A mannose receptor mediates mannosyl-rich glycoprotein-induced mitogenesis in bovine airway smooth muscle cells.

Lew, D. Betty; Songu-Mize, Emel; Pontow, Suzanne; Stahl, Philip D.; Rattazzi, Mario C.

doi:10.1172/jci117535

Cited by 60 publications

(36 citation statements)

References 49 publications

(32 reference statements)

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“…Several lectin receptors, including the mannose receptor family, are involved in the capture of glycosylated antigen [2] and possibly more than one lectin receptor may be expressed by cattle DC, as has been reported for human macrophages [60]. Lectin receptors are known to effectively mediate uptake by endocytic routes involving small coated vesicles [52,61]. In this respect, the slightly reduced Fig.…”

Section: Discussionmentioning

confidence: 74%

Involvement of caveolae in the uptake of respiratory syncytial virus antigen by dendritic cells

Werling¹,

Hope²,

Chaplin

et al. 1999

Journal of Leukocyte Biology

178

144

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The uptake of respiratory syncytial virus (RSV) antigen by cattle dendritic cells was investigated. Pathways of antigen uptake were monitored by flow cytometry using specific tracers and by proliferation assays, which were used to measure the presentation of RSV antigen and ovalbumin. Inhibitors that differentially affected pathways were used to distinguish them. Presentation of RSV antigen, but not ovalbumin, was inhibited by phorbol myristate acetate and filipin, which have been reported to inhibit caveolae, but not by cytochalasin D, amiloride, or mannose. These inhibitors have been reported to block macropinocytosis and other actin-dependent uptake mechanisms, endocytic pathways involving clathrin-coated pits, and the mannose receptor. Furthermore, co-localization of RSV antigen and caveolae was observed by confocal microscopy. Thus, the major route for uptake of RSV antigen by cattle dendritic cells is one mediated by caveolae, adding a pathway of antigen uptake by dendritic cells to those established. J. Leukoc. Biol. 66: 50-58; 1999.

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Section: Discussionmentioning

confidence: 74%

Involvement of caveolae in the uptake of respiratory syncytial virus antigen by dendritic cells

Werling¹,

Hope²,

Chaplin

et al. 1999

Journal of Leukocyte Biology

178

144

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“…Although both are expressed on macrophages (18,35), Endo180 is also found on fibroblasts and chondrocytes, chondrocytes, a subset of endothelial cells, and in tissues undergoing ossification (1, 17, 18, 38 -40), whereas the mannose receptor has been detected on lymphatic and hepatic endothelium, smooth muscle cells, and some epithelia (41)(42)(43)(44). These differences in distribution may reflect accessibility to distinct sets of ligands in vivo.…”

