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Originally published In Press as doi:10.1074/jbc.R100038200 on November 20, 2001
J. Biol. Chem., Vol. 277, Issue 7, 4589-4592, February 15, 2002
MINIREVIEW
Signaling Properties of Hyaluronan Receptors*
Eva A.
Turley §,
Paul W.
Noble¶, and
Lilly Y. W.
Bourguignon
From the London Regional Cancer Center,
University of Western Ontario, London N6A 4L6, Canada,
¶ Pulmonary and Critical Care Section, Yale University School
of Medicine, New Haven, Connecticut 06520-8057, and Department
of Medicine, University of California and San Francisco Veterans
Affairs Medical Center, San Francisco, California 94121
 |
INTRODUCTION |
In 1979, hyaluronan was demonstrated to bind
specifically and with high affinity to intact cells (1), and in 1980, it was shown to enhance cell motility on two-dimensional culture
surfaces where the hydrodynamic properties of hyaluronan were not
necessary to open spaces for cells to move into (2). These two
demonstrations raised the possibility that hyaluronan had the potential
to directly modify cell behavior. In 1989, hyaluronan was shown to
promote protein tyrosine phosphorylation cascades (3) that were later proven to be required for hyaluronan-mediated motility on planar culture surfaces (4). Since then, small amounts (nanograms) of
hyaluronan have been shown to activate a variety of protein tyrosine
and serine/threonine kinases. These include the non-receptor protein
tyrosine kinase Src (5, 6), HER2/Neu receptor (7), focal adhesion kinase (4, 8-10), protein kinase C (11, 12), and
MAP1 kinases (9, 10). Likely
as a consequence of regulating these kinases, hyaluronan promotes
expression of specific cytokines and proteins involved in extracellular
matrix remodeling (e.g. Ref. 13).
The study of murine cardiac cells derived from hyaluronan synthase 2 (HAS2) knockout mice has provided the most convincing evidence for a
signaling capability of hyaluronan (14). HAS2 / cardiac cells do not
undergo an endothelial-mesenchymal transformation associated with
migration from tissue explants whereas wild-type cells do (14).
However, the addition of nanogram amounts of exogenous hyaluronan
"rescues" knockout cells. Furthermore, a dominant negative mutant
of the small GTPase, Ras, blocks the effects of exogenous
hyaluronan (14). These results suggest that hyaluronan signals through
Ras to regulate motility and are consistent with previous studies
showing that exogenous hyaluronan-receptor interactions regulate Ras
signaling (4, 8). This ability of hyaluronan to activate intracellular
signaling cascades requires interactions with cell-associated
hyaluronan-binding proteins or hyaladherins (15) but is additionally
modified by the amount and size of hyaluronan present in the
environment of the cell. Further, not all cell types activate signaling
cascades in response to hyaluronan (11), indicating that cell
background is also an important determinant. Here, we review current
understanding of the mechanisms by which hyaluronan signals.
 |
Role of Hyaluronan Receptors in Signaling |
The first cell-associated hyaladherin, RHAMM, whose cell
surface form is now designated CD168, was isolated from embryonic heart
cells (16).2 Later CD44 was
identified as the first integral hyaluronan "receptor." Both RHAMM
and CD44 mediate hyaluronan signaling and participate in growth
factor-regulated signaling. However, they likely regulate signaling by
different mechanisms because they are not homologous proteins, are
compartmentalized differently in the cell (17),2 and differ
in the mechanisms by which they bind to hyaluronan (18) (Figs.
1 and 2). Additional cellular
hyaladherins have been identified
(19-22), but their role in cell signaling has not yet been reported.
Therefore, this review focuses upon the signaling cascades that RHAMM
and CD44 regulate.

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Fig. 1.
A current model for hyaluronan dependent,
CD44-specific signaling pathways. CD44-hyaluronan interactions
promote tyrosine kinase (TK) activity of HER2 and the
non-receptor kinase, Src. Src phosphorylates cortactin, which recruits
it to the cell membrane. CD44-hyaluronan interactions also activate
RHOA and Rac1, and CD44 binds to Tiam1 and Vav2. Hyaluronan
(HA) also promotes the association of CD44 forms with
cytoskeletal proteins such as ankyrin and ERM proteins. Activation of
these signaling pathways together leads to tumor behavior such as
migration and invasion. Our current model suggests that the
close interactions between CD44 and its selected binding partners play
a pivotal role in coordinating "cross-talk" among various
intracellular signaling pathways (e.g. Rho/Ras signaling and
receptor-linked (p185HER2)/non-receptor-linked (c-Src) tyrosine
kinase pathways) leading to the concomitant onset of multiple functions
such as tumor cell adhesion, proliferation/growth, migration, and
invasion. MLC, myosin light chains.
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Fig. 2.
A current model for hyaluronan
(HA)-dependent,
RHAMM-mediated signaling pathways. RHAMM is an itinerant
hyaladherin that occurs in multiple subcellular compartments and that
can also be exported to the extracellular milieu where it binds to the
cell surface. Cell surface RHAMM-hyaluronan interactions regulate
signaling through Ras and Src. Cell surface RHAMM modifies the ability
of the PDGF receptor to activate Erk kinase, a key map kinase involved
in cell motility. Intracellular RHAMM proteins encode multiple kinase
docking and recognition sites, and one intracellular form has been
shown to physically associate with Erk1 kinase. Intracellular forms
also associate with the cytoskeleton, notably interphase and mitotic
spindle microtubules. The ability of intracellular RHAMM forms to
associate with multiple signaling complexes and to associate with the
cytoskeleton suggest that they function as adapter proteins like
vinculin and paxillin. FAK, focal adhesion kinase.
