ArticleThe Journal of biological chemistry2014
Serglycin proteoglycan is required for multiple myeloma cell adhesion, in vivo growth, and vascularization.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Multiomics analysis and prognostic modeling reveal the molecular features and potential therapeutic targets of breast cancer brain metastasis.Clinical and experimental medicine · 2025Article
- Matrix: a complex amalgam of structures and functions in tumor microenvironment.FEBS open bio · 2025Review
- Proteoglycans and glycosaminoglycans: critical regulators in angiogenesis, vasculogenesis, and vascularized tissue engineering.Angiogenesis · 2025Review
- A translational perspective of the malignant hematopoietic proteoglycome.Cell & bioscience · 2025Review
- Article
- M6PR- and EphB4-Rich Exosomes Secreted by Serglycin-Overexpressing Esophageal Cancer Cells Promote Cancer Progression.International journal of biological sciences · 2023Article
- Highly expressed genes in multiple myeloma cells - what can they tell us about the disease?European journal of haematology · 2022Article
- The extracellular matrix of hematopoietic stem cell niches.Advanced drug delivery reviews · 2022Review
- Proteoglycans and their functions in esophageal squamous cell carcinoma.World journal of clinical oncology · 2021Review
- Cancer-associated fibroblasts secrete hypoxia-induced serglycin to promote head and neck squamous cell carcinoma tumor cell growth in vitro and in vivo by activating the Wnt/β-catenin pathway.Cellular oncology (Dordrecht, Netherlands) · 2021Article
- Serglycin activates pro-tumorigenic signaling and controls glioblastoma cell stemness, differentiation and invasive potential.Matrix biology plus · 2020Article
- Identification of Common Differentially Expressed Genes and Potential Therapeutic Targets in Ulcerative Colitis and Rheumatoid Arthritis.Frontiers in genetics · 2020Article
- SRGN crosstalks with YAP to maintain chemoresistance and stemness in breast cancer cells by modulating HDAC2 expression.Theranostics · 2020Article
- The dual role of the glycosaminoglycan chondroitin-6-sulfate in the development, progression and metastasis of cancer.The FEBS journal · 2019Review
- Multiple Myeloma: What Do We Do About Immunodeficiency?Journal of Cancer · 2019Review
- Multiple Roles of Glycans in Hematological Malignancies.Frontiers in oncology · 2018Review
- Proteoglycans-Biomarkers and Targets in Cancer Therapy.Frontiers in endocrinology · 2018Review
- Chondroitin sulfate proteoglycan serglycin influences protein cargo loading and functions of tumor-derived exosomes.Oncotarget · 2017Article
- Extracellular matrix and the myeloid-in-myeloma compartment: balancing tolerogenic and immunogenic inflammation in the myeloma niche.Journal of leukocyte biology · 2017Review
- Serglycin in tumor microenvironment promotes non-small cell lung cancer aggressiveness in a CD44-dependent manner.Oncogene · 2017Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Recently, it was discovered that serglycin, a hematopoietic cell proteoglycan, is the major proteoglycan expressed and constitutively secreted by multiple myeloma (MM) cells. High levels of serglycin are present in the bone marrow aspirates of at least 30% of newly diagnosed MM patients. However, its contribution to the pathophysiology of MM is unknown. Here, we show that serglycin knockdown (by ∼85% compared with normal levels), using lentiviral shRNA, dramatically attenuated MM tumor growth in mice with severe combined immunodeficiency. Tumors formed from cells deficient in serglycin exhibited diminished levels of hepatocyte growth factor expression and impaired development of blood vessels, indicating that serglycin may affect tumor angiogenesis. Furthermore, knockdown of serglycin significantly decreased MM cell adhesion to bone marrow stromal cells and collagen I. Even though serglycin proteoglycan does not have a transmembrane domain, flow cytometry showed that serglycin is present on the MM cell surface, and attachment to the cell surface is, at least in part, dependent on its chondroitin sulfate side chains. Co-precipitation of serglycin from conditioned medium of MM cells using a CD44-Fc chimera suggests that CD44 is the cell surface-binding partner for serglycin, which therefore may serve as a major ligand for CD44 at various stages during myeloma progression. Finally, we demonstrate that serglycin mRNA expression in MM cells is up-regulated by activin, a predominant cytokine among those increased in MM patients with osteolytic lesions. These studies provide direct evidence for a critical role for serglycin in MM pathogenesis and show that targeting serglycin may provide a novel therapeutic approach for MM.
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Registered trials
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