments and their comparison with nonreproductive organs. In serum and all nonreproductive tissues examined, the concentration of alpha 2- macroglobulin progressively decreased with advancing age. However, in both the testis and epididymis, the levels of this protein increased with the age of the animals. Serum alpha 2-macroglobulin levels were consistently higher than those in any other tissues until 60 days when the concentrations of this protein were the highest in the epididymis. The distribution of alpha 2-macroglobulin in various nonreproductive tissues from female rats was similar to that observed for male rats in that its levels tended to decrease with age. However, uterine levels of alpha 2-macroglobulin increased progressively with advancing age, whereas ovarian levels of alpha 2-macroglobulin remained relatively stable with an increase in animal age. As serum alpha 2-macroglobulin is an acute-phase protein in the rat, the response of this protein in the testis to induced inflammation was examined. The concentration of alpha 2-macroglobulin in serum rose about 150-fold after injection of fermented yeast. By contrast, the levels of this protein in rete testis fluid, which is derived exclusively from seminiferous fluid, did not change in response to inflammation. These results suggest that there might be distinctive mechanisms that regulate this protein in the systemic circulation vs. the microenvironment behind the blood-testis barrier in the seminiferous epithelium.
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W.-Y. Lui, Y. H. Cheng, D. D Mruk, C. H. Cheng, M. Y. Mo, W. M Lee, and C Y. Cheng {alpha}2-Macroglobulin expression in the liver in response to inflammation is mediated by the testis J. Endocrinol., June 1, 2005; 185(3): 497 - 505. [Abstract] [Full Text] [PDF] |
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C.-h. Wong, D. D. Mruk, M. K. Y. Siu, and C. Y. Cheng Blood-Testis Barrier Dynamics Are Regulated by {alpha}2-Macroglobulin via the c-Jun N-Terminal Protein Kinase Pathway Endocrinology, April 1, 2005; 146(4): 1893 - 1908. [Abstract] [Full Text] [PDF] |
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D. D. Mruk and C. Y. Cheng Sertoli-Sertoli and Sertoli-Germ Cell Interactions and Their Significance in Germ Cell Movement in the Seminiferous Epithelium during Spermatogenesis Endocr. Rev., October 1, 2004; 25(5): 747 - 806. [Abstract] [Full Text] [PDF] |
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C.-h. Wong, D. D. Mruk, W.-y. Lui, and C. Y. Cheng Regulation of blood-testis barrier dynamics: an in vivo study J. Cell Sci., February 15, 2004; 117(5): 783 - 798. [Abstract] [Full Text] [PDF] |
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D. D. Mruk, M. K.Y. Siu, A. M. Conway, N. P.Y. Lee, A. S.N. Lau, and C. Y. Cheng Role of Tissue Inhibitor of Metalloproteases-1 in Junction Dynamics in the Testis J Androl, July 1, 2003; 24(4): 510 - 523. [Abstract] [Full Text] [PDF] |
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C. Y. Cheng and D. D. Mruk Cell Junction Dynamics in the Testis: Sertoli-Germ Cell Interactions and Male Contraceptive Development Physiol Rev, October 1, 2002; 82(4): 825 - 874. [Abstract] [Full Text] [PDF] |
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N. P.Y. Chung, D. Mruk, M.-y. Mo, W. M. Lee, and C. Y. Cheng A 22-Amino Acid Synthetic Peptide Corresponding to the Second Extracellular Loop of Rat Occludin Perturbs the Blood-Testis Barrier and Disrupts Spermatogenesis Reversibly In Vivo Biol Reprod, November 1, 2001; 65(5): 1340 - 1351. [Abstract] [Full Text] [PDF] |
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D. D. Mruk and C. Y. Cheng Sertolin Is a Novel Gene Marker of Cell-Cell Interactions in the Rat Testis J. Biol. Chem., September 17, 1999; 274(38): 27056 - 27068. [Abstract] [Full Text] [PDF] |
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J. Grima, C. C. S. Wong, L.-j. Zhu, S.-d. Zong, and C. Y. Cheng Testin Secreted by Sertoli Cells Is Associated with the Cell Surface, and Its Expression Correlates with the Disruption of Sertoli-Germ Cell Junctions but Not the Inter-Sertoli Tight Junction J. Biol. Chem., August 14, 1998; 273(33): 21040 - 21053. [Abstract] [Full Text] [PDF] |
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L. Braghiroli, B. Silvestrini, C. Sorrentino, J. Grima, D. Mruk, and C. Yan Cheng Regulation of {alpha}2-Macroglobulin Expression in Rat Sertoli Cells and Hepatocytes by Germ Cells In Vitro Biol Reprod, July 1, 1998; 59(1): 111 - 123. [Abstract] [Full Text] |
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G. R. Aravindan, D. Mruk, W. M. Lee, and C. Y. Cheng Identification, Isolation, and Characterization of a 41-Kilodalton Protein from Rat Germ Cell-Conditioned Medium Exhibiting Concentration-Dependent Dual Biological Activities Endocrinology, August 1, 1997; 138(8): 3259 - 3268. [Abstract] [Full Text] [PDF] |
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