Metalloproteinase inhibitors from bovine cartilage and body fluids

Bunning, R.A.D.; Murphy, Gillian; Kumar, Shant; Phillips, P. J.; Reynolds, John J.

doi:10.1111/j.1432-1033.1984.tb07978.x

Cited by 60 publications

(32 citation statements)

References 29 publications

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“…Another gene possibly involved in the development of synovial sarcoma is the erythroid-potentiating activity/tissue-inhibitor of metalloproteinase gene (EPA/TIMP gene), which also has been mapped to Xpl1.1-Xpll.4 (18). The tissue inhibitor of metalloproteinase (TIMP) is an inhibitor of collagenase and other tissue metalloproteinases and has been purified from pig synovium among other sources (19). The physiological properties and regulation of this gene are still poorly understood.…”

Section: Methodsmentioning

confidence: 99%

Involvement of chromosome X in primary cytogenetic change in human neoplasia: nonrandom translocation in synovial sarcoma.

Turc‐Carel¹,

Cin²,

Limon³

et al. 1987

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

198

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A translocation that involves chromosome X (band pll.2) and chromosome 18 (band qll.2) was observed in short-term in vitro cultures of cells from five synovial sarcomas and one malignant fibrous histiocytoma. In four of these tumors, the translocation t(X;18)(pll.2;qll.2) was reciprocal. The two other tumors had complex translocations: t(X;18;21)(pll.2;qll.2;p13) and t(X;15;18)(pll.2;q23;qll.2).A translocation between chromosomes X and 18 was not detected in other histological types of soft tissue sarcoma. The X;18 rearrangement appears to characterize the synovial sarcoma and is the first description of a primary, nonrandom change in the sex chromosome of a human solid tumor. (2) and certain subtypes of rhabdomyosarcoma (3, 4). Another soft tissue sarcoma, synovial sarcoma, has been analyzed extensively in the clinical and pathology literature, but its chromosome pattern has been described in only a single report (5).Synovial sarcoma, according to the experience of Enzinger and Weiss (6), is the fourth most common type of soft tissue sarcoma. The neoplasm usually develops in adolescents and young adults, is more common in males than females, and has no racial bias.A sex chromosome has not been shown to be involved in a consistent primary chromosomal change in any human neoplasm. In a study of the karyotype of soft tissue sarcomas in humans, we detected translocations affecting the X chromosome in four synovial sarcomas. The observation prompted a critical review of two soft tissue sarcomas (one poorly differentiated and one spindle cell) in which we had identified similar changes in the X chromosome (7). This report describes the findings of a more detailed histological and chromosomal analysis of these six tumors. MATERIALS AND METHODSClinical Histories and Pathology. Patient 1. In September 1984, a 25-year-old white female underwent an above-knee amputation for a synovial sarcoma in the calf. She received postoperative chemotherapy, but developed pulmonary metastases that were resected in April and October 1985. In January 1986, a third thoracotomy showed widespread metastases and chemotherapy was administered. The patient was alive at the time of the last follow-up (May 1986). Microscopic examination of sections from tissue removed at the time of amputation revealed a typical biphasic synovial sarcoma of the soft tissue of the left calf. The metastatic lesions showed a synovial sarcoma, lacking the typical biphasic pattern.Patient 2. A 24-year-old black female had, in April 1984, a 3-month history of pain and swelling of the right foot. A needle biopsy was used to identify a synovial sarcoma, and a below-knee amputation was performed a month later. The tumor microscopically invaded adjacent tissues but no distant disease was found. She remained free of tumor until multiple pulmonary metastases were found 6 months later. She responded transiently to chemotherapy but died 18 months after the initial diagnosis of synovial sarcoma. Histologically the tumor was a high-grade synovial sarcoma of the monoph...

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Section: Methodsmentioning

confidence: 99%

Involvement of chromosome X in primary cytogenetic change in human neoplasia: nonrandom translocation in synovial sarcoma.

Turc‐Carel¹,

Cin²,

Limon³

et al. 1987

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

198

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“…TIMP is known to inhibit interstitial collagenase, gelatinases, and stromelysin (6,(24)(25)(26)(27) and to form a stoichiometric complex with collagenase (28,29); at present, MI has been shown to inhibit interstitial collagenase and gelatinases (10). Thus there may be overlap in their interactions with metalloproteinases.…”

Section: Discussionmentioning

confidence: 99%

cDNA cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases.

