Gene interactions and pathways from curated databases and text-mining

◀ Back to EPHB2

CD44 — EPHB2

Text-mined interactions from Literome

Kobayashi et al., Int J Cancer 2002 (Bone Neoplasms...) : Our study indicates that ( i ) CD44 stimulation by fragmented HA upregulates expression of uPA and uPAR mRNA and protein but does not affect MMPs secretion or PAI-1 mRNA expression ; ( ii ) the effects of HA fragments are critically HA size dependent : high molecular weight HA is inactive, but lower molecular weight fragmented HA ( Mr 3.5 kDa ) is active ; ( iii ) cells can bind avidly Mr 3.5 kDa fragmented HA through a CD44 molecule, whereas cells do not effectively bind higher Mr HA ; ( iv ) a fragmented HA induces phosphorylation of MAP kinase proteins ( MEK1/2, ERK1/2 and c-Jun ) within 30 min ; ( v ) CD44 is critical for the response ( activation of MAP kinase and upregulation of uPA and uPAR expression ) ; and ( vi ) cell invasion induced by CD44 stimulation with a fragmented HA is inhibited by anti-CD44 mAb, MAP kinase inhibitors, neutralizing anti-uPAR pAb, anti-catalytic anti-uPA mAb or amiloride
Bourguignon et al., J Biol Chem 2005 (Disease Progression...) : In addition, the binding of HA to CD44 promoted the association of ERK2 with the IQGAP1 molecule, which stimulated both ERK2 phosphorylation and kinase activity
Marhaba et al., Cell Signal 2005 (MAP Kinase Signaling System...) : In the absence of any stimulus, ERK1/2 was partly phosphorylated, and phosphorylation was significantly increased by CD44v6 cross linking ... Instead, CD44s cross linking induced ERK1/2 , JNK, c-jun, and IkappaBalpha phosphorylation only in the context of TCR engagement
Shi et al., Immunity 2006 : CD74 alone mediated MIF binding ; however, MIF induced ERK1 and ERK2 kinase phosphorylation required the coexpression of full-length CD44 ... Investigations that used siRNA or kinase inhibitors indicate that MIF induced ERK1 and ERK2 activation through CD44 required the Src tyrosine kinase
Tolg et al., J Cell Biol 2006 : Rhamm-/- fibroblasts are defective in CD44 mediated ERK1,2 motogenic signaling, leading to defective skin wound repair
Kim et al., Mol Immunol 2008 (Dermatitis, Allergic Contact...) : CD44 mediated effect of antigen on phosphorylation of ERK , p38MAPK, ROS production, secretion of beta-hexosaminidase, and histamine release
Suwan et al., J Biol Chem 2009 : These results demonstrate that versican is essential for matrix assembly involving hyaluronan and that diminished versican deposition increases free hyaluronan fragments that interact with CD44 and increase phosphorylation of ERK1/2 , leading to cellular senescence
Hatano et al., Lab Invest 2011 (Fibroma, Ossifying) : The results raise the novel idea that the EGFR may activate Raf-MEK-ERK signaling in response to the binding of HA to CD44
Xie et al., PloS one 2011 (MAP Kinase Signaling System) : It was reported that MIF induced rapid ERK activation requires its co-receptor CD44