Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily

Kelm, Sørge; Pelz, Andrea; Schauer, Roland; Filbin, Marie T.; Tang, Song; Bellard, María Elena de; Schnaar, Ronald L.; Mahoney, James A.; Hartnell, Adele; Bradfield, Paul F.; Crocker, Paul R.

doi:10.1016/s0960-9822(00)00220-7

Cited by 388 publications

(354 citation statements)

References 44 publications

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“…Therefore, CD22 is regarded as a member of the sialoadhesin or SigLec subclass of the Ig superfamily, characterized by functioning as lectins (Engel et al, 1993;Kelm et al, 1994). Additional molecules in this class include other sialic acid-binding receptors, such as sialoadhesin and CD33.…”

Section: Cd22 As a Target For Immunotherapy In B-cell Malignanciesmentioning

confidence: 99%

Preclinical and clinical evaluation of epratuzumab (anti-CD22 IgG) in B-cell malignancies

Leonard

Goldenberg

2007

Oncogene

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The vast majority of non-Hodgkin's lymphomas are of B-cell phenotype. Development of unlabeled or radiolabeled therapeutic monoclonal antibodies against the cell surface antigen, CD20, has revolutionized the treatment of these malignancies. It is clear that antibodies targeting other B-cell-specific molecules, such as CD22, also offer potential therapeutic benefit. Epratuzumab is a humanized anti-CD22 monoclonal, which has undergone preclinical and phase I/II clinical evaluation in patients with indolent or aggressive lymphoma. Data suggest that this agent is well tolerated, and can induce tumor regressions. Trials are currently evaluating its safety and activity in combination with rituximab (chimeric anti-CD20) and standard chemotherapy are ongoing. Initial results suggest that these regimens have acceptable toxicity, and that epratuzumab warrants further evaluation as an adjunct to standard lymphoma treatment regimens.

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Section: Cd22 As a Target For Immunotherapy In B-cell Malignanciesmentioning

confidence: 99%

Preclinical and clinical evaluation of epratuzumab (anti-CD22 IgG) in B-cell malignancies

Leonard

Goldenberg

2007

Oncogene

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“…mAb against CCR3 (83101.111, PE) was from R&D systems (Minneapolis, MN). Affinity-purified polyclonal rabbit anti-mouse CD22 IgG [30] and sheep anti-hSiglec-5 IgG were prepared in our own lab. PE-conjugated CD1d/ § -GalCer tetramers [22] or PEconjugated unloaded CD1d as a control for the specificity of tetramer staining [22] were kindly provided by K. Hammond and M. Kronenberg (La Jolla Institute for Allergy & Immunology, CA).…”

Section: Reagents and Abmentioning

confidence: 99%

“…The resultant pDEFmSiglec-E-3c-Fc was transfected into Chinese hamster ovary K1 cells by electroporation, and hygromycin-resistant clones were selected. mSiglec-E-Fc fusion protein was then purified with protein A Sepharose [30] and coupled to cyanogen bromide pre-activated Sepharose CL-4B (Amersham Pharmacia Biotech) at a density of 3 mg/ml wet beads.…”

Section: Production Of Fc Fusion Proteinsmentioning

confidence: 99%

The murine inhibitory receptor mSiglec‐E is expressed broadly on cells of the innate immune system whereas mSiglec‐F is restricted to eosinophils

et al. 2004

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Murine (m) Siglec-E and mSiglec-F are recently discovered murine sialic acid-binding Ig-like lectins with tyrosine-based inhibitory signaling motifs. They are postulated to be the orthologs of human (h) siglec-7, -8 or -9 and siglec-5, respectively. We report here the first detailed characterization of mSiglec-E, and compare its expression pattern with mSiglec-F. Similar to hSiglec-7, mSiglec-E preferred § 2-8-linked disialic acid over § 2-3-and § 2-6-linked sialic acids. Using a specific Ab, FACS analysis demonstrated that mSiglec-E was expressed mainly on neutrophils in blood and their immature precursors in bone marrow. mSiglec-E was present on peritoneal cavity macrophages and on subsets of mature NK cells and splenic dendritic cells. mSiglec-E was also found on a novel population of peritoneal cavity B-1a-like cells and a subset of splenic B cells enriched in transitional T2 and marginal zone B cells. In striking contrast to mSiglec-E, mSiglec-F was expressed predominantly on eosinophils in blood and their precursors in the bone marrow. The distinct and largely nonoverlapping expression profiles of mSiglec-E and mSiglec-F suggest that they play nonredundant roles in the innate immune system. mSiglec-E is likely to modulate the functions of several types of effector cells, whereas mSiglec-F is likely to be more restricted to eosinophil biology.

