Abundance of ADAM-8, -9, -10, -12, -15 and -17 and ADAMTS-1 in mouse uterus during the oestrous cycle
Jiyoung Kim A , Haekwon Kim A , Seung-Jae Lee B , Young Min Choi C F , Su-Jae Lee D and Joon Yeong Lee EA Department of Biotechnology, Seoul Women’s University, 126 Gongreung-dong, Nowon-gu, Seoul 139-774, Korea.
B Mirae and Heemang Obstetrics and Gynecology Clinic, 523-7 Sinsa-dong, Gangnam-gu, Seoul 135-120, Korea.
C Department of Obstetrics and Gynecology, Institute of Reproductive Medicine and Population, Medical Research Center, Seoul National University College of Medicine, 28 Yongon-dong, Chongno-gu, Seoul 110-744, Korea.
D Laboratory of Radiation Effect, Institute of Radiological and Medical Sciences, Korea Atomic Energy Research Institute, 215-4 Gongreung-dong, Nowon-gu, Seoul 139-706, Korea.
E Department of Life Science, Chungbuk National University, 12 Gaesshin-dong, Cheongju 361-763, Korea.
F Corresponding author. Email: ymchoi@snu.ac.kr
Reproduction, Fertility and Development 17(5) 543-555 https://doi.org/10.1071/RD04110
Submitted: 5 October 2004 Accepted: 31 March 2005 Published: 19 May 2005
Abstract
The aim of the present study was to determine whether a disintegrin and metalloproteinase (ADAM)-8, -9, -10, -12, -15 and -17 and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)-1 are involved in the remodelling process of the mouse uterus during the oestrous cycle. The mRNA expression of ADAM was observed in all uterine tissues throughout the entire cycle. The levels of ADAM-8 mRNA were maximal at pro-oestrus, whereas the expression of ADAM-9 and ADAMTS-1 mRNA was maximal at oestrus. The minimum mRNA level of all ADAM genes always occurred at dioestrus. The mRNA levels of ADAM-10, -12, -15 and -17 did not vary significantly, regardless of the stage of the oestrous cycle. Immunoblot analyses demonstrated the presence of all ADAM proteins throughout the cycle. In terms of protein intensities, ADAM-8, -12 and -17 were maximal at pro-oestrus, whereas ADAM-10 and ADAMTS-1 were maximal at metoestrus and ADAM-9 was maximal at oestrus. Regardless of the ADAM species, minimal protein expression always occurred at dioestrus. Immunohistochemical studies showed ADAM protein expression in luminal and glandular epithelial layers, but not in the stromal layer. Moreover, ADAM proteins were found to be heterogeneously localised and their individual localisations depended on the stage of the oestrous cycle. From these observations, we suggest that the ADAM genes play an important role in mouse uterine tissue remodelling during the oestrous cycle.
Acknowledgment
This study was supported by a grant of the Korean Health 21 R&D Project, Ministry of Health and Welfare, Republic of Korea (01-PJ10-PG6–01GN13–0002).
Asakura, M. , Kitakaze, M. , Takashima, S. , Liao, Y. , and Ishikura, F. , et al. (2002). Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat. Med. 8, 35–40.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Sahin, U. , Weskamp, G. , Kelly, K. , Zhou, H. M. , Higashiyama, S. , Peschon, J. , Hartmann, D. , Saftig, P. , and Blobel, C. P. (2004). Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J. Cell Biol. 164, 769–779.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Sapir, A. , Assa-Kunik, E. , Tsruya, R. , Schejter, E. , and Shilo, B. Z. (2005). Unidirectional Notch signaling depends on continuous cleavage of Delta. Development 132, 123–132.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Scarff, K. L. , Ung, K. S. , Nandurkar, H. , Crack, P. J. , Bird, C. H. , and Bird, P. I. (2004). Targeted disruption of SPI3/Serpinb6 does not result in developmental or growth defects, leukocyte dysfunction, or susceptibility to stroke. Mol. Cell. Biol. 24, 4075–4082.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Schlomann, U. , Rathke-Hartlieb, S. , Yamamoto, S. , Jockusch, H. , and Bartsch, J. W. (2000). Tumor necrosis factor alpha induces a metalloprotease-disintegrin, ADAM8 (CD 156): implications for neuron–glia interactions during neurodegeneration. J. Neurosci. 20, 7964–7971.