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CD44
CD44 is an integral protein that is subject to extensive
alternative splicing (23-26). All CD44 isoforms contain a link module hyaluronan-binding site in their extracellular domain (see minireview by Day and Prestwich (18) in this series). The binding of CD44 isoforms
to hyaluronan affects cell adhesion to extracellular matrix components
and is implicated in the stimulation of aggregation, proliferation,
migration, and angiogenesis (23-25, 27, 28). The intracellular domain
of CD44 isoforms selectively interacts with cytoskeletal proteins and
regulates specific signaling (27). Therefore, CD44 isoforms likely
provide a direct association between hyaluronan and the cytoskeleton.
The mechanisms by which CD44 achieves this association and the
signaling cascades that it regulates are summarized in Fig. 1.
CD44 Interaction with Tyrosine Kinases--
CD44 is tightly
coupled with at least two tyrosine kinases, p185HER2 (7)
and c-Src kinase (6). CD44 and p185HER2 are physically
linked to each other via interchain disulfide bonds; and hyaluronan can
stimulate CD44-associated p185HER2 tyrosine kinase activity
that leads to increased tumor cell growth (7). The cytoplasmic domain
of CD44 binds to c-Src kinase at a single site with high affinity (6,
29). Importantly, hyaluronan interaction with CD44 stimulates c-Src
kinase activity, increasing tyrosine phosphorylation of the
cytoskeletal protein, cortactin. This attenuates the ability of
cortactin to cross-link filamentous actin in vitro (Fig. 1)
(6). Most Src family kinases are modified with specific lipids that
direct them to subdomains of the cell membrane called "rafts" that
have high cholesterol and glycolipid content. The Src kinases, Lck and
Fyn, associate with CD44 in glycosphingolipid-rich plasma membrane
domains of human peripheral blood lymphocytes (29). Thus, direct
binding of CD44 to c-Src kinase in the membrane "rafts" may
facilitate hyaluronan-mediated stimulation of the catalytic activity of
c-Src kinase and induce cytoskeleton-regulated tumor cell migration.
Therefore, the binding of hyaluronan to CD44 isoforms, which complex
with p185HER2 and c-Src kinase, likely trigger direct
"cross-talk" between two tyrosine kinase-linked signaling pathways
during tumor progression.
CD44-specific Activation of Rho-like GTPases--
Rho GTPases such
as RhoA and Rac1 participate in the interaction between CD44 and
cytoskeletal proteins. In particular, RhoA is non-covalently linked to
a CD44 alternate isoform (e.g.
CD44V3,8-10) in breast tumor cells (30). When
complexed with CD44V3, RhoA stimulates Rho kinase (ROK) to
phosphorylate several cellular proteins including
CD44V3,8-10. This phosphorylation promotes binding of the
CD44 variant to ankyrin (Fig. 1). Overexpression of the Rho-binding
domain can act as a dominant negative inhibitor of ROK and reverse
tumor cell-specific phenotypes (30). Therefore, it has been proposed
that CD44v3,8-10 and RhoA-mediated signaling are involved
in the up-regulation of ROK and that this is necessary for
membrane-cytoskeleton interactions and tumor cell migration during the
progression of breast cancers (30).
Binding of hyaluronan to some CD44-expressing cells also activates Rac1
signaling, a pathway known to regulate actin assembly that is
associated with membrane ruffling, cellular projections, cell motility,
and cell transformation (31, 32). In particular, the cytoplasmic domain
of CD44 binds to guanine nucleotide exchange factors such as Tiam1 and
Vav2 that have been shown to catalyze the GDP-GTP exchange leading to
hyaluronan-mediated tumor cell migration (Fig. 1) (32-34). The fact
that both Tiam1-Rac1 activation (31, 33, 34) and RhoA-mediated ROK
activity (30) are involved in regulating cytoskeleton function and cell
motility in a hyaluronan- and CD44-dependent manner
suggests these pathways play a pivotal role in hyaluronan-stimulated
CD44 signaling.
CD44 Interaction with the Cytoskeleton--
The first 19 residues
of the cytoplasmic domain of CD44 interact with the cytoskeleton
membrane linker proteins, ezrin/radixin/moesin (ERM) (32), which
contain the KKXn(K/R)K motif for phosphatidylinositol 4,5-bisphosphate (PIP2) binding (35).
Mutation of this motif on ezrin results in the loss of the
PIP2 requirement for optimal binding of ezrin to CD44 but
does not influence the complex formation between ezrin and CD44 (35).
These findings suggest that the linkage between ERM and CD44 can form
in either a PIP2-dependent or a
PIP2-independent manner. An involvement of PIP2
in regulating CD44-ERM interaction during hyaluronan signaling has not
yet been reported.
Ankyrin is also a family of membrane-associated cytoskeletal proteins
expressed in a variety of biological systems (24, 28). The cytoplasmic
domain of CD44 (~70 amino acids) is highly conserved in most of the
CD44 isoforms and is directly involved in ankyrin binding (24, 28).