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“…The immunoglobulin domains are arranged in a linear array made up of 16 C2-set domains and one N-terminal, membrane distal, V-set domain. Sn is most closely related in sequence in its N-terminal two domains to the myelin-associated glycoprotein (MAG), CD22, and CD33, and, with these, it forms the sialoadhesin family, a subgroup of the IgSF involved in the recognition of specific sialylated glycans (Kelm et al, 1994a;Freeman et al, 1995). It has been shown by domain deletion experiments that the membrane distal N-terminal domain is both necessary and sufficient to mediate sialic acid-dependent adhesion (Nath et al, 1995).…”

mentioning

confidence: 99%

“…Structural studies on both rat and human CD2 (Jones et al, 1992;Bodian et al, 1994) have provided information on the adhesive interactions between IgSF domains; studies on VCAM-I (Jones et al, 1995) gave insight into IgSF/integrin adhesion. It is hoped that the structural analysis of this fragment of Sn will lead to information on the details of IgSF/carbohydrate interactions and their role in intercellular adhesion, and provide a template for studying other members of the recently characterized sialoadhesin family (Kelm et al, 1994a;Freeman et al, 1995). The structure of the N-terminal domain of sialoadhesin will be the first of a new class of carbohydrate-binding proteins.…”

mentioning

confidence: 99%

Expression, crystallization, and preliminary X-ray analysis of a sialic acid-binding fragment of sialoadhesin in the presence and absence of ligand

et al. 1997

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Abstract:Sialoadhesin is a macrophage-restricted cell surface receptor, consisting of 17 immunoglobulin domains, which mediates cell adhesion via the recognition of specific sialylated glycoconjugates. A functional fragment of sialoadhesin, comprising the N-terminal immunoglobulin domain, has been expressed in Chinese hamster ovary cells as both native (SnDI) and selenomethionyl (Se-SnD1) stop protein. The successful production of 86% selenomethionine-incorporated protein represents a rare example of production of selenium-labeled protein in mammalian cells. SnD 1 and Se-SnD 1 have been crystallized in the absence of ligand, and SnDl has also been crystallized in the presence of its ligand 2,3 sialyllactose. The ligand-free crystals of SnDl and Se-SnDI were isomorphous, of space group P3121 or P3221, with unit cell dimensions a = b = 38.9 A, c = 152.6 A, LY = p = 90°, y = 120°, and diffracted to a maximum resolution of 2.6 8. Cocrystals containing 2,3 sialyllactose diffracted to 1.85 A at a synchrotron source and belong to space group P212121, with unit cell dimensions a = 40.9 A, b = 97.6 A, c = 101.6 A, LY = p = y = 90".Keywords: cell adhesion; complex; crystallization; lectin; selenomethionine; sialic acid Sialoadhesin is a cell surface receptor that mediates cellular interactions by recognizing specific sialylated glycans in cell surface

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Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily

Cited by 388 publications

References 44 publications

Preclinical and clinical evaluation of epratuzumab (anti-CD22 IgG) in B-cell malignancies

Preclinical and clinical evaluation of epratuzumab (anti-CD22 IgG) in B-cell malignancies

The murine inhibitory receptor mSiglec‐E is expressed broadly on cells of the innate immune system whereas mSiglec‐F is restricted to eosinophils

Expression, crystallization, and preliminary X-ray analysis of a sialic acid-binding fragment of sialoadhesin in the presence and absence of ligand

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