Paracrine Regulation of Matrix Metalloproteinase Expression in the Normal Human Endometrium

Osteen, Kevin G.; Keller, Nancy R.; Feltus, F. Alex; Melner, Michael H.

doi:10.1159/000052863

Cited by 92 publications

(66 citation statements)

References 40 publications

(65 reference statements)

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“…Matrix metalloproteinases are important enzymes within the stroma that play a major role in the degradation of most components of the extracellular matrix during the menstrual phase (Osteen et al 1999). The pattern of expression of endometrial metalloproteinases during the menstrual cycle in macaques is similar to that reported for women.…”

Section: Noncellular Componentsmentioning

confidence: 55%

The Macaque Endometrium, with Special Reference to the Cynomolgus Monkey (Macaca fascicularis)

Esch¹,

Cline²,

Buse³

et al. 2008

Toxicol Pathol

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The macaque endometrium undergoes dramatic morphologic and functional changes during the menstrual cycle that are nearly identical to those of the human endometrium. The sequential events that take place in the endometrium are mainly driven by the ovarian steroids and their respective receptors. To be able to interpret the changes and effects induced by mammalian or synthetic hormones and other compounds that could have influence on the hormonal status of the animal, a thorough knowledge of the anatomy, physiology, and histology of the cyclic hormone-mediated processes within the endometrium is indispensable. In this paper we give an overview of uterine growth and development, anatomy, basic histology, aging, spontaneous pathology, and the techniques to study the endometrium in-life. In addtion, a comprehensive description of the receptor-mediated, hormonedriven morphological changes during the menstrual cycle in the cynomolgus monkey (Macaca fascicularis) is given. Where possible, differences between the macaque and human endometria are discussed.Keywords: female reproduction; endometrium; histology; menstrual cycle; hormone receptors; endometrial dating; cynomolgus monkey.human. For this reason, monkey species belonging to this group are preferred as experimental models in studies of human reproduction, pharmacology, and toxicology. Especially for studies with sex hormones, synthetic steroidal compounds or compounds that interfere with the hypothalamus-pituitary-ovarian (or testicular) axis, such monkey species are predictive . The rhesus monkey (Macaca mulatta) and the cynomolgus monkey (Macaca fascicularis) are the species most often used for these purposes. In our laboratories, purpose-bred cynomolgus monkeys are used for such studies. Besides their resemblance in menstrual cycle physiology, these monkeys are relatively small and easy to handle.Both the human and the macaque monkey endometria undergo dramatic morphologic and functional changes during the menstrual cycle. The sequential events that take place in the endometrium are mainly driven by the ovarian steroids estradiol and progesterone and their respective receptors.To be able to interpret the changes and effects induced by mammalian or synthetic hormones and other compounds that could have influence on the hormonal status of the animal, or that interfere with the regulatory processes within the endometrium, a thorough knowledge of the anatomy, physiology, and histology of cyclic hormone-mediated processes within the endometrium is indispensable.In this paper we give a brief overview of endometrial growth and development, anatomy, basic histology, and the effects of aging, and we briefly discuss the spontaneous pathology of the endometrium of macaques. The receptor-mediated,

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Section: Noncellular Componentsmentioning

confidence: 55%

The Macaque Endometrium, with Special Reference to the Cynomolgus Monkey (Macaca fascicularis)

Esch¹,

Cline²,

Buse³

et al. 2008

Toxicol Pathol

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“…IL-1-induced expression and release of MMPs is a crucial factor in the pathogenesis of rheumatoid arthritis (41), periodontal diseases (42), postmyocardial infarction remodeling (43), and in the remodeling of normal human endometrium (44). Furthermore, PTP␣ is important in cellular transformation (45).…”

Section: Discussionmentioning

confidence: 99%

Importance of Protein-tyrosine Phosphatase-α Catalytic Domains for Interactions with SHP-2 and Interleukin-1-induced Matrix Metalloproteinase-3 Expression

