Matrilysin expression in human prostate carcinoma

Knox, J. David; Wolf, Catherine; Mcdaniel, Kathleen M.; Clark, Virginia A.; Loriot, Maria; Bowden, G. Tim; Nagle, Ray B.

doi:10.1002/(sici)1098-2744(199601)15:1<57::aid-mc8>3.0.co;2-p

Cited by 73 publications

(44 citation statements)

References 24 publications

(17 reference statements)

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“…However, no studies have elucidated the molecular mechanism regulating MMP-7 localization to the basal epithelial compartment or the depolarized diffuse cytoplasmic distribution of MMP-7 in adenocarcinoma cells at the invasive front. Similar to other MMPs such as MMP-2, the activated form of MMP-7 is readily detected within both carcinoma 11,17 and normal intestinal tissues. 6 Our previous in vitro biochemical studies have shown that proMMP-7 is fully activated by treatment with trypsin or MMP-3, and partially with plasmin or leukocyte elastase.…”

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confidence: 82%

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Shiomi

Inoki

Kataoka

et al. 2005

Laboratory Investigation

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Matrix metalloproteinase-7 (MMP-7) (also known as matrilysin-1) is secreted as a proenzyme (proMMP-7) and plays a key role in the degradation of various extracellular matrix (ECM) and non-ECM molecules after activation. To identify the binding proteins related to proMMP-7 activation, a human lung cDNA library was screened by yeast two-hybrid system using proMMP-7 as bait. We identified a candidate molecule CD151, which is a member of the transmembrane 4 superfamily. Complex formation of proMMP-7 with CD151 was demonstrated by immunoprecipitation of the molecules from CaR-1 cells, a human rectal carcinoma cell line, expressing both proMMP-7 and CD151, and CD151 stable transfectants incubated with proMMP-7. Yeast twohybrid assays using deletion mutants of proMMP-7 and CD151 suggested an interaction between the propeptide of proMMP-7 and the COOH-terminal extracellular loop of CD151. The binding activity of 125 I-labeled proMMP-7 to CD151 on the cell membranes was shown with CD151 stable transfectants. Laser-scanning confocal microscopy demonstrated that proMMP-7 colocalizes with CD151 on the cell membranes of CD151 stable transfectants and CaR-1 cells. In situ zymography using crosslinked carboxymethylated transferrin, a substrate of MMP-7, demonstrated proteinase activity on and around CD151 stable transfectants and CaR-1 cells, while the activity was abolished by their treatment with MMP inhibitors, anti-MMP-7 antibody or anti-CD151 antibody. In human lung adenocarcinoma tissues, colocalization of MMP-7 and CD151 was demonstrated on the carcinoma cells. Metalloproteinase activity was present in these tissues and could be inhibited by antibodies to MMP-7 or CD151. These data demonstrate for the first time that proMMP-7 is captured and activated on the cell membranes through interaction with CD151, and suggest the possibility that similar to the MT1-MMP/MMP-2 system, MMP-7 is involved in the pericellular activation mechanism mediated by CD151, a crucial step in proteolysis on the cell membranes under various pathophysiological conditions including cancer invasion and metastasis.

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confidence: 82%

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Shiomi

Inoki

Kataoka

et al. 2005

Laboratory Investigation

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“…34 This has been observed in adenomas or premalignant lesions of the intestine, stomach, prostate, breast and ovary. [51][52][53][54][55][56] We observed low levels of MMP7 in normal human lung epithelial cells, while the expression increased in premalignant and neoplastic cells. Using genetically manipulated animals, a definite role for MMP7 in early tumor development has been established.…”

Section: Discussionmentioning

confidence: 99%

Achaete-scute homolog-1 linked to remodeling and preneoplasia of pulmonary epithelium

Wang

Dakir

Naizhen

et al. 2007

Laboratory Investigation

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The basic helix-loop-helix protein achaete-scute homolog-1 (ASH1) is involved in lung neuroendocrine (NE) differentiation and tumor promotion in SV40 transgenic mice. Constitutive expression of human ASH-1 (hASH1) in mouse lung results in hyperplasia and remodeling that mimics bronchiolization of alveoli (BOA), a potentially premalignant lesion of human lung carcinomas. We now show that this is due to sustained cellular proliferation in terminal bronchioles and resistance to apoptosis. Throughout the airway epithelium the expression of anti-apoptotic Bcl-2 and c-Myb was increased and Akt/mTOR pathway activated. Moreover, the expression of matrix metalloproteases (MMPs) including MMP7 was specifically enhanced at the bronchiolo-alveolar duct junction and BOA suggesting that MMPs play a key role in this microenvironment during remodeling. We also detected MMP7 in 70% of human BOA lesions. Knockdown of hASH1 gene in human lung cancer cells in vitro suppressed growth by increasing apoptosis. We also show that forced expression of hASH1 in immortalized human bronchial epithelial cells decreases apoptosis. We conclude that the impact of hASH1 is not limited to cells with NE phenotype. Rather, constitutive expression of hASH1 in lung epithelium promotes remodeling through multiple pathways that are commonly activated during lung carcinogenesis. The collective results suggest a novel model of BOA formation via hASH1-induced suppression of the apoptotic pathway. Our study yields a promising new preclinical tool for chemoprevention of peripheral lung carcinomas. KEYWORDS: achaete-scute homolog 1; apoptosis; bronchiolization of alveoli; lung; mouse model; preneoplasia; proliferation Lung cancer is the leading cause of cancer deaths in both men and women in the United States. The 5-year survival rate has remained low (15%), because the disease is generally detected at advanced and disseminated stage. 1 Contributing to the late diagnosis is the fact that precursor lesions for most lung cancer types are poorly understood. We have previously shown that the deletion of achaete-scute homolog-1 (ASH1, ASCL1), a proneural transcription factor, highly expressed in lung neuroendocrine (NE) cancers leads to the absence of pulmonary NE cells (PNECs), potential progenitors for NE cancers. 2 Constitutive expression of human ASH1 (hASH1) in the airway epithelium, on the other hand, results in epithelial proliferation and metaplasia suggesting a preneoplastic phenotype.ASH1 belongs to a diverse family of transcriptional regulators involved in fetal development and cancer that utilize the evolutionarily conserved basic helix-loop-helix (bHLH) motif. 3 Murine ASH1 (mASH1) plays a critical role in the development of the brain and the diffuse NE system including adrenal medullary chromaffin cells, thyroid parafollicular C cells, glomus chief cells and PNECs, 2,4-8 potential progenitors for small cell lung cancer (SCLC). During neurogenesis mASH1 expression is confined to mitotically active precursors where it is involved in the early stages o...