Deletion mutation analyses indicate that at least two subregions within
the CD44 cytoplasmic domain contribute to the ankyrin binding, namely
region I (e.g. the high affinity ankyrin-binding region) and
region II (e.g. the regulatory region). In particular,
region I (306NGGNGTVEDRKPSEL320 in the mouse
CD44 and 304NSGNGAVEDRKPSGL318 in the human
CD44) is required for hyaluronan-mediated binding and cell adhesion
(24). Furthermore, an ankyrin-binding domain of CD44 isoforms has also
been shown to be necessary for oncogenic signaling and tumor cell
transformation (27). Recently, fragments of the ankyrin repeat
domain and/or the subdomain 2 of ankyrin repeat domain have been
identified as an ankyrin-binding region for both CD44 (26) and Tiam1
(32). Overexpression of these ankyrin fragments promotes
hyaluronan-dependent and CD44-specific tumor cell migration
(33). These observations support the notion that CD44-ankyrin
interaction is not only very important for presenting CD44 properly for
hyaluronan binding but is also required for cytoskeleton activation
during hyaluronan signaling (Fig. 1).
RHAMM
Like CD44, RHAMM is alternatively spliced.2 Truncated
RHAMM forms are also expressed in cells following injury (36), in
tumors, and in some mutant active Ras-transformed cell lines (9,
37-39). RHAMM distributes into multiple compartments including the
cell surface (40),2 cytoskeleton (41), mitochondria (42),
and cell nucleus (41, 43). The RHAMM gene does not encode a traditional
leader sequence to permit secretion via the traditional
Golgi/endoplasmic reticulum export pathway, thus, resembling proteins
such as bFGF, HIV Tat protein, the homeobox protein engrailed (44),
heat shock proteins (45, 46), and epimorphin (47).
The binding of exogenous hyaluronan to cell surface RHAMM plays a key
role in activating signaling cascades, probably as a co-receptor for
integral membrane proteins. Although the role(s) of intracellular RHAMM
protein forms are not yet known, their ability to associate with
kinases (5, 9), calmodulin (41, 42), and the cytoskeleton (41, 43)
predicts that they play key roles in cytoskeletal assembly. The
presence of intracellular hyaladherins typified by RHAMM also raises
the interesting possibility that intracellular hyaluronan (48-50)
plays a role in signaling. If so, the separation of cell surface RHAMM
from the intracellular RHAMM forms provides the potential for a modular
association among hyaluronan, cytoskeleton-signaling complexes, and the
cell nucleus (Fig. 2). In this case, hyaladherins such as RHAMM could
contribute to the back and forth flow of information between the cell
genome and the extracellular environment, a phenomenon that has been termed "dynamic reciprocity" (51). For instance, RHAMM modules could represent a modified version of "inside-outside" signaling characteristic of integrin receptors (52).
RHAMM Interaction with Tyrosine and Serine/Threonine Kinases (see
Fig. 2)--
Cell surface RHAMM-hyaluronan interactions mediate
activation of the protein tyrosine kinases, Src (5) and focal adhesion kinase (4, 8, 10), as well as Erk kinases (10) and protein kinase C
(11, 12). Additionally, cell surface RHAMM is required for activation
of Erk kinases through PDGF (9), nerve growth factor (53), and after
stretch injury (54). Activation of Src through cell surface RHAMM is
transient (5) but is nevertheless required for turnover of lamellae
focal adhesions and consequently for RHAMM-regulated cell motility (5).
Proteins that are phosphorylated on tyrosine as a result of
hyaluronan-RHAMM interactions include paxillin, cortactin, focal
adhesion kinase, and the MAP kinases, Erk1 and -2 (10).
RHAMM co-associates with ~20% of total cellular Erk1 kinase (9) and
~10% of total cellular Src (5), as determined by co-immunoprecipitation analyses. Because RHAMM contains recognition sequences for both Src and Erk (MOTIF SCANNER,
cansite.bidmc.harvard.edu), it is likely that intracellular RHAMM
forms associate directly with these kinases. RHAMM contains
multiple SH3- and SH2-binding sites as well as putative phosphoacceptor
sites for additional serine/threonine kinases. Intracellular forms may
therefore participate in linking kinases together as complexes and/or
retaining them within the cytoskeleton and the nucleus.
RHAMM Regulation of Ras GTPase--
Several studies have indicated
that RHAMM regulates Ras (4, 5, 8, 9, 37, 55), and this regulation
likely involves both cell surface and intracellular RHAMM forms. Cell
surface RHAMM is required for random motility (4, 5), progression through the G2M boundary of cell cycle (55), and
transformation by oncogenic Ras (8), as determined by antibody blocking
and soluble protein competition. Both cell surface and intracellular forms of RHAMM may regulate Ras but at different points along the
signaling pathways (e.g. in Fig. 2).
The ability of RHAMM to regulate Ras requires its hyaluronan binding
ability. Thus, mutation of the RHAMM hyaluronan-binding sites blocks
oncogenic Ras-mediated motility and transformation (8). This is
consistent with a requirement for Ras in the hyaluronan-mediated rescue
of HAS2 / cell motility (14).
