92-kD type IV collagenase mediates invasion of human cytotrophoblasts.

Librach, Clifford L.; Werb, Zena; Fitzgerald, Marilyn L.; Chiu, King; Corwin, Nanci M.; Esteves, Ruth A.; Grobelny, Damian; Galardy, Richard E.; Damsky, Caroline H.; Fisher, Susan J.

doi:10.1083/jcb.113.2.437

Cited by 699 publications

(441 citation statements)

References 64 publications

(71 reference statements)

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“…MMPs are involved in extracellular matrix turnover during many reproductive processes (8)(9)(10)(11)(12)(13)(14), as well as during normal nonreproductive functions (15)(16)(17). These potent enzymes also play an important role in the pathological process of tumor invasion and metastasis (18)(19)(20)(21)(22) …”

Section: Discussionmentioning

confidence: 99%

Stromal-epithelial interaction mediates steroidal regulation of metalloproteinase expression in human endometrium.

Osteen

Rodgers

Gaire

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

175

144

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The hallmark of the menstrual cycle is extensive steroid-dependent tissue turnover. Estrogen mediates endometrial cell growth and structural remodeling, whereas progeserone suppresses estrogen-dependent proliferation and promotes cellular differentiation. In nonfertile cycles, tissue degradation and menstruation occur as a consequence of steroidal deprivation as the ovarian corpus luteum fails. Stromalepithelial interactions are recognized as a necesary component in mediating steroid-induced endometrial turnover. Specific mRNAs for metalloproteinases of the stromelysin family are expressed during endometrial growth and menstrual breakdown but are absent in the progestin-dominated secretory phase. This expression pattern suggss involvement of stromelysins in remodeling the extracellular matrix of the endometrium during tissue growth and breakdown and implicates progesteronE in the suppression of these enzymes. We examined the regulation of endometrial stromelysins in explant cultures and found no acute effect ofestradiol on their expression, whereas progesterone was a potent inhibitor of stromelysin expression. Progesterone also suppressed stromelysin expression in cultures ofisolated stromal cells, but epithelial cells were progesterone insensitive. Coculture ofrecombined stromal and epithelial cells restored steroidal suppression of the epithelial-specific metalloproteinase. Our data confirm that progesterone inhibits endometrial stromelysins and further demonstrate the necessity for a stromalderived factor(s) as a mediator of steroid suppression of an epithelial metalloproteinase.The human endometrium undergoes extensive estradiolinduced growth and remodeling during the proliferative phase of the menstrual cycle, followed by secretory maturation in response to postovulatory progesterone (1). This rapid and extensive degree of steroid-mediated tissue development, which rivals that of many neoplasias, appears to be a necessary component of providing an environment suitable for sustaining hemochorial placentation (2). In the absence of implantation and the continued progestational environment of pregnancy, the superficial functionalis region of the endometrium undergoes degradation and is expelled with menstrual blood flow. Several laboratories have recently described the expression of matrix metalloproteinases (MMPs) in the normal, cycling human endometrium (3-6). These enzymes degrade many components of the extracellular matrix, including proteoglycans, glycoproteins, and basement membrane collagens (7). Our studies (5, 6) identified a cell type-specific expression pattern of mRNAs coding for members of the stromelysin family only during the proliferative and premenstrual/menstrual stage of the cycle; none of the enzymes were identified during the progesterone-dominated secretory menstrual interval. This pattern of expression suggests an active role for stromelysins during growth-associated structural remodeling as well as during the extensive tissue breakdown associated with menstruation.MMPs of the st...

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Section: Discussionmentioning

confidence: 99%

Stromal-epithelial interaction mediates steroidal regulation of metalloproteinase expression in human endometrium.