Section: Figmentioning

confidence: 99%

Characterization of Sugar Binding by the Mannose Receptor Family Member, Endo180

East

Rushton²,

Taylor³

et al. 2002

Journal of Biological Chemistry

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Members of the mannose receptor family, the mannose receptor, the phospholipase A 2 receptor, DEC-205, and Endo180, contain multiple C-type lectin-like domains (CTLDs) within a single polypeptide. In addition, at their N termini, all four family members contain a cysteine-rich domain similar to the R-type carbohydrate recognition domains of ricin. However, despite the common presence of multiple lectin-like domains, these four endocytic receptors have divergent ligand binding activities, and it is clear that the majority of these domains do not bind sugars. Here the functions of the lectin-like domains of the most recently discovered family member, Endo180, have been investigated. Endo180 is shown to bind in a Ca 2؉ -dependent manner to mannose, fucose, and N-acetylglucosamine but not to galactose. This activity is mediated by one of the eight CTLDs, CTLD2. Competition assays indicate that the monosaccharide binding specificity of Endo180 CTLD2 is similar to that of mannose receptor CTLD4. However, additional experiments indicate that, unlike the cysteine-rich domain of the mannose receptor, the cysteine-rich domain of Endo180 does not bind sulfated sugars. Thus, although Endo180 and the mannose receptor are now both known to be mannose binding lectins, each receptor is likely to have a distinct set of glycoprotein ligands in vivo.The mannose receptor family comprises the mannose receptor, the M-type phospholipase A 2 receptor, the dendritic cell receptor DEC-205, and Endo180 (also known as uPARAP) (1-3). The four members of the family share a common structural organization. Each receptor is a type I transmembrane receptor with an extracellular region containing an N-terminal cysteinerich domain similar to the galactose-binding domains of ricin, a fibronectin type II (FNII) 1 domain, and either 8 (mannose receptor, phospholipase A 2 receptor, and Endo180) or 10 (DEC-205) C-type lectin-like domains (CTLDs). The short cytoplasmic domain of each receptor mediates internalization of the receptor into the cell and recycling back to the plasma membrane (4 -8). These common features and the fact that the mannose receptor functions in the clearance of glycoproteins, initially suggested that a main function of each of these receptors would be to mediate cellular uptake of glycosylated ligands. However, although each receptor contains multiple lectin-like domains, the majority of these domains do not bind sugars.CTLDs are found in a wide variety of proteins and are characterized by a sequence motif that specifies a conserved fold (9). They were initially described in C-type lectins such as serum mannose-binding protein (MBP-A) and the asialoglycoprotein receptor, which bind sugars in a Ca 2ϩ -dependent manner. However, it has become clear that many of these domains lack the residues required for Ca 2ϩ -dependent sugar binding and are thus predicted to have other functions. The majority of CTLDs within proteins of the mannose receptor family have not conserved the key amino acids required for coordination of Ca 2ϩ ions and...

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“…Therefore, we suggest that this enzyme could participate in airway inflammation and remodeling. β-hex and other mannosyl-rich lysosomal hydrolases are potent mitogens for bovine airway smooth muscle cells [24], and this mitogenic action is mediated via airway smooth muscle mannose-recognizing receptors [25] that have been isolated from bovine airway smooth muscle cells and human bronchial smooth muscle [26]. Lew et al [27] demonstrated that β-hex-induced airway smooth muscle cell proliferation is mediated by activation of p21Ras/MEK/p44/42 MAPK and protein kinase C. β-hex causes activation of p44/42 MAPK that is late in onset (30 min) and sustained for 4 h [27].…”

Section: Discussionmentioning

confidence: 99%

N-Acetyl-Beta-Hexosaminidase Activity in Asthma

Tomasiak

Tomasiak²,

Ziętkowski³

et al. 2008

Int Arch Allergy Immunol

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Background: N-acetyl-β-hexosaminidase (β-hex) is a lysosomal hydrolase, which is selectively secreted into the extracellular space by inflammatory cells. The aim of our study was to assess the activity of β-hex in the plasma of asthmatic patients, and to establish whether it correlates with asthma severity and airway inflammation. Methods: The study was conducted in a group of 46 asthmatic patients and 13 healthy volunteers. All study participants underwent analysis of exhaled nitric oxide and flow-volume spirometry. β-hex activity, peripheral blood eosinophils, total serum IgE and eosinophil cationic protein were analyzed in blood samples from all asthmatic patients and healthy volunteers. Results: β-hex activity was significantly higher in patients with severe or moderate asthma compared with healthy volunteers and was positively correlated with exhaled nitric oxide levels and serum eosinophil cationic protein in these groups of patients. There was no correlation between β-hex activity and forced expiratory volume in 1 s, blood eosinophil count or total serum IgE in these groups of asthmatics. Conclusions: Our results suggest that β-hex could take part in airway inflammation and remodeling in asthma. Our study is the first report in which the elevated activity of β-hex in subjects with asthma has been observed. However, more studies are needed to establish the precise role of this enzyme in asthma in humans.

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A mannose receptor mediates mannosyl-rich glycoprotein-induced mitogenesis in bovine airway smooth muscle cells.

Cited by 60 publications

References 49 publications

Involvement of caveolae in the uptake of respiratory syncytial virus antigen by dendritic cells

Involvement of caveolae in the uptake of respiratory syncytial virus antigen by dendritic cells

Characterization of Sugar Binding by the Mannose Receptor Family Member, Endo180

N-Acetyl-Beta-Hexosaminidase Activity in Asthma

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