Wang

Rajshankar

Laschinger

et al. 2010

Journal of Biological Chemistry

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Interleukin-1 (IL-1) induces extracellular matrix degradation as a result of increased expression of matrix metalloproteinases (MMPs).Reversible phosphorylation of proteins on tyrosine residues is a pivotal, post-translational modification in many signal transduction pathways. The extent of these modifications is determined by the balance between the activities of proteintyrosine kinases and phosphatases (1, 2). Whereas proteintyrosine kinases are thought to regulate the amplitude of responses to extracellular signals, protein-tyrosine phosphatases (PTPs) 2 may determine the rate and duration of these responses (3). For IL-1 signaling in adherent cells, tyrosine phosphorylation of focal adhesion proteins such as the focal adhesion kinase is a critical, rate-limiting process (4). Tyrosine phosphorylated proteins, such as focal adhesion kinase, paxillin, and Src family kinases, which are enriched in focal adhesions (5), influence the assembly, maturation, and disassembly of these adhesive structures (6 -9) and also impact signaling through focal adhesions (10). The dynamic and reversible nature of tyrosine phosphorylation of focal adhesion proteins suggests an important role for protein-tyrosine kinases and PTPs in focal adhesion-dependent signaling (11). There are numerous PTPs in focal adhesions, and, in particular, SHP-2 is recruited to focal adhesions upon integrin engagement (12-14). In the absence of SHP-2, the number of focal adhesions and actin stress fibers increases, which is associated with diminished spreading and motility (15, 16). Expression of a dominant-negative SHP-2 enhances the formation of focal adhesions and stress fibers (17). The dynamics of focal adhesion assembly and IL-1-induced signaling pathways, including Ca 2ϩ release and ERK phosphorylation, are dependent on phosphorylation of Tyr 542 of 18,19), which can in turn affect the phosphatase activity of SHP-2 (20).We recently reported that another PTP, namely PTP␣, plays a prominent role in the regulation of focal adhesions during cell adhesion, spreading, and motility (21). PTP␣ is a receptor-like PTP that can activate Src family kinases (e.g. Src and Fyn) via dephosphorylation of an inhibitory C-terminal tyrosine residue (22)(23)(24)(25)(26)(27). We have also shown that through its interactions with Src, PTP␣ controls IL-1 induced phosphorylation of the inositol 1,4,5-phosphate receptor and consequently, Ca 2ϩ release (28). Further, PTP␣ regulates formation of focal adhesions in response to mechanical force, strengthens connections between integrins and the cytoskeleton, and modulates cytoskeletal reorganization in response to integrin ligation (26,27). In the absence of PTP␣, fibroblasts demonstrated reduced spreading, increased numbers of abnormal focal adhesions, decreased tyrosine phosphorylation of focal * This work was supported by grants from the Canadian Institutes of Health Research (MOP 84254; to C. A. M. and G. P. D.). This work was also supported in part by National Institutes of Health Grant HL090669 (to G. P. D.) and funds ...

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“…In the endometrium, the control of MMP and TIMP production by ovarian steroids is locally mediated, at least partially, by cytokines secreted by the epithelial, stromal, inflammatory and endothelial cells of the endometrium [8][9][10][11][12][13]. IL-1 is produced by inflammatory cells, trophoblast and epithelial cells, and increases MMP-1, 3 and 9 production, while it inhibits TIMP-1 and 3 expression [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Human Endometrial Epithelial Cells Modulate the Activation of Gelatinase A by Stromal Cells

Goffin

Frankenne²,

Béliard³

et al. 2002

Gynecol Obstet Invest

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Metalloproteinases (MMPs) are central effectors in endometrial physiology. Their production is tightly regulated by ovarian steroids and cytokines. Using zymography, we investigated MMP-2 production by human endometrial cells treated with estradiol-17β + progesterone (E₂+P) and by various key cytokines in endometrial physiology (IL-1β, LIF, TGF-β, and TNF-α). No gelatinase activity was detected in the culture media of epithelial cells. In basal conditions, stromal cells produced the pro form of MMP-2. MMP-2 production/activation was not directly affected by cytokine treatment. Interestingly, activated MMP-2 was only detected after treatment of stromal cells with culture medium from epithelial cells. Cytokine treatment of epithelial cells increased the capacity of conditioned medium to stimulate stromal cells to activate MMP-2. As the tissue inhibitor of MMP-2 (TIMP-2) is a regulator of gelatinase A activity, its concentration was measured by ELISA. TIMP-2 production by stromal cells was not affected by cytokines or by epithelial cell-conditioned medium. These results strongly suggest that regulation of stromal MMP-2 activation involves soluble factor(s) derived from the epithelial compartment.

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Paracrine Regulation of Matrix Metalloproteinase Expression in the Normal Human Endometrium

Cited by 92 publications

References 40 publications

The Macaque Endometrium, with Special Reference to the Cynomolgus Monkey (Macaca fascicularis)

The Macaque Endometrium, with Special Reference to the Cynomolgus Monkey (Macaca fascicularis)

Importance of Protein-tyrosine Phosphatase-α Catalytic Domains for Interactions with SHP-2 and Interleukin-1-induced Matrix Metalloproteinase-3 Expression

Human Endometrial Epithelial Cells Modulate the Activation of Gelatinase A by Stromal Cells

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