RHAMM Interaction with the Cytoskeleton--
Cell surface RHAMM
occurs in cell lamellae and podosomes where it co-distributes with
cortactin.2 Exogenous hyaluronan initially promotes
spreading of cell lamellae and turnover of focal adhesions in
fibroblasts transfected with oncogenic Ras that express cell surface
RHAMM and that are plated onto fibronectin-coated surfaces (4). This
effect of hyaluronan is proposed to act through cell surface RHAMM
because blocking RHAMM antibodies inhibit, whereas agonist RHAMM
antibodies mimic this effect (6, 7). The rapid formation and then
disassembly of focal adhesions precede a hyaluronan-induced increase in
cell motility (4). These effects are possibly mediated, either directly or indirectly, through integrin receptors. For example, cell surface RHAMM co-regulates migration of thymocytes on fibronectin substrata in
concert with the integrin fibronectin receptors,
4 1 or 5 1 (56).
Intracellular RHAMM forms associate with the actin cytoskeleton and
both interphase and mitotic spindle microtubules (41). The ability of
RHAMM to form coiled coils as well as its limited homology with
proteins such as D-CLIP (57) that link microtubules and actin filaments
suggests that intracellular RHAMM proteins may connect actin and
microtubule cytoskeleton (58). Because an association of RHAMM with
several kinases has already been established, it is likely that
intracellular RHAMM proteins act as adapter molecules, much like
vinculin and paxillin (59, 60) that connect the cytoskeleton to
signaling complexes. Transcriptional profiling of the cell cycle
progression reveals enhanced expression of both RHAMM and hyaluronan
synthase 2 (HAS2) at the G2M boundary (61). These last
results and the demonstration that intracellular hyaluronan decorates
the mitotic spindle (41) once again raise the possible role of
intracellular hyaluronan/RHAMM interactions in signaling.
RHAMM and CD44 can perform separate functions in regulating cell
signaling (10, 38, 62, 63). For instance, CD44, but not cell surface
RHAMM, can mediate adhesion of endothelial cells and thymocytes
to hyaluronan (62) and regulate proliferation (38, 63). In
contrast, cell surface RHAMM, but not CD44, is required for migration
(62, 63). As well, cell surface RHAMM but not CD44 appears to be
essential for activation of protein tyrosine kinase cascades by
endothelial cells responding to hyaluronan (10). Deletion of either
CD44 or RHAMM3 does not
result in embryonic lethality and therefore either these two
hyaladherins share some functions and/or other cellular hyaladherins are able to compensate for the loss of either CD44 or RHAMM. Phenotypes for CD44 / have been described (Ref. 64 and see below).
 |
Potential Role of Hyaluronan Size in Signaling: Importance in
Response to Injury |
In physiologic conditions, hyaluronan is a high average molecular
mass polymer in excess of 106 Da. However, following tissue
injury, hyaluronan fragments of lower molecular mass accumulate. A
potential functional significance for hyaluronan fragments has been
suggested by in vitro studies (e.g. Refs.
65-67). Oligomers of 8-16 disaccharides prepared by enzymatic
digestion of native hyaluronan induce angiogenesis in a chick corneal
assay whereas the native hyaluronan molecules do not (68). Small
amounts of high molecular weight hyaluronan can activate
protein-tyrosine kinase cascades in endothelial cells and
Ras-transformed fibroblasts (4, 10), although at lower levels than
smaller fragments (10). Studies with inflammatory macrophages have
shown that fragmented hyaluronan with an average molecular mass of
250,000 Da, but not native hyaluronan from which it was prepared, can
induce the expression of inflammatory genes (64, 65-69). Similar
results have been shown with renal tubular epithelial cells (70), T-24
carcinoma cells (71), and eosinophils (72). Smaller hyaluronan
oligosaccharides in the 6-20 kDa size range (but not the 250,000 Da or
higher molecular mass hyaluronan) induce inflammatory gene expression
in dendritic cells (73). Controls for excluding contaminating
substances that can be present in even medical grade hyaluronan
preparations are often lacking, as noted in Ref. 75. Nevertheless,
biological relevance is suggested by reports showing that fragmented
hyaluronan that induces inflammatory gene expression in
vitro is in the same size range as hyaluronan that accumulates
under inflammatory conditions in vivo (74). A common theme
appears to be that low (but not high) molecular weight hyaluronan can
initiate gene transcription geared toward cell proliferation and
migration. Generation of hyaluronan fragments under conditions of
inflammation, tumorigenesis, or tissue injury as a result of
hyaluronidases (76) or oxidation (77) may then signal the host that
normal homeostasis has been profoundly disturbed.
 |
Role of Hyaladherins in Hyaluronan Internalization and Host
Response to Injury |
Cellular hyaladherins also bind and internalize hyaluronan (1).
Depending on the cell type, the binding affinity and rate of
internalization varies. Elegant studies have recently shown that the
avidity of binding of hyaluronan oligomers to CD44 increases with an
oligomer size of up to 38 sugars (78). Labeled hyaluronan is also
observed in the cytoplasm as a diffuse network and in vesicles,
in lamellae and the nucleus of smooth muscle cells and fibroblasts (49, 50). This unusual pattern of uptake is most obvious
following stimulation of serum-starved 3T3 cells or in subconfluent,
mutant active Ras-transfected fibroblasts. Hyaluronan uptake into these
novel compartments is associated with enhanced cell motility (49).
CD44-deficient mice develop normally but exhibit abnormalities in
hematopoiesis and lymphocyte recirculation (79, 80). Induction of
inflammatory gene expression in response to hyaluronan is observed in
the absence of CD44 in cultures of bone marrow and dendritic cells (73,
81). These data suggest that there are CD44-independent mechanisms for
induction of gene expression by hyaluronan. In contrast, CD44-deficient
mice challenged in models of tissue injury have revealed essential
roles for CD44 in regulating pathogenesis of host injury (82, 83).
