Dentin Matrix Protein 1 Is Expressed in Human Lung Cancer

Chaplet, Michael; Leval, Laurence de; Waltregny, David; Detry, Cédric; Fornaciari, Gino; Bevilacqua, Generoso; Fisher, LW; Castronovo, Vincenzo; Bellahcène, Akeila

doi:10.1359/jbmr.2003.18.8.1506

Cited by 39 publications

(31 citation statements)

References 16 publications

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“…Previous and relatively recent reports show the up-regulation of some SIBLINGs in different tumors, including oral cancers (Bellahcéne et al 1996;Waltregny et al 1998;Chaplet et al 2003;. At the same time, reports have indicated that the up-regulation of MMP-2, MMP-3, and/or MMP-9 is associated with increased aggressiveness of tumors (Birkedal-Hansen et al 1993;Brabletz et al 1999;Thomas et al 1999;Ogbureke et al , 2012.…”

Section: Discussionmentioning

confidence: 93%

Expression of Matrix Metalloproteinase (MMP)-20 and Potential Interaction with Dentin Sialophosphoprotein (DSPP) in Human Major Salivary Glands

Koli

Saxena

Ogbureke

2015

J Histochem Cytochem.

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SummaryMatrix metalloproteinase-20 (MMP-20) expression is widely regarded as tooth-specific, with expression limited to dental hard tissues. Necessary for sound enamel formation, MMP-20 and MMP-2 proteolytically process dentin sialophosphoprotein (DSPP) into dentin sialoprotein, dentin phosphoprotein, and dentin glycoprotein during tooth formation. In the mid-2000s, three members of the small integrin-binding ligand N-linked glycoproteins (SIBLINGs) were reported to bind specifically with high affinity (nM) to, and activate, three MMPs in vitro: bone sialoprotein with MMP-2; osteopontin with MMP-3; and dentin matrix protein1 with MMP-9. The SIBLING-MMP interaction was confirmed in biological systems such as the ducts of salivary glands, where all five members of the SIBLINGs are expressed. Recently, we documented MMP-20 expression and interaction with DSPP (another member of the SIBLING family) in human oral squamous cell carcinoma. Here we report the expression of MMP-20, and confirm its co-expression and potential interaction with DSPP in human major salivary gland tissues and cell line using immunohistochemistry, immunofluorescence, western blot, quantitative RT-PCR, and proximity ligation assay. This report reinforces our earlier suggestion that the SIBLING-MMP complexes may be involved in the turnover of extracellular proteins damaged by oxidation byproducts in metabolically active duct epithelial systems. (J Histochem Cytochem 63:524-533, 2015)

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Section: Discussionmentioning

confidence: 93%

Expression of Matrix Metalloproteinase (MMP)-20 and Potential Interaction with Dentin Sialophosphoprotein (DSPP) in Human Major Salivary Glands

Koli

Saxena

Ogbureke

2015

J Histochem Cytochem.

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“…BSP expression was been reported in breast (4,5), prostate (6), lung (7), and thyroid cancer (8). DMP1 has been shown to be strongly up-regulated in lung cancer (9). Elevated levels of MEPE mRNA expression by tumors from patients with hypophosphatemia and osteomalacia have been reported (10).…”

Section: Introductionmentioning

confidence: 99%

Small Integrin Binding Ligand N -Linked Glycoprotein Gene Family Expression in Different Cancers

Fisher

Jain

Tayback

et al. 2004

Clinical Cancer Research

109

115

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Purpose: Members of the small integrin binding ligand N-linked glycoprotein (SIBLING) gene family have the capacity to bind and modulate the activity of matrix metalloproteinases (MMPs). The expression levels of five SIBLING gene family members [bone sialoprotein (BSP), osteopontin (OPN), dentin matrix protein 1 (DMP1), matrix extracellular phosphoglycoprotein (MEPE), and dentin sialophosphoprotein (DSPP)] and certain MMPs were determined using a commercial cancer array.Experimental Design: Cancer profiling arrays containing normalized cDNA from both tumor and corresponding normal tissues from 241 individual patients were used to screen for SIBLING and MMP expression in nine distinct cancer types.Results: Significantly elevated expression levels were observed for BSP in cancer of the breast, colon, stomach, rectum, thyroid, and kidney; OPN in cancer of the breast, uterus, colon, ovary, lung, rectum, and thyroid; DMP1 in cancer of the breast, uterus, colon, and lung; and dentin sialophosphoprotein in breast and lung cancer. The degree of correlation between a SIBLING and its partner MMP was found to be significant within a given cancer type (e.g., BSP and MMP-2 in colon cancer, OPN and MMP-3 in ovarian cancer; DMP1 and MMP-9 in lung cancer). The expression levels of SIBLINGs were distinct within subtypes of cancer (e.g., breast ductal tumors compared with lobular tumors). In general, SIBLING expression increased with cancer stage for breast, colon, lung, and rectal cancer.Conclusions: These results suggest SIBLINGs as potential markers of early disease progression in a number of different cancer types, some of which currently lack vigorous clinical markers.

