IndraLab

Statements

CD44 binds ADAM10. 14 / 15
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"A detailed analysis of CD8 + T cell-targeting interactions, filtered for cases in which either the ligands, the receptors, or both were differentially expressed, revealed similar patterns for classical interactions, such as HLA-A:CD8A , which is relevant for antigen recognition, and the ADAM10:CD44 interaction, which is relevant for receptor shedding."
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"To further validate these findings, we examined the potential of a physical interaction between CD44 and ADAM10 using co-immunoprecipitation."
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"In addition, we showed that simvastatin inhibited the generation of the mature form of ADAM10, ADAM10 activity as well as the interaction of CD44 and ADAM10.We demonstrated by co-immunoprecipitation a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In addition, simvastatin mediated inhibition of cholesterol biosynthesis and the dissolution of lipid rafts is likely responsible for preventing interactions between CD44 and ADAM10, thereby blocking [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Second, simvastatin inhibits the interaction between CD44 and ADAM10 due to a decrease in the proportion of CD44 existing in lipid raft.CD44 cleavage occurs in a variety of tissues and is mediated by [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"GPNMB in TME is mainly expressed by TAMs, can be cleaved into a soluble form by ADAM10 which then binds to CD44 receptor in cancer cells to induce release several chemokines (CXCL1, CXCL2, CCL2, CCL5 and CCL7) as well as cytokines (IL-6, IL-11, and IL-33) [26]."
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"In particular, the interaction between ADAM10 and CD44 facilitated the communication between CSCs and T cells ( xref , xref ) [ xref , xref ]."
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"ADAM10 interacts with CD44 and PrPc and promotes their nuclear transportation."
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"Together, these data show that ADAM10 interacts with CD44 and PrPc, and initiates CD44 and PrPc intramembrane proteolysis followed by nuclear transport and signaling of the cytoplasmic domain."
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"In TNBC cells, we find that ADAM10 interacts with CD44 and PrPc and initiates their intramembrane proteolysis followed by nuclear transport and signaling of the cytoplasmic domain."
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"To further validate these findings, we examined the potential of a physical interaction between CD44 and ADAM10 using co-immunoprecipitation."
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"In addition, simvastatin-mediated inhibition of cholesterol biosynthesis and the dissolution of lipid rafts is likely responsible for preventing interactions between CD44 and ADAM10, thereby blocking [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Second, simvastatin inhibits the interaction between CD44 and ADAM10 due to a decrease in the proportion of CD44 existing in lipid raft."
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"We demonstrated by co-immunoprecipitation analysis that the ADAM10 associated with CD44 in control, untreated chondrocytes was predominately the 90 kD immature isoform whereas following IL-1β + OSM tr[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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