| PubMed |
Schlomann, U. , Wildeboer, D. , Webster, A. , Antropova, O. , and Zeuschner, D. , et al. (2002). The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. J. Biol. Chem. 277, 48 210–48 219.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Seals, D. F. , and Courtneidge, S. A. (2003). The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17, 7–30.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Shi, Z. , Xu, W. , Loechel, F. , Wewer, U. M. , and Murphy, L. J. (2000). ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3. J. Biol. Chem. 275, 18 574–18 580.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Shi, W. , Chen, H. , Sun, J. , Buckley, S. , Zhao, J. , Anderson, K. D. , Williams, R. G. , and Warburton, D. (2003). TACE is required for fetal murine cardiac development and modeling. Dev. Biol. 261, 371–380.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Shindo, T. , Kurihara, H. , Kuno, K. , Yokoyama, H. , and Wada, T. , et al. (2000). ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function. J. Clin. Invest. 105, 1345–1352.
| PubMed |
Six, E. , Ndiaye, D. , Laabi, Y. , Brou, C. , Gupta-Rossi, N. , Israel, A. , and Logeat, F. (2003). The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase. Proc. Natl Acad. Sci. USA 100, 7638–7643.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Srour, N. , Lebel, A. , McMahon, S. , Fournier, I. , Fugere, M. , Day, R. , and Dubois, C. M. (2003). TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity. FEBS Lett. 554, 275–283.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Surveyor, G. A. , Gendler, S. J. , Pemberton, L. , Das, S. K. , Chakraborty, I. , Julian, J. , Pimental, R. A. , Wegner, C. C. , Dey, S. K. , and Carson, D. D. (1995). Expression and steroid hormonal control of Muc-1 in the mouse uterus. Endocrinology 136, 3639–3647.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Takahashi, E. , Ino, M. , Miyamoto, N. , and Nagasu, T. (2004). Expression analysis of P/Q-type Ca2+ channel alpha 1A subunit mRNA in olfactory mitral cell in N-type Ca2+ channel alpha 1B subunit gene-deficient mice. Neurosci. Lett. 359, 37–40.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Thathiah, A. , Blobel, C. P. , and Carson, D. D. (2003). Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding. J. Biol. Chem. 278, 3386–3394.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Weskamp, G. , Kratzschmar, J. , Reid, M. S. , and Blobel, C. P. (1996). MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell Biol. 132, 717–726.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Weskamp, G. , Cai, H. , Brodie, T. A. , Higashyama, S. , Manova, K. , Ludwig, T. , and Blobel, C. P. (2002). Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol. Cell. Biol. 22, 1537–1544.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
White, J. M. (2003). ADAMs: modulators of cell–cell and cell–matrix interactions. Curr. Opin. Cell Biol. 15, 598–606.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Wilson, C. L. , Heppner, K. J. , Labosky, P. A. , Hogan, B. L. , and Matrisian, L. M. (1997). Intestinal tumorigenesis is suppressed in mice lacking the metalloproteinase matrilysin. Proc. Natl Acad. Sci. USA 94, 1402–1407.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Zhao, J. , Chen, H. , Peschon, J. J. , Shi, W. , Zhang, Y. , Frank, S. J. , and Warburton, D. (2001). Pulmonary hypoplasia in mice lacking tumor necrosis factor-alpha converting enzyme indicates an indispensable role for cell surface protein shedding during embryonic lung branching morphogenesis. Dev. Biol. 232, 204–218.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
Zhou, M. , Graham, R. , Russell, G. , and Croucher, P. I. (2001). MDC-9 (ADAM-9/Meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin. Biochem. Biophys. Res. Commun. 280, 574–580.
| Crossref | GoogleScholarGoogle Scholar | PubMed |
