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, and I
B Kinases 1 and 2 Are Downstream Effectors of CD44 During the Activation of NF-B by Hyaluronic Acid Fragments in T-24 Carcinoma Cells1
Department of Biochemistry and Biotechnology Institute, Trinity College, Dublin, Ireland
We have investigated the ability of hyaluronic acid (HA) fragments
to activate the transcription factor NF-
B. HA fragments activated
NF-B in the cell lines T-24, HeLa, MCF7, and J774. Further studies
in T-24 cells demonstrated that HA fragments also induced IB
phosphorylation and degradation, B-linked reporter gene expression,
and ICAM-1 promoter activity in an NF-B-dependent manner. The effect
of HA was size dependent as neither disaccharide nor native HA were
active. CD44, the principal cellular receptor for HA, was critical for
the response because the anti-CD44 Ab IM7.8.1 blocked the effect on
NF-B. HA fragments activated the IB kinase complex, and the
effect on a B-linked reporter gene was blocked in T-24 cells
expressing dominant negative IB kinases 1 or 2. Activation of
protein kinase C (PKC) was required because calphostin C inhibited
NF-B activation and IB phosphorylation. In particular, PKC
was required because transfection of cells with dominant negative
PKC blocked the effect of HA fragments on B-linked gene
expression and HA fragments increased PKC activity. Furthermore,
damnacanthal and manumycin A, two mechanistically distinct inhibitors
of Ras, blocked NF-B activation. Transfection of T-24 cells with
dominant negative Ras (RasN17) blocked HA fragment-induced B-linked
reporter gene expression, and HA fragments activated Ras activity
within 5 min. Taken together, these studies establish a novel signal
transduction cascade eminating from CD44 to Ras, PKC, and IB
kinase 1 and 2.
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