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Gene Review

DMBT1  -  deleted in malignant brain tumors 1

Homo sapiens

Synonyms: Deleted in malignant brain tumors 1 protein, GP340, Glycoprotein 340, Gp-340, Hensin, ...
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Disease relevance of DMBT1


High impact information on DMBT1

  • Lack of DMBT1 expression has been demonstrated in 4/5 brain-tumour cell lines [4].
  • DMBT1, a new member of the SRCR superfamily, on chromosome 10q25.3-26.1 is deleted in malignant brain tumours [4].
  • We have used representational difference analysis to identify a homozygous deletion at 10q25.3-26.1 in a medulloblastoma cell line and have cloned a novel gene, DMBT1, spanning this deletion [4].
  • The 13 SRCR domains are followed by two C1r/C1s Uegf Bmp1 domains separated by a 14th SRCR domain and a zona pellucida domain. gp-340 seems to be an alternative spliced form of DMBT1 [6].
  • P-selectin glycoprotein ligand-1 (PSGL-1) is a muclin-like glycoportein ligand for P- and E-selectin on myeloid cells and a subset of lymphocytes [7].

Chemical compound and disease context of DMBT1


Biological context of DMBT1

  • Our refined mapping data point to the 10q25-26 region as the primary target on 10q, an area that also harbors the DMBT1 candidate tumor suppressor gene [9].
  • At the DMBT1 locus, LOH was observed very frequently in all three histological groups, with no significant difference in the frequency of LOH among the three histological groups [2].
  • However, presence or absence of DMBT1 did not correlate with any in vitro phenotype assessed in our model system [10].
  • Moreover, the loss of expression could not be rescued by treatment with a demethylation agent (5-azacytidine) in two NSCLC cell lines lacking DMBT1 expression, suggesting that de novo methylation of the promoter region of the gene is unlikely to play a role in inactivation of the gene [11].
  • An elaborate alternative splicing may generate a great variety of DMBT1 isoforms [12].

Anatomical context of DMBT1


Associations of DMBT1 with chemical compounds

  • The DMBT1 mRNA is expressed throughout the immune system, and Western blot studies demonstrated that isoforms of DMBT1 are identical to the collectin-binding protein gp-340, a glycoprotein that is involved in the respiratory immune defense [5].
  • In rats, uterine DMBT1 RNA levels were dramatically up-regulated by estrogen [13].
  • As determined by a microarray experiment and quantitative analysis of RNA levels, mifepristone inhibited estrogenic induction of DMBT1 [13].
  • Immunohistochemical studies showed that DMBT1 is specifically induced in glandular and luminal epithelia of the rat endometrium [13].
  • It led to an exchange of an evolutionary conserved proline residue for serine and located within the second CUB domain of DMBT1 [14].

Physical interactions of DMBT1

  • Glycoprotein-340 (gp-340) was first identified as a surfactant protein (SP)-D-binding molecule purified from lung lavage of patients with alveolar proteinosis (Holmskov, et al., J. Biol. Chem. 1997;272:13743) [15].
  • Salivary agglutinin is encoded by DMBT1 and has been shown to bind Streptococcus mutans and Helicobacter pylori [16] and binds secretory IgA in calcium dependent interaction [17].

Regulatory relationships of DMBT1


Other interactions of DMBT1


Analytical, diagnostic and therapeutic context of DMBT1

  • Subsequent cloning and characterization of the rat DMBT1 homologue revealed a highly inducible expression in ductular reactions composed of transit-amplifying ductular (oval) cells, but not in ductular reactions after ligation of the common bile duct [8].
  • High-quality blood DNA samples were available in 5 tumors carrying homozygous deletion and, using long-range PCR, 3 of these blood samples showed germline hemizygous deletions in a region between introns 10 and 26 of DMBT1 [23].
  • We assembled a 4.5 kb porcine DMBT1 cDNA sequence from RT-PCR amplified seminal vesicle RNA [24].
  • Immunohistochemistry showed nerves, sweat glands and the stratum spinosum of the epidermis to be DMBT1 protein positive, whereas the naevi and melanoma cells themselves were negative [25].
  • So far, DMBT1 is obtained from natural sources such as bronchioalveolar lavage or saliva, resulting in time consuming sample collection, low yields, and protein preparations which may substantially vary due to differential processing and genetic polymorphism, all of which impedes functional research on DMBT1 [26].


