Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 19454271Publication DOI: 10.1016/j.yexmp.2009.01.006Journal NLM ID: 0370711Publisher: Amsteram: Elsevier
Correspondence: jun.yan
louisville.edu
Institutions: Tumor Immunobiology Program, James Graham Brown Cancer Center, Louisville, USA, Department of Microbiology and Immunology, Louisville, USA, Department of Medicine, University of Louisville, Louisville, USA
Beta-glucan is an immuno-stimulating agent that has been used to treat cancer and infectious disease for many years with varying and unpredictable efficacy. Recent studies have unraveled the action mode of yeast-derived β-glucan in combination with anti-tumor monoclonal antibodies (mAbs) in cancer therapy. It has demonstrated that particulate or large molecular weight soluble β-glucans are ingested and processed by macrophages. These macrophages secrete the active moiety that primes neutrophil complement receptor 3 (CR3) to kill iC3b-opsonized tumor cells. In vitro and in vivo data demonstrate that successful combination therapy requires complement activation and deposition on tumors and CR3 expression on granulocytes. Pre-clinical animal studies have demonstrated the efficacy of combined β-glucan with anti-tumor mAb therapy in terms of tumor regression and long-term survival. Clinical trials are underway using anti-epidermal growth factor receptor mAb (cetuximab) in combination with β-glucan for metastatic colorectal cancer. This review provides a brief overview of this combination therapy in cancer and describes in detail the β-glucan composition and structure, mechanism of action, and preclinical studies in human carcinoma xenograft models. It is proposed that the addition of β-glucan will further improve the therapeutic efficacy of anti-tumor mAbs in cancer patients.
complement, β-glucan, Neutrophils, Immunotherapy, anti-tumor monoclonal antibody, complement regulatory proteins
Structure type: fragment of a bigger structure
Location inside paper: p.209
Trivial name: glucan particle, PFLP
Compound class: cell wall polysaccharide, glucan
Contained glycoepitopes: IEDB_1397514,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_2278476,IEDB_2278477,IEDB_558869,IEDB_857743,IEDB_983931,SB_192
Biological activity: blastoconidia is phagocytosed by neutrophils once CR3 binds β-glucan on the yeast surface; on the larger hyphae, β-glucan recognition does not result in phagosytosis because of the large size of this form; when the hyphae predominates, β-glucan is bound by neutrophils and respiratory burst follows
Comments, role: backbone structure with bDGlcp(1,6)-linked side chains
Related record ID(s): 40030, 43662
NCBI Taxonomy refs (TaxIDs): 5476Reference(s) to other database(s): GTC:G51056AN
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error