Stromelysin-3 mRNA Associated with Myofibroblasts Is Overexpressed in Aggressive Basal Cell Carcinoma and in Dermatofibroma but Not in Dermatofibrosarcoma

Undén, Anne Birgitte; Sandstedt, Bengt; Bruce, K. Ferguson; Hedblad, Mari‐Anne; Ståhle‐Bäckdahl, Mona

doi:10.1111/1523-1747.ep12329541

Cited by 51 publications

(36 citation statements)

References 22 publications

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“…Thus, mRNAs for MMP-1, MMP2 , MMP-11 (Basset et al, 1990), MMP-13 (Nielsen et al, 2001) and MT1-MMP (Okada et al, 1995) have been all found to be expressed by fibroblast-like cells. The fibroblastic cells expressing MMP-11 (Unden et al, 1996), MMP-13 (Nielsen et al, 2001) or MT1-MMP (unpublished data) have been identified as myofibroblasts. It is particularly noteworthy that cocultivation of fibroblasts with tumor cells induced the up-regulation of MMP2 and MT1-MMP expression by fibroblasts (Noel et al, 1994;.…”

Section: Mt1-mmp and Cancermentioning

confidence: 98%

Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis

et al. 2003

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The matrix metalloproteinases (MMPs) constitute a multigene family of over 23 secreted and cell-surface associated enzymes that cleave or degrade various pericellular substrates. In addition to virtually all extracellular matrix (ECM) compounds, their targets include other proteinases, chemotactic molecules, latent growth factors, growth factor-binding proteins and cell surface molecules. The MMP activity is controlled by the physiological tissue inhibitors of MMPs (TIMPs). There is much evidence that MMPs and their inhibitors play a key role during extracellular remodeling in physiological situations and in cancer progression. They have other functions that promoting tumor invasion. Indeed, they regulate early stages of tumor progression such as tumor growth and angiogenesis. Membrane type MMPs (MT-MMPs) constitute a new subset of cell surface-associated MMPs. The present review will focus on MT1-MMP which plays a major role at least, in the ECM remodeling, directly by degrading several of its components, and indirectly by activating pro-MMP2. As our knowledge on the field of MT1-MMP biology has grown, the unforeseen complexities of this enzyme and its interaction with its inhibitor TIMP-2 have emerged, often revealing unexpected mechanisms of action.Keywords: MT1-MMP ; tumoral angiogenesis ; vascular endothelial growth factor ; protease inhibitors ; estradiol MMP structure and functionsMatrix metalloproteinases (MMPs) are a broad family of zinc-binding endopeptidases that play a key role in the extracellular matrix (ECM) degradation associated with cancer cell invasion, metastasis and angiogenesis (Egeblad and Werb, 2002;McCawley and Matrisian, 2000). At present, more than 21 human MMPs and the homologues from other species have been identified (Egeblad and Werb, 2002). The MMP family can be segregated into two groups, the soluble type and the membrane-type MMPs (MT-MMPs and MMP23). Although initially classified according to their substrate specificity (McCawley and Matrisian, 2000), the MMP classification is now based on their structure (Egeblad and Werb, 2002). The 'minimal-domain MMPs' (MMP7 and MMP26) contains (i) a signal peptide that directs them to the endoplasmic reticulum, (ii) a propeptide, with a zinc-interacting thiol (SH) group that maintains the proMMP in a latent form (zymogen), and (iii) a catalytic domain containing the highly conserved Zn 2+ binding site (HEXGHXXGXXHS/T) (Fig. 1). With the exception of MMP23, all other MMPs display a prolinerich hinge region that links the catalytic domain to the hemopexin/vitronectin-like domain. This C-terminal domain influences substrate specificity and the binding to tissue inhibitors of MMPs (TIMPs) and cell surface molecules. The hemopexin-containing MMPs are further distinguished by the presence of specific insert(s). The gelatin-binding MMPs (MMP2 and MMP9 or gelatinases) contain inserts that resemble the collagen-binding type II repeats of fibronectin. The membrane type (MT)-MMPs have a single pass transmembrane domain and a short cytoplasmic...