  1. Acquisition of the glioblastoma phenotype during astrocytoma progression is associated with loss of heterozygosity on 10q25-qter. Fujisawa, H., Kurrer, M., Reis, R.M., Yonekawa, Y., Kleihues, P., Ohgaki, H. Am. J. Pathol. (1999) [Pubmed]
  2. Allelic deletion analyses of MMAC/PTEN and DMBT1 loci in gliomas: relationship to prognostic significance. Lin, H., Bondy, M.L., Langford, L.A., Hess, K.R., Delclos, G.L., Wu, X., Chan, W., Pershouse, M.A., Yung, W.K., Steck, P.A. Clin. Cancer Res. (1998) [Pubmed]
  3. Site-characteristic expression and induction of trefoil factor family 1, 2 and 3 and malignant brain tumor-1 in normal and diseased intrahepatic bile ducts relates to biliary pathophysiology. Sasaki, M., Tsuneyama, K., Saito, T., Kataoka, H., Mollenhauer, J., Poustka, A., Nakanuma, Y. Liver Int. (2004) [Pubmed]
  4. DMBT1, a new member of the SRCR superfamily, on chromosome 10q25.3-26.1 is deleted in malignant brain tumours. Mollenhauer, J., Wiemann, S., Scheurlen, W., Korn, B., Hayashi, Y., Wilgenbus, K.K., von Deimling, A., Poustka, A. Nat. Genet. (1997) [Pubmed]
  5. DMBT1 encodes a protein involved in the immune defense and in epithelial differentiation and is highly unstable in cancer. Mollenhauer, J., Herbertz, S., Holmskov, U., Tolnay, M., Krebs, I., Merlo, A., Schrøder, H.D., Maier, D., Breitling, F., Wiemann, S., Gröne, H.J., Poustka, A. Cancer Res. (2000) [Pubmed]
  6. Cloning of gp-340, a putative opsonin receptor for lung surfactant protein D. Holmskov, U., Mollenhauer, J., Madsen, J., Vitved, L., Gronlund, J., Tornoe, I., Kliem, A., Reid, K.B., Poustka, A., Skjodt, K. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  7. P-selectin glycoprotein ligand-1 is broadly expressed in cells of myeloid, lymphoid, and dendritic lineage and in some nonhematopoietic cells. Laszik, Z., Jansen, P.J., Cummings, R.D., Tedder, T.F., McEver, R.P., Moore, K.L. Blood (1996) [Pubmed]
  8. Heterogeneity of ductular reactions in adult rat and human liver revealed by novel expression of deleted in malignant brain tumor 1. Bisgaard, H.C., Holmskov, U., Santoni-Rugiu, E., Nagy, P., Nielsen, O., Ott, P., Hage, E., Dalhoff, K., Rasmussen, L.J., Tygstrup, N. Am. J. Pathol. (2002) [Pubmed]
  9. Somatic deletion mapping on chromosome 10 and sequence analysis of PTEN/MMAC1 point to the 10q25-26 region as the primary target in low-grade and high-grade gliomas. Maier, D., Zhang, Z., Taylor, E., Hamou, M.F., Gratzl, O., Van Meir, E.G., Scott, R.J., Merlo, A. Oncogene (1998) [Pubmed]
  10. Functional and molecular analyses of 10q deletions in human gliomas. Steck, P.A., Lin, H., Langford, L.A., Jasser, S.A., Koul, D., Yung, W.K., Pershouse, M.A. Genes Chromosomes Cancer (1999) [Pubmed]
  11. Expression of DMBT1, a candidate tumor suppressor gene, is frequently lost in lung cancer. Wu, W., Kemp, B.L., Proctor, M.L., Gazdar, A.F., Minna, J.D., Hong, W.K., Mao, L. Cancer Res. (1999) [Pubmed]
  12. Deleted in Malignant Brain Tumors 1 is a versatile mucin-like molecule likely to play a differential role in digestive tract cancer. Mollenhauer, J., Herbertz, S., Helmke, B., Kollender, G., Krebs, I., Madsen, J., Holmskov, U., Sorger, K., Schmitt, L., Wiemann, S., Otto, H.F., Gröne, H.J., Poustka, A. Cancer Res. (2001) [Pubmed]
  13. The putative tumor suppressor deleted in malignant brain tumors 1 is an estrogen-regulated gene in rodent and primate endometrial epithelium. Tynan, S., Pacia, E., Haynes-Johnson, D., Lawrence, D., D'Andrea, M.R., Guo, J.Z., Lundeen, S., Allan, G. Endocrinology (2005) [Pubmed]