Boone

Johnson²,

Clerck³

et al. 1990

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

178

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The purification and characterization of a metalloproteinase inhibitor (MI) from bovine aortic endothelial cells, and the demonstration that it is related to, but distinct from, tissue inhibitor of metalloproteinases (TIMP) 2). These zinc-dependent endopeptidases include interstitial collagenase (MMP-1), 72-kDa gelatinase (type IV collagenase, MMP-2), 92-kDa gelatinase, and stromelysin (proteoglycanase, transin, MMP-3). Virtually all extracellular matrix constituents can be degraded by this family of enzymes, and while there is some specificity in substrate recognition, there is also considerable overlap (2).The MMPs are synthesized and secreted as inactive zymogens, and their activity in the extracellular milieu is regulated by activators and inhibitors (2). Changes in the balance between active enzymes and their inhibitors may be involved in a number of human diseases, including arthritis, fibrosis, and tumor invasion (see review, ref. 3).Several inhibitors of metalloproteinases have been described and characterized. These include small cationic proteins extracted from cartilage and large blood vessels (4); a2-macroglobulin, a major serum inhibitor with Mr -725,000 (5); and tissue inhibitor of metalloproteinases (TIMP), a glycoprotein of Mr 'z30,000 (6, 7) for which the human cDNA has been cloned and sequenced (8,9). TIMP is ubiquitous among tissues and species and is considered a major regulatory inhibitor in the extracellular milieu (see review, ref. 2).We recently described the purification and characterization of TIMP and a novel metalloproteinase inhibitor (designated MI), both secreted by bovine aortic endothelial cells (10). The MI was shown to have an apparent Mr of 27,500, to be unglycosylated, and to have 51% identity to the bovine TIMP in the first 45 (8,9). Deoxyinosine (I) was used at codon nucleotide positions of fourfold degeneracy (11)

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“…EGF and TIMPs (tissue inhibitors of matrix metalloproteinases) may be intrauterine epigenetic modifiers for MEE cell differentiation, because they are contained in amniotic fluid (Sundell et al, 1980;Murphy et al, 1981;Bunning et al, 1984;Kelly, et al, 1997) and can inhibit MEE cell disappearance in the fusing palate in vitro (Dixon and Ferguson, 1992;Blavier et al, 2001;Yamamoto et al, 2003). However, since amniotic fluid could prevent MEE cell differentiation only when the MEE was exposed directly to the fluid, palatal shelf contact and midline seam formation are prerequisite for MEE cell differentiation as well as palatal fusion to occur in utero (Fig.…”

Section: G D E H F I Jmentioning

confidence: 99%

Terminal differentiation of palatal medial edge epithelial cells in vitro is not necessarily dependent on palatal shelf contact and midline epithelial seam formation

Takigawa

Shiota²

2004

Int. J. Dev. Biol.

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During fusion of the mammalian secondary palate, it has been suggested that palatal medial edge epithelial (MEE) cells disappear by means of apoptosis, epithelial-mesenchymal transformation (EMT) and epithelial cell migration. However, it is widely believed that MEE cells never differentiate unless palatal shelves make contact and the midline epithelial seam is formed. In order to clarify the potential of MEE cells to differentiate, we cultured single (unpaired) palatal shelves of ICR mouse fetuses by using suspension and static culture methods with two kinds of gasmixtures. We thereby found that MEE cells can disappear throughout the medial edge even without contact and adhesion to the opposing MEE in suspension culture with 95% O 2 /5% CO 2 . Careful examination of MEE cell behavior in the culture revealed that apoptosis, EMT, and epithelial cell migration all occurred at various stages of MEE cell disappearance, including the transient formation and disappearance of epithelial triangles and islets. In contrast, MEE cells showed poor differentiation in static culture in a CO 2 incubator. Furthermore, mouse and human amniotic fluids were found to prevent MEE cell differentiation in the cultured single palatal shelf, although paired palatal shelves fused successfully even in the presence of amniotic fluid. We therefore conclude that terminal differentiation of MEE cells is not necessarily dependent on palatal shelf contact and midline epithelial seam formation, but such MEE cell differentiation appears to be prevented in utero by amniotic fluid unless palatal shelves make close contact and the midline epithelial seam is formed.

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Metalloproteinase inhibitors from bovine cartilage and body fluids

Cited by 60 publications

References 29 publications

Involvement of chromosome X in primary cytogenetic change in human neoplasia: nonrandom translocation in synovial sarcoma.

Involvement of chromosome X in primary cytogenetic change in human neoplasia: nonrandom translocation in synovial sarcoma.

cDNA cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases.

Terminal differentiation of palatal medial edge epithelial cells in vitro is not necessarily dependent on palatal shelf contact and midline epithelial seam formation

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