Glycoprotein 340 in mucosal immunity and ocular surface

Osei, Kwaku A.; Deivanayagam, Champion; Nichols, Jason J.

doi:10.1016/j.jtos.2018.04.006

Cited by 8 publications

(6 citation statements)

References 83 publications

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“…DMBT1 has previously been detected in various tissues, such as the small intestine, lungs, vagina, placenta, mammillary ducts, and ocular surfaces. 11,23–27 However, to date, the localization and distribution of DMBT1 has not been systematically studied in healthy human tissues. Therefore, we aimed to systematically investigate the localization and distribution of DMBT1 in different healthy human organ samples.…”

Section: Introductionmentioning

confidence: 99%

Immunohistochemical Localization of Deleted in Malignant Brain Tumors 1 in Normal Human Tissues

Nexøe

Pedersen

Huth

et al. 2020

J Histochem Cytochem.

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Deleted in malignant brain tumors 1 (DMBT1) is part of the innate immune system and is expressed on mucosal surfaces in various tissues throughout the human body. However, to date, the localization of DMBT1 has not been investigated systematically and comprehensively in normal human tissues. In this study, we analyzed the mRNA expression of DMBT1 in human tissue by quantitative real-time PCR and examined its localization and distribution in the tissue by immunohistochemical staining using the monoclonal DMBT1 antibody HYB213-6. Anti-ovalbumin was used as an isotype control. The highest level of mRNA expression of DMBT1 was found in the small intestine, and the expression level was high throughout the luminal digestive tract. The expression of DMBT1 was especially high in the luminal digestive tract and salivary glands. The lowest expression level was found in the spleen. Immunohistochemical staining showed a high expression level of DMBT1 on mucosal surfaces throughout the body. There was a clear correlation between the mRNA expression and immunohistochemical expression of DMBT1 in the tissue. DMBT1 is strongly expressed on mucosal surfaces and in salivary glands

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Section: Introductionmentioning

confidence: 99%

Immunohistochemical Localization of Deleted in Malignant Brain Tumors 1 in Normal Human Tissues

Nexøe

Pedersen

Huth

et al. 2020

J Histochem Cytochem.

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“…Wang et al suggested that the water-soluble Na-polyP can be used as a biomimetic tear fluid to restore the corneal surface [ 296 ]. Except from polyP, many other substances are reported to have potential functions in improving corneal regeneration, such as trehalose, polymer 2-methacryloyloxyethyl phosphorylcholine (poly-MPC), glycoprotein 340, ferrostatin-1, agrin, fiber-reinforced gelatin methacrylate hydrogel, and keratan sulfate [ 297 , 298 , 299 , 300 , 301 , 302 ]. These potential substances may exert beneficial effects in clinical practice for patients with LSCD.…”

Section: Therapy Of Lscdmentioning

confidence: 99%

Corneal Epithelial Stem Cells–Physiology, Pathophysiology and Therapeutic Options

Ruan

Jiang

Musayeva

et al. 2021

Cells

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In the human cornea, regeneration of the epithelium is regulated by the stem cell reservoir of the limbus, which is the marginal region of the cornea representing the anatomical and functional border between the corneal and conjunctival epithelium. In support of this concept, extensive limbal damage, e.g., by chemical or thermal injury, inflammation, or surgery, may induce limbal stem cell deficiency (LSCD) leading to vascularization and opacification of the cornea and eventually vision loss. These acquired forms of limbal stem cell deficiency may occur uni- or bilaterally, which is important for the choice of treatment. Moreover, a variety of inherited diseases, such as congenital aniridia or dyskeratosis congenita, are characterized by LSCD typically occurring bilaterally. Several techniques of autologous and allogenic stem cell transplantation have been established. The limbus can be restored by transplantation of whole limbal grafts, small limbal biopsies or by ex vivo-expanded limbal cells. In this review, the physiology of the corneal epithelium, the pathophysiology of LSCD, and the therapeutic options will be presented.

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“…Deleted in malignant brain tumors 1 (DMBT1), also known as salivary agglutinin or gp‐340, is a high molecular mass glycoprotein belonging to the scavenger receptor cysteine‐rich (SRCR) superfamily (Osei et al., 2018; Reichhardt et al., 2017). The DMBT1 protein is composed of conserved peptide motifs: 14 SRCR domains that are separated by SRCR‐interspersed domains (SIDs), two C1r/C1s Uegf Bmp1 domains, and a zona pellucida domain (Bikker et al., 2002).…”

Section: Introductionmentioning

confidence: 99%

A novel mannose‐containing sialoprotein adhesin involved in the binding of Candida albicans cells to DMBT1

Setoguchi

Nagata

Oho

2022

Molecular Oral Microbiology

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Candida albicans colonizes the oral cavity and causes oral candidiasis and early childhood caries synergistically with cariogenic Streptococcus mutans. Colonization of oral tissues with C. albicans is an essential step in the initiation of these infectious diseases. Deleted in malignant brain tumors 1 (DMBT1), also known as salivary agglutinin or gp‐340, belongs to the scavenger receptor cysteine‐rich (SRCR) superfamily and has important functions in innate immunity. In the oral cavity, DMBT1 causes microbial adherence to tooth enamel and oral mucosa surfaces, but the adherence of C. albicans to DMBT1 has not been examined. In this study, we investigated the binding of C. albicans to DMBT1 and isolated the fungal components responsible for the binding. Candida albicans specifically bound to DMBT1 and strongly bound to the peptide domain SRCRP2. Binding to SRCRP2 was inhibited by N‐acetylneuraminic acid and mannose and by lectins recognizing these sugars. The isolated component had a molecular mass of 25 kDa, contained sialic acid and mannose residues, and inhibited C. albicans binding to SRCRP2. The localization of the 25‐kDa protein on the surface of C. albicans cell walls was confirmed by immunostaining and a cell ELISA using an antiserum to the protein, and Western blotting revealed the presence of the 25‐kDa protein in the cell wall fraction of C. albicans. These results suggest that the isolated adhesin is localized on the surface of C. albicans cell walls and that sialic acid and mannose residues in the adhesin play a significant role in the binding reaction.

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Glycoprotein 340 in mucosal immunity and ocular surface

Cited by 8 publications

References 83 publications

Immunohistochemical Localization of Deleted in Malignant Brain Tumors 1 in Normal Human Tissues

Immunohistochemical Localization of Deleted in Malignant Brain Tumors 1 in Normal Human Tissues

Corneal Epithelial Stem Cells–Physiology, Pathophysiology and Therapeutic Options

A novel mannose‐containing sialoprotein adhesin involved in the binding of Candida albicans cells to DMBT1

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