  14. Frequent downregulation of DMBT1 and galectin-3 in epithelial skin cancer. Mollenhauer, J., Deichmann, M., Helmke, B., Müller, H., Kollender, G., Holmskov, U., Ligtenberg, T., Krebs, I., Wiemann, S., Bantel-Schaal, U., Madsen, J., Bikker, F., Klauck, S.M., Otto, H.F., Moldenhauer, G., Poustka, A. Int. J. Cancer (2003) [Pubmed]
  15. Glycoprotein-340 binds surfactant protein-A (SP-A) and stimulates alveolar macrophage migration in an SP-A-independent manner. Tino, M.J., Wright, J.R. Am. J. Respir. Cell Mol. Biol. (1999) [Pubmed]
  16. Salivary agglutinin, which binds Streptococcus mutans and Helicobacter pylori, is the lung scavenger receptor cysteine-rich protein gp-340. Prakobphol, A., Xu, F., Hoang, V.M., Larsson, T., Bergstrom, J., Johansson, I., Frängsmyr, L., Holmskov, U., Leffler, H., Nilsson, C., Borén, T., Wright, J.R., Strömberg, N., Fisher, S.J. J. Biol. Chem. (2000) [Pubmed]
  17. Binding of salivary agglutinin to IgA. Ligtenberg, A.J., Bikker, F.J., De Blieck-Hogervorst, J.M., Veerman, E.C., Nieuw Amerongen, A.V. Biochem. J. (2004) [Pubmed]
  18. Lung and salivary scavenger receptor glycoprotein-340 contribute to the host defense against influenza A viruses. Hartshorn, K.L., White, M.R., Mogues, T., Ligtenberg, T., Crouch, E., Holmskov, U. Am. J. Physiol. Lung Cell Mol. Physiol. (2003) [Pubmed]
  19. Clinical utility of fluorescence in situ hybridization (FISH) in morphologically ambiguous gliomas with hybrid oligodendroglial/astrocytic features. Fuller, C.E., Schmidt, R.E., Roth, K.A., Burger, P.C., Scheithauer, B.W., Banerjee, R., Trinkaus, K., Lytle, R., Perry, A. J. Neuropathol. Exp. Neurol. (2003) [Pubmed]
  20. Loss of a small region around the PTEN locus is a major chromosome 10 alteration in prostate cancer xenografts and cell lines. Hermans, K.G., van Alewijk, D.C., Veltman, J.A., van Weerden, W., van Kessel, A.G., Trapman, J. Genes Chromosomes Cancer (2004) [Pubmed]
  21. Detection of gene amplification and deletion in high-grade gliomas using a genome DNA microarray (GenoSensor Array 300). Sasaki, T., Arai, H., Beppu, T., Ogasawara, K. Brain tumor pathology. (2003) [Pubmed]
  22. Regulation of DMBT1 via NOD2 and TLR4 in intestinal epithelial cells modulates bacterial recognition and invasion. Rosenstiel, P., Sina, C., End, C., Renner, M., Lyer, S., Till, A., Hellmig, S., Nikolaus, S., Fölsch, U.R., Helmke, B., Autschbach, F., Schirmacher, P., Kioschis, P., Hafner, M., Poustka, A., Mollenhauer, J., Schreiber, S. J. Immunol. (2007) [Pubmed]
  23. Mutation analysis of DMBT1 in glioblastoma, medulloblastoma and oligodendroglial tumors. Pang, J.C., Dong, Z., Zhang, R., Liu, Y., Zhou, L.F., Chan, B.W., Poon, W.S., Ng, H.K. Int. J. Cancer (2003) [Pubmed]
  24. Molecular characterization of the porcine deleted in malignant brain tumors 1 gene (DMBT1). Haase, B., Humphray, S.J., Lyer, S., Renner, M., Poustka, A., Mollenhauer, J., Leeb, T. Gene (2006) [Pubmed]
  25. Analysis of losses of heterozygosity of the candidate tumour suppressor gene DMBT1 in melanoma resection specimens. Deichmann, M., Mollenhauer, J., Helmke, B., Thome, M., Hartschuh, W., Poustka, A., Näher, H. Oncology (2002) [Pubmed]
  26. Generation of a vector system facilitating cloning of DMBT1 variants and recombinant expression of functional full-length DMBT1. End, C., Lyer, S., Renner, M., Stahl, C., Ditzer, J., Holloschi, A., Kuhn, H.M., Flammann, H.T., Poustka, A., Hafner, M., Mollenhauer, J., Kioschis, P. Protein Expr. Purif. (2005) [Pubmed]
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