Depending on the mechanism of pathogenesis and the predominant cell
types that mediate the host injury, differing effects of CD44 have been observed. In a model of endothelial cell injury mediated by
interleukin-2, CD44-deficient mice were protected from endothelial
injury (82). This protection may be because of a decrease in
interleukin-2-induced lymphocyte-activated killer cell activity.
However, in a model of hepatocellular injury due to administration of
concanavalin A, CD44-deficient mice exhibited enhanced hepatitis (83).
The increased susceptibility to hepatocyte injury correlated with the
observation that T cells from CD44-deficient animals were resistant to
activation-induced cell death. The challenge of future studies will be
to sort out the CD44-dependent as well as the independent
roles in mediating hyaluronan-cell interactions.
 |
Conclusions |
Hyaluronan signaling involves cellular hyaladherins such as CD44
and RHAMM that are selectively coupled with their particular downstream
signaling pathway(s) leading to the onset of
hyaluronan-dependent functions in various cell types and
tissues. A signaling response to hyaluronan may be strongly influenced
by both the size of hyaluronan and the cell background. Additional
studies with defined preparations of hyaluronan of varying size that
utilize hyaladherin null mice are clearly required to sort out the
cellular conditions that permit hyaluronan-mediated signaling.
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FOOTNOTES |
*
This minireview will be reprinted
in the 2002 Minireview Compendium, which
will be available in December, 2002.
§
To whom correspondence should be addressed: London Regional Cancer
Center, University of Western Ontario, 790 Commissioners Rd. E., London
N6A 4L6, Canada. Tel.: 519-685-8651; Fax: 519-685-8646; E-mail:
eva. turley@lrcc.on.ca.
Published, JBC Papers in Press, November 20, 2001, DOI 10.1074/jbc.R100038200
2
E. A. Turley and R. E. Harrison,
www.glycoforum.gr.jp.
3
C. Toelg, S. Hamilton, and E. A. Turley,
unpublished results.
 |
ABBREVIATIONS |
The abbreviations used are:
MAP, mitogen-activated protein;
HAS2, hyaluronan synthase 2;
ROK, Rho
kinase;
ERM, ezrin/radixin/moesin;
PIP2, phosphatidylinositol 4,5-bisphosphate;
PDGF, platelet-derived growth
factor;
RHAMM, receptor for hyaluronan-mediated motility.
 |
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[Full Text]
[PDF]
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D. R. Yager, R. A. Kulina, and L. A. Gilman
Wound Fluids: A Window Into the Wound Environment?
International Journal of Lower Extremity Wounds,
December 1, 2007;
6(4):
262 - 272.
[Abstract]
[PDF]
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M. Choudhary, X. Zhang, P. Stojkovic, L. Hyslop, G. Anyfantis, M. Herbert, A. P. Murdoch, M. Stojkovic, and M. Lako
Putative Role of Hyaluronan and Its Related Genes, HAS2 and RHAMM, in Human Early Preimplantation Embryogenesis and Embryonic Stem Cell Characterization
Stem Cells,
December 1, 2007;
25(12):
3045 - 3057.
[Abstract]
[Full Text]
[PDF]
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M. Ramaswamy, C. Dumont, A. C. Cruz, J. R. Muppidi, T. S. Gomez, D. D. Billadeau, V. L. J. Tybulewicz, and R. M. Siegel
Cutting Edge: Rac GTPases Sensitize Activated T Cells to Die via Fas
J. Immunol.,
November 15, 2007;
179(10):
6384 - 6388.
[Abstract]
[Full Text]
[PDF]
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P. A. Singleton, R. Salgia, L. Moreno-Vinasco, J. Moitra, S. Sammani, T. Mirzapoiazova, and J. G. N. Garcia
CD44 Regulates Hepatocyte Growth Factor-mediated Vascular Integrity: ROLE OF c-Met, Tiam1/Rac1, DYNAMIN 2, AND CORTACTIN
J. Biol. Chem.,
October 19, 2007;
282(42):
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[Abstract]
[Full Text]
[PDF]
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V. Sancho-Shimizu, R. Khan, S. Mostowy, L. Lariviere, R. Wilkinson, N. Riendeau, M. Behr, and D. Malo
Molecular Genetic Analysis of Two Loci (Ity2 and Ity3) Involved in the Host Response to Infection With Salmonella Typhimurium Using Congenic Mice and Expression Profiling
Genetics,
October 1, 2007;
177(2):
1125 - 1139.
[Abstract]
[Full Text]
[PDF]
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P. M Taylor
Biological matrices and bionanotechnology
Phil Trans R Soc B,
August 29, 2007;
362(1484):
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[Abstract]
[Full Text]
[PDF]
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D. Manzanares, M.-E. Monzon, R. C. Savani, and M. Salathe
Apical Oxidative Hyaluronan Degradation Stimulates Airway Ciliary Beating via RHAMM and RON
Am. J. Respir. Cell Mol. Biol.,
August 1, 2007;
37(2):
160 - 168.