Osteen

Rodgers

Gaire

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

175

144

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“…The enzyme has been isolated and characterized from a number of different cell types [1][2][3]. Tt~e expression of MMP-9 is implicated to both physiological an.t pathological breakdown of the connective tissue during invasion of cytotrophoblasts [4], the detachment of epithelial cells from basement membrane in the wound healing process [5 chronic inflammation such as rheumatoid arthritis [6,7] and tumor cell invasion and metastasis [8].…”

Section: Introductionmentioning

confidence: 99%

Tumor necrosis factor α (TNFα) induces pro‐matrix metalloproteinase 9 production in human uterine cervical fibroblasts but interleukin 1 α antagonizes the inductive effect of TNFα

et al. 1996

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We have examined the regulation of precursor of matrix metalloproteinase 9 (proMMP-9)lprogelatinase B production by tumor necrosis factor et (TNFet) and interleukin let (H-let) using human uterine cervical fibroblasts. TNF~ but not IL-la, induces the production of proMMP-9 in the cervical cells. IL--let, however, suppresses the TNFet-ioduced proMMP-9 production. 12-O-tetradeeanoylphorbol 13-acetate (TPA) also stimulates the cervical cells to produce proMMP-9, and IL-let synergistically enhances its production. TNFet-induced proMMP-9 production is not mediated by protein kinase C (PKC), whereas the effect of IL-la is through PKC. By contrast, proMMP-31prostromelysin 1 is up-regulated by TNFet or TPA in the presence of IL-I~ whose modulation is PKC-dependent. The suppressive effect of IL-la on the TNFet-induced proMMP-9 production is a new biological effect of IL-1 on MMP production.

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“…16,17 When employing these cells to study trophoblast migration it is crucial to assess purity of cell isolates, as cytotrophoblast isolation procedures are prone to contamination with low levels of fibroblasts that are highly motile and multiply rapidly in culture. 18 A number of researchers have reported that first trimester cytotrophoblasts exhibit invasive activity (indicative of EVT differentiation) following culture on Matrigel, [19][20][21] but the resulting cell population is frequently not well characterized, and the proportion of differentiated EVT progeny obtained is unclear. In contrast, cytotrophoblasts isolated from term placentae appear to demonstrate a greater propensity to syncytialize in culture and do not differentiate into an invasive EVT phenotype.…”

Section: Isolated Primary Trophoblastsmentioning

confidence: 99%

Quantifying trophoblast migration: In vitro approaches to address in vivo situations

James

Tun

Clark

2016

Cell Adhesion & Migration

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When trophoblasts migrate and invade in vivo, they do so by interacting with a range of other cell types, extracellular matrix proteins, chemotactic factors and physical forces such as fluid shear stress. These factors combine to influence overall trophoblast migration and invasion into the decidua, which in turn determines the success of spiral artery remodeling, and pregnancy itself. Our understanding of these important but complex processes is limited by the simplified conditions in which we often study cell migration in vitro, and many discrepancies are observed between different in vitro models in the literature. On top of these experimental considerations, the migration of individual trophoblasts can vary widely. While time-lapse microscopy provides a wealth of information on trophoblast migration, manual tracking of individual cell migration is a time consuming task that ultimately restricts the numbers of cells quantified, and thus the ability to extract meaningful information from the data. However, the development of automated imaging algorithms is likely to aid our ability to accurately interpret trophoblast migration in vitro, and better allow us to relate these observations to in vivo scenarios. This commentary discusses the advantages and disadvantages of techniques commonly used to quantify trophoblast migration and invasion, both from a cell biology and a mathematical perspective, and examines how such techniques could be improved to help us relate trophoblast migration more accurately to in vivo function in the future.

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92-kD type IV collagenase mediates invasion of human cytotrophoblasts.

Cited by 699 publications

References 64 publications

Stromal-epithelial interaction mediates steroidal regulation of metalloproteinase expression in human endometrium.

Stromal-epithelial interaction mediates steroidal regulation of metalloproteinase expression in human endometrium.

Tumor necrosis factor α (TNFα) induces pro‐matrix metalloproteinase 9 production in human uterine cervical fibroblasts but interleukin 1 α antagonizes the inductive effect of TNFα

Quantifying trophoblast migration: In vitro approaches to address in vivo situations

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