Monoclonal antibodies against the human mannose receptor as a specific marker in flow cytometry and immunohistochemistry for macrophages

Noorman, Femke; Braat, E.A.M.; Barrett-Bergshoeff, M.M.; Barbé, Ellis; Leeuwen, A. van; Lindeman, J.; Rijken, D.C.

doi:10.1002/jlb.61.1.63

Cited by 50 publications

(38 citation statements)

References 29 publications

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“…Phagocytosis of unopsonized C. albicans by MØ has been shown to be mediated, to a considerable extent, by the MR; mannan and mannose-BSA inhibited 80% of C. albicans uptake by human monocyte-derived MØ (25) and murine peritoneal MØ. 2 The inhibition of sMR production by the matrix metalloprotease inhibitor BB 2116 strongly suggests a role for a metalloprotease in the release of sMR from the membrane. The matrix metalloproteases are a large family of extracellular zinc proteases, at least 18 distinct members of which have been discovered (28).…”

Section: Discussionmentioning

confidence: 99%

“…1 is a type I integral membrane glycoprotein expressed on many macrophage (MØ) subtypes, monocyte-derived dendritic cells, and hepatic endothelium (1)(2)(3)(4). MR is the founding member of a family of molecules sharing the same basic domain structure: an NH 2 -terminal cysteinerich domain; a fibronectin type II domain; and a variable number of C-type lectin carbohydrate recognition domains (CRDs), eight in the case of MR, followed by a transmembrane domain and a COOH-terminal intracellular domain (5)(6)(7).…”

Section: The Mannose Receptor (Mr)mentioning

confidence: 99%

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A Functional Soluble Form of the Murine Mannose Receptor Is Produced by Macrophages in Vitro and Is Present in Mouse Serum

Martı́nez-Pomares¹,

Mahoney²,

Káposzta³

et al. 1998

Journal of Biological Chemistry

108

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A soluble form of the mannose receptor (sMR) has been found in conditioned medium of primary macrophages in vitro and in mouse serum. sMR was released as a single species, had a smaller size than the cellassociated form, and accumulated in macrophage-conditioned medium, in a cytokine-regulated manner, to levels comparable with those found for cell-associated mannose receptor. Pulse-chase experiments showed that sMR production in culture occurred by constitutive cleavage of pre-existing full-length protein. A binding assay was developed to determine the sugar specificity of sMR and its ability to interact with pathogens and particulate antigens (i.e. Candida albicans and zymosan). Protease inhibitor studies suggested that sMR was produced by cleavage of an intact mannose receptor by a matrix metalloprotease or ADAM metalloprotease. A role for sMR in the immune response is proposed based on its binding properties, regulation by cytokines, and the previous discovery of putative ligands for the cysteine-rich domain of the mannose receptor in lymph nodes and spleen. The mannose receptor (MR)1 is a type I integral membrane glycoprotein expressed on many macrophage (MØ) subtypes, monocyte-derived dendritic cells, and hepatic endothelium (1-4). MR is the founding member of a family of molecules sharing the same basic domain structure: an NH 2 -terminal cysteinerich domain; a fibronectin type II domain; and a variable number of C-type lectin carbohydrate recognition domains (CRDs), eight in the case of MR, followed by a transmembrane domain and a COOH-terminal intracellular domain (5-7). The other members of the family are: (i) the phospholipase A 2 receptor, which contains eight CRDs and is widely distributed (8 -10); (ii) the receptor DEC-205, which contains 10 CRDs and is expressed mostly by dendritic cells in T-cell areas of secondary lymphoid organs and by thymic and intestinal epithelia (11-13); and (iii) a recently described molecule found by its homology to the C-type lectin domain of E-selectin (14).Mannosylated molecules and particles can be endocytosed and phagocytosed through their interaction with the MR (3, 4, 15-19). The domains likely to be involved in this process are the CRDs and the transmembrane and the COOH-terminal intracellular domains. Neither the cysteine-rich domain nor the fibronectin type II domain seems to be required (18,20). MR synthesis and function are regulated by MØ maturation, lipopolysaccharide (LPS) (3), and cytokines; inhibited by interferon (IFN)-␥ (6); and up-regulated by 22).Using as a probe a chimeric protein containing the cysteinerich domain of the MR fused to the Fc region of human IgG1 (CR-Fc), we found putative ligand(s) for this domain of the MR in marginal zone metallophilic and subcapsular sinus MØ in naive mice and in the germinal centers of immunized mice. CR-Fc ϩ cells with dendritic morphology migrated toward the follicular areas and paracortex of lymph nodes during a secondary immune response (23). We hypothesized a role for a soluble form of the MR in the transport...

