Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Keywords: brain ; PEPTIDE ; RECEPTOR ; tumor ; LUNG ; SITE ; PROTEIN ; PROTEINS ; TUMORS ; FAMILY ; DOMAIN ; BINDING ; BIOLOGY ; MEMBER ; MOLECULAR-BIOLOGY ; SEQUENCE ; SEQUENCES ; SUPPRESSION ; ACID ; FORM ; NUMBER ; PEPTIDES ; SUPERFAMILY ; NETHERLANDS ; DOMAINS ; MOLECULAR-CLONING ; DMBT1 ; SALIVARY AGGLUTININ ; SURFACTANT PROTEIN-D ; HOST-DEFENSE ; SCAVENGER RECEPTOR ; molecular biology ; MOTIF ; AGGLUTININ ; brain tumor ; BRAIN-TUMORS ; DEFENSE ; pathogen ; RESIDUES ; SPONGE GEODIA-CYDONIUM ; SRCR DOMAIN ; STREPTOCOCCUS-MUTANS ; TUMOR SUPPRESSION
    Abstract: The scavenger receptor cysteine-rich (SRCR) proteins form an archaic group of metazoan proteins characterized by the presence of SRCR domains. These proteins are classified in group A and B based on the number of conserved cysteine residues in their SRCR domains, i.e. six for group A and eight for group B. The protein DMBT1 (deleted in malignant brain tumors 1), which is identical to salivary agglutinin and lung gp-340, belongs to the group B SRCR proteins and is considered to be involved in tumor suppression and host defense by pathogen binding. In a previous study we used non-overlapping synthetic peptides covering the SRCR consensus sequence to identify a 16-amino acid bacteria-binding protein loop (peptide SRCRP2; QGRVEVLYRGSWGTVC) within the SRCR domains. In this study, using overlapping peptides, we pinpointed the minimal bacteria-binding site on SRCRP2, and thus DMBT1, to an 11-amino acid motif (DMBT1 pathogen-binding site 1 or DMBT1pbs1; GRVEVLYRGSW). An alanine substitution scan revealed that VEVL and Trp are critical residues in this motif. Bacteria binding by DMBT1pbs1 was different from the bacteria binding by the macrophage receptor MARCO in which an RXR motif was critical. In addition, the homologous consensus sequences of a number of SRCR proteins were synthesized and tested for bacteria binding. Only consensus sequences of DMBT1 orthologues bound bacteria by this motif
    Type of Publication: Journal article published
    PubMed ID: 15355985
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    Keywords: brain ; RECEPTOR ; CANCER ; EXPRESSION ; tumor ; LUNG ; lung cancer ; LUNG-CANCER ; GENE ; TISSUE ; TUMORS ; TISSUES ; immunohistochemistry ; EPITHELIAL-CELLS ; NETHERLANDS ; TRACT ; GLANDS ; salivary gland ; TERMINAL DIFFERENTIATION ; BINDS ; DMBT1 ; GP-340 ; SALIVARY AGGLUTININ ; SURFACTANT PROTEIN-D ; MALIGNANT BRAIN-TUMORS ; AGGLUTININ ; brain tumor ; BRAIN-TUMORS ; DEFENSE ; STREPTOCOCCUS-MUTANS ; DIGESTIVE-TRACT ; DMBT1 EXPRESSION ; salivary gland tumor ; salivary glands ; SRCR ; TUMOR-SUPPRESSOR ; VARIANT
    Abstract: Salivary agglutinin (SAG) is encoded by the gene Deleted in Malignant Brain Tumors 1 (DMBT1) and represents the salivary variant of DMBT1 (DMBT1(SAG) ). While SAG is a bona fide anti-caries factor, DMBT1 was proposed as a candidate tumor-suppressor for brain, digestive tract, and lung cancer. Though DMBT1(SAG) is expressed in the salivary glands, its expression in salivary gland tumors is unknown. Here we analyzed DMBT1(SAG) expression in 20 salivary gland tumors and 14 tumor-flanking tissues by immunohistochemistry. DMBT1(SAG) in salivary gland tumors resembles the changes of expression levels known from DMBT1 in tumors in other cancer types. Particularly, DMBT1(SAG) was up-regulated in 10/14 tumor-flanking tissues, and a strong staining of the luminal content in the tumor and/or the tumor-flanking tissue was observed in 14/20 cases. This suggests that, in addition to its role in caries defense, SAG may serve as a potential tumor indicator and/or tumor suppressor in salivary gland tissue
    Type of Publication: Journal article published
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...