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“…DMP1 was detected at high levels by Northern analysis in fetal bovine brain and cultured long bone as well as in odontoblasts (6). Most recently, DMP1 was localized by immunohistochemistry in human lung cancer tissue (7).…”

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confidence: 99%

In Vitro Effects of Dentin Matrix Protein-1 on Hydroxyapatite Formation Provide Insights into in Vivo Functions

Tartaix

Doulaverakis

George

et al. 2004

Journal of Biological Chemistry

174

146

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Dentin matrix protein-1 (DMP1) is a mineralized tissue matrix protein synthesized by osteoblasts, hypertrophic chondrocytes, and ameloblasts as well as odontoblasts. DMP1 is believed to have multiple in vivo functions, acting both as a signaling molecule and a regulator of biomineralization. Using a cell-free system in vitro, we evaluated the action of DMP1 in the regulation of hydroxylapatite (HA) formation and crystal growth. The non-phosphorylated recombinant protein acted as an HA nucleator, increasing the amount of mineral formed in a gelatin gel HA growth system relative to protein-free controls. The recombinant protein phosphorylated in vitro had no detectable effect on HA formation and growth. In contrast, phosphorylated bovine DMP1 expressed in marrow stromal cells with an adenovirus vector containing 29.7 phosphates/mol was an effective inhibitor of HA formation and growth. The native full-length protein appeared to be absent or present in only small amounts in the extracellular matrix of bones and teeth. However, two highly phosphorylated fragments representing the N-and C-terminal portions of DMP1 have been identified, apparently arising from proteolytic cleavage of four X-Asp bonds. The highly phosphorylated C-terminal 57-kDa fragment (containing 42 phosphates/mol), like the non-phosphorylated DMP1, was an HA nucleator. These data suggest that, in its native form, DMP1 inhibits mineralization, but when cleaved or dephosphorylated, it initiates mineralization. These in vitro data are consistent with the findings in the DMP1 knockout mouse.Dentin matrix protein-1 (DMP1) 1 is an acidic, phosphorylated, integrin-binding extracellular matrix protein first identified by screening a rat cDNA library (1). Northern blot analysis in the rat originally suggested that the DMP1 message was odontoblast-specific, with in situ hybridization showing DMP1 mRNA expression to be restricted to those fully differentiated odontoblasts engaged in active dentin matrix formation, with transient expression by ameloblasts (1, 2). More recent in situ hybridization studies show a much broader pattern of expression of DMP1, with expression associated with a number of mineralizing tissues, including bone and cementum (3). In rat and chicken bone, immunohistochemical detection showed an association of DMP1 with osteocytes, but not with osteoblasts (4). In the mouse, hypertrophic chondrocytes express more DMP1 than other cell types (5). DMP1 was detected at high levels by Northern analysis in fetal bovine brain and cultured long bone as well as in odontoblasts (6). Most recently, DMP1 was localized by immunohistochemistry in human lung cancer tissue (7).DMP1 is a small protein that has been postulated to have a high affinity for hydroxylapatite (HA) (8,9). This coupled with its localization in mineralized tissues suggested that DMP1 could have an important role in mineralization. DMP1 is a member of the SIBLING (small integrin-binding ligand, Nlinked glycoprotein) family of proteins (10, 11). Like other members of the SIBLING family...

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Dentin Matrix Protein 1 Is Expressed in Human Lung Cancer

Cited by 39 publications

References 16 publications

Expression of Matrix Metalloproteinase (MMP)-20 and Potential Interaction with Dentin Sialophosphoprotein (DSPP) in Human Major Salivary Glands

Expression of Matrix Metalloproteinase (MMP)-20 and Potential Interaction with Dentin Sialophosphoprotein (DSPP) in Human Major Salivary Glands

Small Integrin Binding Ligand N -Linked Glycoprotein Gene Family Expression in Different Cancers

In Vitro Effects of Dentin Matrix Protein-1 on Hydroxyapatite Formation Provide Insights into in Vivo Functions

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