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Section: Discussionmentioning

confidence: 99%

Section: The Mannose Receptor (Mr)mentioning

confidence: 99%

A Functional Soluble Form of the Murine Mannose Receptor Is Produced by Macrophages in Vitro and Is Present in Mouse Serum

Martı́nez-Pomares¹,

Mahoney²,

Káposzta³

et al. 1998

Journal of Biological Chemistry

108

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“…Finally, based on the number of cells in involuting tissue that express macrophage mannose receptor and IL-13, a marker for M2 macrophages in humans and an M2-associated cytokine, we conclude that macrophages with an M2 phenotype are abundant in the human involuting mammary gland ( Figure 3H, arrows). 26,27,62 The breast tissues used for these studies were obtained from women who were subsequently diagnosed with cancer or found to be without evidence of malignancy. It might be anticipated that normal adjacent human breast tissue taken from the women with breast cancer would have higher levels of M2 macrophages present throughout the gland and, further, that these cases account for the higher levels of immune cells observed in the involuting human breast tissues depicted in Figure 3, D and E. First, in an attempt to minimize this confounder, lobules were taken from areas of the breast specimens that were morphologically normal but distinct from the tumor.…”

Section: Human Breast Involutionmentioning

confidence: 99%

Alternatively Activated Macrophages and Collagen Remodeling Characterize the Postpartum Involuting Mammary Gland across Species

O’Brien

Lyons

Monks

et al. 2010

The American Journal of Pathology

257

300

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Recent pregnancy correlates with decreased survival for breast cancer patients compared with non-pregnancy-associated breast cancer. We hypothesize that postpartum mammary involution induces metastasis through wound-healing programs known to promote cancer. It is unknown whether alternatively activated M2 macrophages , immune cells important in woundhealing and experimental tumorigenesis that also predict poor prognosis for breast cancer patients, are recruited to the normal involuting gland. Macrophage markers CD68 , CSF-1R , and F4/80 were examined across the pregnancy and involution cycle in rodent and human mammary tissues. Quantitative immunohistochemistry revealed up to an eightfold increase in macrophage number during involution , which returned to nulliparous levels with full regression. The involution macrophages exhibit an M2 phenotype as determined by high arginase-1 and low inducible nitric oxide synthase staining in rodent tissue , and by mannose receptor expression in human breast tissue. M2 cytokines IL-4 and IL-13 also peaked during involution. Extracellular matrix (ECM) isolated from involuting rat mammary glands was chemotactic for macrophages compared with nulliparous mammary ECM. Although it is recognized that full-term pregnancy at an early age reduces the lifetime risk of developing breast cancer, women of all ages have a transient increase in breast cancer risk with a recent pregnancy.1-4 Breast cancers diagnosed up to five years out from a completed pregnancy have been referred to as pregnancy-associated or PABC. 5,6 Several studies have shown that PABC frequently metastasizes, resulting in poor prognosis for the patient.6 -8 Epidemiological data identify women whose breast cancer is diagnosed postpartum, rather than during pregnancy, as having the worst outcomes.7-14 Further, when breast cancer patients were matched for known prognostic indicators, the postpartum window proved to be an independent factor for metastasis, whereas a diagnosis during pregnancy did not. 11,14,15 We have proposed the involution-hypothesis to account for the high metastatic oc-

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“…The expression of MR is primarily restricted to tissue macrophages, myeloid DCs, and hepatic endothelial cells (33)(34)(35)(36), and as such makes an attractive candidate for targeting Ags to APCs. We generated a human anti-MR mAb, B11, by immunization of human Ig-expressing mice with immature human DCs, followed by standard hybridoma methodology.…”

Section: Characterization Of Anti-mr Mab B11mentioning

confidence: 99%

Mannose Receptor Targeting of Tumor Antigen pmel17 to Human Dendritic Cells Directs Anti-Melanoma T Cell Responses via Multiple HLA Molecules

Ramakrishna¹,

Treml²,

Vitale³

et al. 2004

The Journal of Immunology

107

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Targeting recycling endocytic receptors with specific Abs provides a means for introducing a variety of tumor-associated Ags into human dendritic cells (DCs), culminating in their efficient presentation to T cells. We have generated a human mAb (B11) against the mannose receptor that is rapidly internalized by DCs through receptor-mediated endocytosis. By genetically linking the melanoma Ag, pmel17, to Ab B11, we obtained the fully human fusion protein, B11-pmel17. Treatment of DCs with B11-pmel17 resulted in the presentation of pmel17 in the context of HLA class I and class II molecules. Thus, potent pmel17-specific T cells were cytotoxic toward gp100+ HLA-matched melanoma targets, but not HLA-mismatched melanoma or gp100− nonmelanoma tumor lines. Importantly, competitive inhibition of lysis of an otherwise susceptible melanoma cell line by cold targets pulsed with known gp100 CD8 T cell epitopes as well as a dose-dependent proliferative response to Th epitopes demonstrates that DCs can process targeted Ag for activation of cytotoxic as well as helper arms of the immune response. Thus, the specific targeting of soluble exogenous tumor Ag to the DC mannose receptor directly contributes to the generation of multiple HLA-restricted Ag-specific T cell responses.

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Monoclonal antibodies against the human mannose receptor as a specific marker in flow cytometry and immunohistochemistry for macrophages

Abstract: Abstract:Recently we developed mouse monoclonal antibodies (inAb) against the isolated human 175-kDa mannose receptor.

Cited by 50 publications

References 29 publications

A Functional Soluble Form of the Murine Mannose Receptor Is Produced by Macrophages in Vitro and Is Present in Mouse Serum

A Functional Soluble Form of the Murine Mannose Receptor Is Produced by Macrophages in Vitro and Is Present in Mouse Serum

Alternatively Activated Macrophages and Collagen Remodeling Characterize the Postpartum Involuting Mammary Gland across Species

Mannose Receptor Targeting of Tumor Antigen pmel17 to Human Dendritic Cells Directs Anti-Melanoma T Cell Responses via Multiple HLA Molecules

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