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“…It has been clearly demonstrated by in situ hybridization that the overexpression of matrilysin mRNA is confined to the epithelial cells of these structures and is not present in the surrounding stroma or infiltrating leukocytes (12). Immunohistochemical analysis confirmed that the expression of matrilysin mRNA in the prostate epithelium correlates with the expression of matrilysin protein.…”

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confidence: 79%

“…In the normal prostate, we have observed that inflamed ductule and acinar epithelia frequently express high levels of matrilysin (11,12). It has been clearly demonstrated by in situ hybridization that the overexpression of matrilysin mRNA is confined to the epithelial cells of these structures and is not present in the surrounding stroma or infiltrating leukocytes (12).…”

mentioning

confidence: 98%

Interleukin-1β Secreted from Monocytic Cells Induces the Expression of Matrilysin in the Prostatic Cell Line LNCaP

Klein

Borchers

Sundareshan

et al. 1997

Journal of Biological Chemistry

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Matrilysin is a matrix metalloprotease that is overexpressed in cancer cells of epithelial origin and in normal tissues during events involving matrix remodeling such as the cycling endometrium. We previously observed that inflamed ductule and acinar epithelia in the prostate also overexpress matrilysin. The presence of infiltrating macrophages in these areas prompted us to determine if factors secreted from monocytes could induce matrilysin expression in a human prostatic cell line. Conditioned media collected from the monocyte cell line THP-1 following lipopolysaccharide treatment substantially induced matrilysin protein and mRNA expression in LNCaP prostate carcinoma cells. Matrilysin expression in LNCaP cells was also induced by recombinant interleukin (IL)-1 (50 pM), but not by equimolar concentrations of recombinant tumor necrosis factor-␣ or IL-6. The matrilysin-inducing activity of THP-1 conditioned medium was completely abrogated by preincubation with a neutralizing antibody to IL-1␤. Transient transfection analyses with a chimeric human matrilysin promoter-chloramphenicol acetyltransferase reporter construct demonstrated that IL-1␤ activates transcription through the matrilysin promoter in LNCaP cells. This is the first report of matrilysin induction by an inflammatory cytokine in a cell line of epithelial origin, and the results suggest a potential mechanism for the overexpression of matrilysin in inflamed ducts and glands of the prostate.The matrix metalloproteases are a family of enzymes that degrade extracellular matrix proteins. Matrilysin (PUMP-1, MMP-7) is a relatively recently described matrix metalloprotease belonging to the stromelysin enzyme subclass (reviewed in Ref. 1). Matrilysin is capable of degrading a diverse set of extracellular matrix proteins including proteoglycans, fibronectin, entactin, laminin, gelatin, and elastin. The expression of matrilysin has been demonstrated in the cycling endometrium (2); the involuting rat prostate (3) and uterus (4); developing mononuclear phagocytes (5); and cancers of the breast (6), lung and upper respiratory tract (7), skin (8), stomach and colon (9, 10), and prostate (11). A unique feature of matrilysin expression is that it appears to predominate in epithelial cells of glandular tissue, while other matrix metalloproteases, such as stromelysin and the gelatinases, are more commonly expressed by cells in the stromal compartment (1). The expression of matrilysin during normal and pathological events that involve matrix remodeling and the cell type specificity of this expression imply an important role for matrilysin in these events.In the normal prostate, we have observed that inflamed ductule and acinar epithelia frequently express high levels of matrilysin (11,12). It has been clearly demonstrated by in situ hybridization that the overexpression of matrilysin mRNA is confined to the epithelial cells of these structures and is not present in the surrounding stroma or infiltrating leukocytes (12). Immunohistochemical analysis confirmed that the ex...

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Matrilysin expression in human prostate carcinoma

Cited by 73 publications

References 24 publications

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Achaete-scute homolog-1 linked to remodeling and preneoplasia of pulmonary epithelium

Interleukin-1β Secreted from Monocytic Cells Induces the Expression of Matrilysin in the Prostatic Cell Line LNCaP

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