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Deleted in malignant brain tumors 1 protein (DMBT1)

Target
DMBT1
Molecular classification
Scavenger receptor cysteine-rich (SRCR) family, Secreted glycoprotein, Pattern recognition molecule, Extracellular matrix protein, Contains CUB domains and zona pellucida (ZP) domain
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Overview

Deleted in malignant brain tumors 1 protein (DMBT1) is a large, multidomain, secreted glycoprotein that is widely expressed at epithelial barriers such as the respiratory tract, gut, and salivary glands[1][2][5][6]. It is a member of the scavenger receptor cysteine-rich (SRCR) superfamily and contains multiple SRCR domains, interspersed with glycosylated regions, as well as CUB and zona pellucida-type domains[1][2][3][5]. DMBT1 acts as a pattern recognition molecule, binding a broad array of pathogens (bacterial and viral), and mediates aggregation and clearance of microbes, providing an important component of mucosal innate immunity[5]. It also binds host immune proteins, including IgA, surfactant proteins, and lactoferrin, modulating immune defense at mucosal surfaces[5]. In addition, DMBT1 is involved in epithelial cell differentiation, polarity, and possibly tissue regeneration; its deletion or downregulation is linked to multiple cancers, where it is believed to contribute to tumor immune surveillance and normal tissue architecture[3][6]. DMBT1 is not currently considered a direct therapeutic target, but its altered expression or mutations serve as biomarkers in certain cancers. No drugs are known to directly target DMBT1.

Other names
Scavenger receptor cysteine-rich domain-containing protein DMBT1glycoprotein 340GP340Gp-340SAGSALSAHensinSalivary agglutininSalivary scavenger and agglutininSurfactant pulmonary-associated D-binding proteinvomeroglandinmuclinCRP-ductinEbnerinapactinpancrinbovine gall bladder mucin
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Mechanism of action

not applicable (no approved drugs directly targeting DMBT1)

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Biological functions

Innate immune response (including pattern recognition, pathogen aggregation, and defense at epithelial barriers)Epithelial cell differentiation and polarityInteraction with and binding of IgA, surfactant proteins (e.g., SP-D, SP-A), lactoferrin, bacteria, and virusesTissue regenerationRole in extracellular matrix interactions
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Disease associations

Cancer (especially brain, gastrointestinal, and lung tumors)Infection (broad antimicrobial and antiviral activities)InflammationDental caries (oral pathogen aggregation)Other: Potential links to tissue regeneration and mucosal immunity
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Safety considerations

Genomic instability of the DMBT1 locus in tumors may complicate its use as a biomarker or therapeutic targetNo direct therapeutic agents—safety issues relate mainly to its role as a biomarker or risk indicator
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Biomarkers

Expression levels or deletion of DMBT1 in cancers (especially glioblastoma, medulloblastoma, and gastrointestinal cancers)Differential glycosylation patterns in disease and health

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