[Abstract]
[Full Text]
[PDF]
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L. Y. W. Bourguignon, E. Gilad, and K. Peyrollier
Heregulin-mediated ErbB2-ERK Signaling Activates Hyaluronan Synthases Leading to CD44-dependent Ovarian Tumor Cell Growth and Migration
J. Biol. Chem.,
July 6, 2007;
282(27):
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[Abstract]
[Full Text]
[PDF]
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K. Hosono, Y. Nishida, W. Knudson, C. B. Knudson, T. Naruse, Y. Suzuki, and N. Ishiguro
Hyaluronan Oligosaccharides Inhibit Tumorigenicity of Osteosarcoma Cell Lines MG-63 and LM-8 in Vitro and in Vivo via Perturbation of Hyaluronan-Rich Pericellular Matrix of the Cells
Am. J. Pathol.,
July 1, 2007;
171(1):
274 - 286.
[Abstract]
[Full Text]
[PDF]
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S. R. Hamilton, S. F. Fard, F. F. Paiwand, C. Tolg, M. Veiseh, C. Wang, J. B. McCarthy, M. J. Bissell, J. Koropatnick, and E. A. Turley
The Hyaluronan Receptors CD44 and Rhamm (CD168) Form Complexes with ERK1,2 That Sustain High Basal Motility in Breast Cancer Cells
J. Biol. Chem.,
June 1, 2007;
282(22):
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[Abstract]
[Full Text]
[PDF]
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D. L. Russell and R. L. Robker
Molecular mechanisms of ovulation: co-ordination through the cumulus complex
Hum. Reprod. Update,
May 1, 2007;
13(3):
289 - 312.
[Abstract]
[Full Text]
[PDF]
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S. J. Wang, K. Peyrollier, and L. Y. Bourguignon
The Influence of Hyaluronan-CD44 Interaction on Topoisomerase II Activity and Etoposide Cytotoxicity in Head and Neck Cancer
Arch Otolaryngol Head Neck Surg,
March 1, 2007;
133(3):
281 - 288.
[Abstract]
[Full Text]
[PDF]
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H. Koyama, T. Hibi, Z. Isogai, M. Yoneda, M. Fujimori, J. Amano, M. Kawakubo, R. Kannagi, K. Kimata, S. Taniguchi, et al.
Hyperproduction of Hyaluronan in Neu-Induced Mammary Tumor Accelerates Angiogenesis through Stromal Cell Recruitment: Possible Involvement of Versican/PG-M
Am. J. Pathol.,
March 1, 2007;
170(3):
1086 - 1099.
[Abstract]
[Full Text]
[PDF]
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E. N. Harris, S. V. Kyosseva, J. A. Weigel, and P. H. Weigel
Expression, Processing, and Glycosaminoglycan Binding Activity of the Recombinant Human 315-kDa Hyaluronic Acid Receptor for Endocytosis (HARE)
J. Biol. Chem.,
February 2, 2007;
282(5):
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[Abstract]
[Full Text]
[PDF]
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L. Y. W. Bourguignon, K. Peyrollier, E. Gilad, and A. Brightman
Hyaluronan-CD44 Interaction with Neural Wiskott-Aldrich Syndrome Protein (N-WASP) Promotes Actin Polymerization and ErbB2 Activation Leading to beta-Catenin Nuclear Translocation, Transcriptional Up-regulation, and Cell Migration in Ovarian Tumor Cells
J. Biol. Chem.,
January 12, 2007;
282(2):
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[Abstract]
[Full Text]
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C. Tolg, S. R. Hamilton, K.-A. Nakrieko, F. Kooshesh, P. Walton, J. B. McCarthy, M. J. Bissell, and E. A. Turley
Rhamm-/- fibroblasts are defective in CD44-mediated ERK1,2 motogenic signaling, leading to defective skin wound repair
J. Cell Biol.,
December 18, 2006;
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[Abstract]
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S. Misra, B. P. Toole, and S. Ghatak
Hyaluronan Constitutively Regulates Activation of Multiple Receptor Tyrosine Kinases in Epithelial and Carcinoma Cells
J. Biol. Chem.,
November 17, 2006;
281(46):
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[Abstract]
[Full Text]
[PDF]
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P. A. Singleton, S. M. Dudek, S.-F. Ma, and J. G. N. Garcia
Transactivation of Sphingosine 1-Phosphate Receptors Is Essential for Vascular Barrier Regulation: NOVEL ROLE FOR HYALURONAN AND CD44 RECEPTOR FAMILY
J. Biol. Chem.,
November 10, 2006;
281(45):
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[Abstract]
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[PDF]
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Y. Goueffic, C. Guilluy, P. Guerin, P. Patra, P. Pacaud, and G. Loirand
Hyaluronan induces vascular smooth muscle cell migration through RHAMM-mediated PI3K-dependent Rac activation
Cardiovasc Res,
November 1, 2006;
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339 - 348.
[Abstract]
[Full Text]
[PDF]
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L. Li, C.-H. Heldin, and P. Heldin
Inhibition of Platelet-derived Growth Factor-BB-induced Receptor Activation and Fibroblast Migration by Hyaluronan Activation of CD44
J. Biol. Chem.,
September 8, 2006;
281(36):
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[Abstract]
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[PDF]
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L. Zhuo, A. Kanamori, R. Kannagi, N. Itano, J. Wu, M. Hamaguchi, N. Ishiguro, and K. Kimata
SHAP Potentiates the CD44-mediated Leukocyte Adhesion to the Hyaluronan Substratum
J. Biol. Chem.,
July 21, 2006;
281(29):
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[Abstract]
[Full Text]
[PDF]
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S. J. Wang and L. Y. W. Bourguignon
Hyaluronan and the Interaction Between CD44 and Epidermal Growth Factor Receptor in Oncogenic Signaling and Chemotherapy Resistance in Head and Neck Cancer.
