Hyaluronan/RHAMM Interactions in Mesenchymal Tumor Pathogenesis

Kouvidi, Katerina; Nikitovic, Dragana; Berdiaki, Aikaterini; Tzanakakis, George N.

doi:10.1016/b978-0-12-800092-2.00012-5

Cited by 34 publications

(31 citation statements)

References 164 publications

(149 reference statements)

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“…Among the most studied receptor proteins are CD44 and receptor for hyaluronan-mediated motility (RHAMM), as they participate in inflammation and cancer motility, migration and metastasis (Slevin et al, 2007; Lokeshwar et al, 2014; Tolg et al, 2014; Misra et al, 2015). Furthermore, both CD44 and RHAMM are associated with the development of stem cell and cancer stem cell (Jiang et al, 2013; Shigeishi et al, 2013; Kouvidi et al, 2014; Jordan et al, 2015). FAK/SRC-mediated ERK activation is involved in signaling event for stem cell development.…”

Section: Ha Receptors and Signalingmentioning

confidence: 99%

HYAL-2–WWOX–SMAD4 Signaling in Cell Death and Anticancer Response

Hsu

Chiang

Sze

et al. 2016

Front. Cell Dev. Biol.

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Hyaluronidase HYAL-2 is a membrane-anchored protein and also localizes, in part, in the lysosome. Recent study from animal models revealed that both HYAL-1 and HYAL-2 are essential for the metabolism of hyaluronan (HA). Hyal-2 deficiency is associated with chronic thrombotic microangiopathy with hemolytic anemia in mice due to over accumulation of high molecular size HA. HYAL-2 is essential for platelet generation. Membrane HYAL-2 degrades HA bound by co-receptor CD44. Also, in a non-canonical signal pathway, HYAL-2 serves as a receptor for transforming growth factor beta (TGF-β) to signal with downstream tumor suppressors WWOX and SMAD4 to control gene transcription. When SMAD4 responsive element is overly driven by the HYAL-2–WWOX–SMAD4 signaling complex, cell death occurs. When rats are subjected to traumatic brain injury, over accumulation of a HYAL-2–WWOX complex occurs in the nucleus to cause neuronal death. HA induces the signaling of HYAL-2–WWOX–SMAD4 and relocation of the signaling complex to the nucleus. If the signaling complex is overexpressed, bubbling cell death occurs in WWOX-expressing cells. In addition, a small synthetic peptide Zfra (zinc finger-like protein that regulates apoptosis) binds membrane HYAL-2 of non-T/non-B spleen HYAL-2+ CD3− CD19− Z lymphocytes and activates the cells to generate memory anticancer response against many types of cancer cells in vivo. Whether the HYAL-2–WWOX–SMAD4 signaling complex is involved is discussed. In this review and opinion article, we have updated the current knowledge of HA, HYAL-2 and WWOX, HYAL-2–WWOX–SMAD4 signaling, bubbling cell death, and Z cell activation for memory anticancer response.

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Section: Ha Receptors and Signalingmentioning

confidence: 99%

HYAL-2–WWOX–SMAD4 Signaling in Cell Death and Anticancer Response

Hsu

Chiang

Sze

et al. 2016

Front. Cell Dev. Biol.

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“…The majority of PGs contain both O ‐ and N ‐type of glycans; however, as the O ‐glycan chain(s), called GAGs are much larger, representing more than a half of the PG MW, the properties and the biological activities of PGs are basically given by GAGs. Due to these carbohydrate chains, often hybrid, PGs are involved in various cellular signaling processes , and interact with many protein enzymes and growth factors (GFs). Minor changes into the fine structure of GAGs, which occur during the physiological process of maturation and aging, may trigger a series of biological events among which also the occurrence of cancer .…”

Section: General Considerations On the Structure And Functions Of Gagsmentioning

confidence: 99%

Applications of capillary electrophoresis electrospray ionization mass spectrometry in glycosaminoglycan analysis

Zamfir

2016

ELECTROPHORESIS

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Proteoglycans (PGs) represent a class of heavily glycosylated proteins distributed in the extracellular matrix, connective tissues, and on the surface of many cell types where, as functional molecules, regulate important biological processes. Structurally, PGs consist of a core protein linked to glycosaminoglycan (GAG) chains, which basically determine the properties and activities of PGs. In view of the structural complexity of GAGs and the existing correlation between this structure and PG functions, systematic efforts are invested into development of analytical methods for GAG characterization. Although less popular and of higher technical difficulty than liquid-based chromatographic methods, CE coupled with ESI MS contributed lately an important progress to glycosaminoglycomics field. In this review article, the most significant CE ESI MS and MS/MS applications in GAG research are highlighted and critically assessed. The advantages and the limitations of each concept as well as the possible further methodological refinements are also concisely discussed. Finally, the review presents the perspectives of CE ESI MS in GAG analysis along with the objectives, which still need to be reached in the near future.

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“…One important characteristic of cancer cells is their ability to express growth factors and growth factor receptors, which contribute to tumor progression [1,2]. Strict regulation of signaling by receptor tyrosine kinases (RTKs) is necessary for biological processes, and its disruption can result in tumor progression [3][4][5].…”

mentioning

confidence: 99%

The E3 ubiquitin ligase Cbl-b inhibits tumor growth in multidrug-resistant gastric and breast cancer cells

Che¹,

Zhang²,

Qu³

et al. 2017

neo

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Most receptor tyrosine kinases (RTKs) contribute to tumor growth, and their ubiquitination and degradation is related to the inhibition of tumor growth. Our previous study showed that the ubiquitin ligase Cbl-b was expressed at low levels in multidrug-resistant (MDR) gastric cancer cells compared with their parental cells. However, whether enhancement of Cbl-b expression in MDR cancer cells could prevent tumor proliferation via ubiquitination and degradation of RTK remains unclear. In the present study, Cbl-b overexpression reduced cell proliferation in MDR gastric and breast cancer cells, and effectively inhibited tumor growth in vivo. Additionally, Cbl-b overexpression reduced the total protein level of insulin-like growth factor 1 (IGF-1R), an important member of the RTK family. Moreover, Cbl-b overexpression promoted interaction of Cbl-b with IGF-1R, and induced ubiquitination and degradation of IGF-1R and inactivation of the IGF-1R pathway. These results suggest that the ubiquitin ligase Cbl-b inhibited tumor growth via ubiquitination and degradation of IGF-1R in MDR gastric and breast cancer cells.

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Hyaluronan/RHAMM Interactions in Mesenchymal Tumor Pathogenesis

Cited by 34 publications

References 164 publications

HYAL-2–WWOX–SMAD4 Signaling in Cell Death and Anticancer Response

HYAL-2–WWOX–SMAD4 Signaling in Cell Death and Anticancer Response

Applications of capillary electrophoresis electrospray ionization mass spectrometry in glycosaminoglycan analysis

The E3 ubiquitin ligase Cbl-b inhibits tumor growth in multidrug-resistant gastric and breast cancer cells

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