Multiple interactions between pituitary hormones and the mannose receptor

Simpson, Daniel Z.; Hitchen, Paul G.; Elmhirst, Elizabeth L.; Taylor, Maureen E.

doi:10.1042/bj3430403

Cited by 33 publications

(5 citation statements)

References 21 publications

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“…All solutions were filtered using a 0.22 µm of polytetrafluoroethylene membrane syringe filter and degassed prior use. Extracellular soluble fragments (MMR1-8) of the human MR (37)(38)(39) and of the human DC-SIGN (8) were immobilized on a CM5 sensor chip. The fragment of MR (MMR1-8) contains all the domains necessary for Ca 2+ -dependent binding of mannose, N-acetylglucosamine, and fucose-terminated glycoconjugates and binds such ligands as the whole receptor does.…”

Section: Methodsmentioning

confidence: 99%

Synthesis of Glycocluster−Tumor Antigenic Peptide Conjugates for Dendritic Cell Targeting

et al. 2007

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The use of dendritic cells (DC) for the development of therapeutic cancer vaccines is attractive because of their unique ability to present tumor epitopes via the MHC class I pathway to induce cytotoxic CD8+ T lymphocyte responses. C-Type membrane lectins, DC-SIGN and the mannose receptor (MR), present on the DC surface, recognize oligosaccharides containing mannose and/or fucose and mediate sugar-specific endocytosis of synthetic oligolysine-based glycoclusters. We therefore asked whether a glycotargeting approach could be used to induce uptake and presentation of tumor antigens by DC. To this end, we designed and synthesized glycocluster conjugates containing a CD8+ epitope of the Melan-A/Mart-1 melanoma antigen. These glycocluster-Melan-A conjugates were obtained by coupling glycosynthons: oligosaccharyl-pyroglutamyl-beta-alanine derivatives containing either disaccharides, a dimannoside (Manalpha-6Man) or lactoside, or a Lewis oligosaccharide, to Melan-A 16-40 peptide comprising the 26-35 HLA-A2 restricted T cell epitope, extended with an oligolysine stretch at the C-terminal end. We showed by confocal microscopy and flow cytometry that fluorescent-labeled Melan-A glycoclusters containing either dimannoside or Lewis oligosaccharide were taken up by DC and concentrated in acidic vesicles; conversely lactoside glycopeptides were not at all taken up. Furthermore, using surface plasmon resonance, we showed that dimannoside and Lewis-Melan-A conjugates bind MR and DC-SIGN with high affinity. DC loaded with these conjugates, but not with the lactose-Melan-A conjugate, led to an efficient presentation of the Melan-A epitope eliciting a CD8+ T-lymphocyte response. These data suggest that synthetically designed glycocluster-tumor antigen conjugates may induce antigen cross-presentation by DC and represent a promising tool for the development of tumor vaccines.

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Section: Methodsmentioning

confidence: 99%

Synthesis of Glycocluster−Tumor Antigenic Peptide Conjugates for Dendritic Cell Targeting

et al. 2007

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“…LH is a ligand for both the CTLD and CR domain of the MR and it is thought that both regions of the molecule cooperate in its recognition [39]. The specificity of its clearance is said to result from selective multimerization of the receptor in the liver, however, no mechanism has been proposed [40].…”

Section: Cytoplasmic Tailmentioning

confidence: 99%

The mannose receptor: linking homeostasis and immunity through sugar recognition

Taylor¹,

Gordon²,

Martı́nez-Pomares³

2005

Trends in Immunology

299

253

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“…Expression and purification of the whole extracellular region of the human macrophage mannose receptor (MMR-S), and the portion consisting of the eight CRDs (MMR1-8) have been described previously [31,32]. For gelatin-binding experiments, MMR-S and MMR1-8 samples were used at concentrations of 0.15 mg/ml and 0.2 mg/ml respectively.…”

Section: Binding Of Mannose Receptor Fragments To Gelatinmentioning

confidence: 99%

Collagen binding by the mannose receptor mediated through the fibronectin type II domain

Napper

Drickamer

Taylor

2006

Biochemical Journal

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The macrophage mannose receptor is the prototype for a family of receptors each having an extracellular region consisting of an N-terminal cysteine-rich domain related to the R-type carbohydrate-recognition domain of ricin, a fibronectin type II domain and eight to ten domains related to C-type carbohydrate-recognition domains. The mannose receptor acts as a molecular scavenger, clearing harmful glycoconjugates or micro-organisms through recognition of their defining carbohydrate structures. Cell-adhesion assays, as well as collagen-binding assays, have now been used to show that the mannose receptor can also bind collagen and that the fibronectin type II domain mediates this activity. Neither of the two types of sugar-binding domain in the receptor is involved in collagen binding. Fibroblasts expressing the mannose receptor adhere to type I, type III and type IV collagens, but not to type V collagen, and the adherence is inhibited by isolated mannose receptor fibronectin type II domain. The fibronectin type II domain shows the same specificity for collagen as the whole receptor, binding to type I, type III and type IV collagens. This is the first activity assigned to the fibronectin type II domain of the mannose receptor. The results suggest additional roles for this multifunctional receptor in mediating collagen clearance or cell-matrix adhesion.

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Multiple interactions between pituitary hormones and the mannose receptor

Cited by 33 publications

References 21 publications

Synthesis of Glycocluster−Tumor Antigenic Peptide Conjugates for Dendritic Cell Targeting

Synthesis of Glycocluster−Tumor Antigenic Peptide Conjugates for Dendritic Cell Targeting

The mannose receptor: linking homeostasis and immunity through sugar recognition

Collagen binding by the mannose receptor mediated through the fibronectin type II domain

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