Arch Otolaryngol Head Neck Surg,
July 1, 2006;
132(7):
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[Abstract]
[Full Text]
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G. Cao, R. C. Savani, M. Fehrenbach, C. Lyons, L. Zhang, G. Coukos, and H. M. DeLisser
Involvement of Endothelial CD44 during in Vivo Angiogenesis
Am. J. Pathol.,
July 1, 2006;
169(1):
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[Abstract]
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S. C. Thakur, V. Kumar, I. Ghosh, A. Bharadwaj, and K. Datta
Appearance of Hyaluronan Binding Protein 1 Proprotein in Pachytene Spermatocytes and Round Spermatids Correlates With Spermatogenesis
J Androl,
July 1, 2006;
27(4):
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[Abstract]
[Full Text]
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A. Kultti, K. Rilla, R. Tiihonen, A. P. Spicer, R. H. Tammi, and M. I. Tammi
Hyaluronan Synthesis Induces Microvillus-like Cell Surface Protrusions
J. Biol. Chem.,
June 9, 2006;
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[Abstract]
[Full Text]
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L. Y. W. Bourguignon, E. Gilad, A. Brightman, F. Diedrich, and P. Singleton
Hyaluronan-CD44 Interaction with Leukemia-associated RhoGEF and Epidermal Growth Factor Receptor Promotes Rho/Ras Co-activation, Phospholipase C{epsilon}-Ca2+ Signaling, and Cytoskeleton Modification in Head and Neck Squamous Cell Carcinoma Cells
J. Biol. Chem.,
May 19, 2006;
281(20):
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[Abstract]
[Full Text]
[PDF]
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K. N. Sugahara, T. Hirata, H. Hayasaka, R. Stern, T. Murai, and M. Miyasaka
Tumor Cells Enhance Their Own CD44 Cleavage and Motility by Generating Hyaluronan Fragments
J. Biol. Chem.,
March 3, 2006;
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[Abstract]
[Full Text]
[PDF]
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M. Ori, M. Nardini, P. Casini, R. Perris, and I. Nardi
XHas2 activity is required during somitogenesis and precursor cell migration in Xenopus development
Development,
February 15, 2006;
133(4):
631 - 640.
[Abstract]
[Full Text]
[PDF]
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K. R. Taylor and R. L. Gallo
Glycosaminoglycans and their proteoglycans: host-associated molecular patterns for initiation and modulation of inflammation
FASEB J,
January 1, 2006;
20(1):
9 - 22.
[Abstract]
[Full Text]
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S. J. Wang and L. Y. W. Bourguignon
Hyaluronan-CD44 Promotes Phospholipase C-Mediated Ca2+ Signaling and Cisplatin Resistance in Head and Neck Cancer
Arch Otolaryngol Head Neck Surg,
January 1, 2006;
132(1):
19 - 24.
[Abstract]
[Full Text]
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H. Nochi, T. Shinomiya, and K. Tamoto
Characterization of Hyaluronan-Binding Proteins on Guinea Pig Polymorphonuclear Leukocytes: Possible Involvement of Complement Receptor Type 3 (CR3, CD11b/CD18) in the Hyaluronan-Leukocyte Interaction
J. Biochem.,
January 1, 2006;
139(1):
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[Abstract]
[Full Text]
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G. Tzircotis, R. F. Thorne, and C. M. Isacke
Chemotaxis towards hyaluronan is dependent on CD44 expression and modulated by cell type variation in CD44-hyaluronan binding
J. Cell Sci.,
November 1, 2005;
118(21):
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[Abstract]
[Full Text]
[PDF]
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V. B. Lokeshwar, W. H. Cerwinka, T. Isoyama, and B. L. Lokeshwar
HYAL1 Hyaluronidase in Prostate Cancer: A Tumor Promoter and Suppressor
Cancer Res.,
September 1, 2005;
65(17):
7782 - 7789.
[Abstract]
[Full Text]
[PDF]
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H. Chao and A. P. Spicer
Natural Antisense mRNAs to Hyaluronan Synthase 2 Inhibit Hyaluronan Biosynthesis and Cell Proliferation
J. Biol. Chem.,
July 29, 2005;
280(30):
27513 - 27522.
[Abstract]
[Full Text]
[PDF]
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K.-J. Bai, A. P. Spicer, M. M. Mascarenhas, L. Yu, C. D. Ochoa, H. G. Garg, and D. A. Quinn
The Role of Hyaluronan Synthase 3 in Ventilator-induced Lung Injury
Am. J. Respir. Crit. Care Med.,
July 1, 2005;
172(1):
92 - 98.
[Abstract]
[Full Text]
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Y. Takahashi, L. Li, M. Kamiryo, T. Asteriou, A. Moustakas, H. Yamashita, and P. Heldin
Hyaluronan Fragments Induce Endothelial Cell Differentiation in a CD44- and CXCL1/GRO1-dependent Manner
J. Biol. Chem.,
June 24, 2005;
280(25):
24195 - 24204.