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Section: Mt1-mmp and Cancermentioning

confidence: 98%

Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis

et al. 2003

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“…37 Stromelysin-3 expression already has been observed in the neoplastic cells of malignant mesenchymal tumors such as histiocytofibrosarcomas, synovialosarcomas, and osteosarcomas 15 as well as in the neoplastic cells of benign mesenchymal tumors such as dermatofibroma of the skin. 38 In this regard, note that in our study the only benign meningioma expressing ST3 had a fibroblastic pattern. In this tumor, ST3 was diffusely expressed within the cytoplasm of the neoplastic and stromal cells.…”

Section: Discussionmentioning

confidence: 49%

Stromelysin‐3 is expressed by aggressive meningiomas

Perret

Duthel

Fotso

et al. 2002

Cancer

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BACKGROUNDStromelysin‐3 (ST3) that belongs to the metalloproteinase family is proposed to play a role in tumor invasion. The purpose of this work was to study the variation of ST3 expression in meningiomas.METHODSTwenty atypical meningiomas were retrieved from the Pathology Department's files at Hopital de Bellevue, Saint‐Etienne, France. They were compared with 20 benign meningiomas randomly selected from the same file. The tumors were classified using standard histologic criteria. Frozen sections of the tumors were immunostained for ST3 and MIB‐1 to evaluate the proliferative activity of tumor cells.RESULTSThe study included 5 fibrous meningiomas, 10 transitional meningiomas, 20 syncitial meningiomas, 2 secretory meningiomas, 2 microcystic meningiomas, and 1 angiomatous meningioma. Stromelysin‐3 was expressed within the stromal and neoplastic cells of only 1 benign meningioma and 13 atypical meningiomas. The MIB‐1 proliferation index was significantly higher in the meningiomas expressing ST3 (Student t test: P < 0.001). The invasion of bone, muscle, and brain by meningiomas as well the recurrence were statistically correlated with their ST3 expression (Kruskal–Wallis nonparametric correlation test, P = 0.001 and P = 0.008, respectively).CONCLUSIONSStromelysin‐3 might play an important role in the invasiveness of meningiomas. Therefore, considering, ST3 in association with evaluation of the MIB‐1 proliferating index may be an useful tool to assess the behavior of meningiomas. Cancer 2002;94:765–72. © 2002 American Cancer Society.DOI 10.1002/cncr.10270

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“…On the other hand, normal PTCH is a transcriptional regulator and down regulates the expression of SMOH. Recent studies using both Northern blotting and in situ hybridization have reported that sporadic and familial BCCs overexpress a dysfunctional, mutated PTCH gene (Gailani et al, 1996;Kallassy et al, 1997;Unden et al, 1997). The over expression of the mutated PTCH mRNA would be presumably due to the loss of PTCH autoregulatory mechanisms (Marigo et al, 1996).…”

Section: Discussionmentioning

confidence: 99%

“…The size limit generally accepted in PCR/SSCP is 250 base pairs. We took various measures to optimize conditions accordingly (Unden et al, 1997). For example, we used Sau3A to enzyme digest exon 13 to shorten the size of the product.…”

Section: Discussionmentioning

confidence: 99%

PTCH gene mutations in invasive transitional cell carcinoma of the bladder

Tw¹,

Maruta²,

Je³

et al. 1998

Oncogene

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LOH analysis suggests that multiple tumor suppressor genes play a role in the development of human TCC. The human homolog of the Drosophila PTCH was recently cloned and mapped to the BCNS locus on 9q22.3, a chromosomal region commonly deleted in TCCs. We ®rst examined the steady state mRNA transcription of the PTCH, SMOH and GLI3 genes of the HH signal transduction pathway in TCC cell lines and normal urothelium. Normal urothelium and TCC cell lines express these three genes within the PTCH signal transduction pathway. We then screened for PTCH mutations in`hot spot' exons 6, 8, 13 and 16 by PCR/ SSCP analysis of genomic DNAs from 54 TCC tumor samples and control autologous peripheral blood lymphocytes. DNA sequence analysis con®rmed TCCspeci®c mutations in two of 54 patients (3.7%). These mutations resulted a single amino acid substitution and two frame shifts. One tumor had PTCH mutations in exon 16 as well as exon 13 and one tumor had a mutation in exon 13 alone. Both TCC tumors that contained PTCH mutations had a loss of heterozygosity at 9q. Although the PTCH protein has an unknown function in urothelial cells, the detection of the PTCH, SMOH and GLI3 transcripts in normal urothelium and TCC cell lines and rare PTCH mutations in tumor samples suggest that the HH pathway may have a role in controlling the proliferation of urothelial cells and that PTCH mutations may contribute to the development of a subset of TCCs.

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Stromelysin-3 mRNA Associated with Myofibroblasts Is Overexpressed in Aggressive Basal Cell Carcinoma and in Dermatofibroma but Not in Dermatofibrosarcoma

Cited by 51 publications

References 22 publications

Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis

Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis

Stromelysin‐3 is expressed by aggressive meningiomas

PTCH gene mutations in invasive transitional cell carcinoma of the bladder

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