[Abstract]
[Full Text]
[PDF]
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S. Misra, S. Ghatak, and B. P. Toole
Regulation of MDR1 Expression and Drug Resistance by a Positive Feedback Loop Involving Hyaluronan, Phosphoinositide 3-Kinase, and ErbB2
J. Biol. Chem.,
May 27, 2005;
280(21):
20310 - 20315.
[Abstract]
[Full Text]
[PDF]
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L. Y. W. Bourguignon, E. Gilad, K. Rothman, and K. Peyrollier
Hyaluronan-CD44 Interaction with IQGAP1 Promotes Cdc42 and ERK Signaling, Leading to Actin Binding, Elk-1/Estrogen Receptor Transcriptional Activation, and Ovarian Cancer Progression
J. Biol. Chem.,
March 25, 2005;
280(12):
11961 - 11972.
[Abstract]
[Full Text]
[PDF]
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V. B. Lokeshwar, W. H. Cerwinka, and B. L. Lokeshwar
HYAL1 Hyaluronidase: A Molecular Determinant of Bladder Tumor Growth and Invasion
Cancer Res.,
March 15, 2005;
65(6):
2243 - 2250.
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S. Bodevin-Authelet, M. Kusche-Gullberg, P. E. Pummill, P. L. DeAngelis, and U. Lindahl
Biosynthesis of Hyaluronan: DIRECTION OF CHAIN ELONGATION
J. Biol. Chem.,
March 11, 2005;
280(10):
8813 - 8818.
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S. Ghatak, S. Misra, and B. P. Toole
Hyaluronan Constitutively Regulates ErbB2 Phosphorylation and Signaling Complex Formation in Carcinoma Cells
J. Biol. Chem.,
March 11, 2005;
280(10):
8875 - 8883.
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C. A. Maxwell, J. J. Keats, A. R. Belch, L. M. Pilarski, and T. Reiman
Receptor for Hyaluronan-Mediated Motility Correlates with Centrosome Abnormalities in Multiple Myeloma and Maintains Mitotic Integrity
Cancer Res.,
February 1, 2005;
65(3):
850 - 860.
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H. Nakamura, R. Kato, A. Hirata, M. Inoue, and T. Yamamoto
Localization of CD44 (Hyaluronan Receptor) and Hyaluronan in Rat Mandibular Condyle
J. Histochem. Cytochem.,
January 1, 2005;
53(1):
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K. J. Straach, J. M. Shelton, J. A. Richardson, V. C. Hascall, and M. S. Mahendroo
Regulation of hyaluronan expression during cervical ripening
Glycobiology,
January 1, 2005;
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S. Nedvetzki, E. Gonen, N. Assayag, R. Reich, R. O. Williams, R. L. Thurmond, J.-F. Huang, B. A. Neudecker, F.-S. Wang, E. A. Turley, et al.
RHAMM, a receptor for hyaluronan-mediated motility, compensates for CD44 in inflamed CD44-knockout mice: A different interpretation of redundancy
PNAS,
December 28, 2004;
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C. D. Blundell, P. L. DeAngelis, A. J. Day, and A. Almond
Use of 15N-NMR to resolve molecular details in isotopically-enriched carbohydrates: sequence-specific observations in hyaluronan oligomers up to decasaccharides
Glycobiology,
November 1, 2004;
14(11):
999 - 1009.
[Abstract]
[Full Text]
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D. Baronas-Lowell, J. L. Lauer-Fields, J. A. Borgia, G. F. Sferrazza, M. Al-Ghoul, D. Minond, and G. B. Fields
Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by {alpha}2{beta}1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen
J. Biol. Chem.,
October 15, 2004;
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R. H. Jenkins, G. J. Thomas, J. D. Williams, and R. Steadman
Myofibroblastic Differentiation Leads to Hyaluronan Accumulation through Reduced Hyaluronan Turnover
J. Biol. Chem.,
October 1, 2004;
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E. V. Maytin, H. H. Chung, and V. M. Seetharaman
Hyaluronan Participates in the Epidermal Response to Disruption of the Permeability Barrier in Vivo
Am. J. Pathol.,
October 1, 2004;
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K. Aoki, S. Matsumoto, Y. Hirayama, T. Wada, Y. Ozeki, M. Niki, P. Domenech, K. Umemori, S. Yamamoto, A. Mineda, et al.
Extracellular Mycobacterial DNA-binding Protein 1 Participates in Mycobacterium-Lung Epithelial Cell Interaction through Hyaluronic Acid
J. Biol. Chem.,
September 17, 2004;
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E. J. Armstrong and J. Bischoff
Heart Valve Development: Endothelial Cell Signaling and Differentiation
Circ. Res.,
September 3, 2004;
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A. Farb, F. D. Kolodgie, J.-Y. Hwang, A. P. Burke, K. Tefera, D. K. Weber, T. N. Wight, and R. Virmani
Extracellular Matrix Changes in Stented Human Coronary Arteries
Circulation,
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110(8):
940 - 947.
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[Full Text]
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L. Y. W. Bourguignon, P. A. Singleton, and F. Diedrich
Hyaluronan-CD44 Interaction with Rac1-dependent Protein Kinase N-{gamma} Promotes Phospholipase C{gamma}1 Activation, Ca2+ Signaling, and Cortactin-Cytoskeleton Function Leading to Keratinocyte Adhesion and Differentiation
J. Biol. Chem.,
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H. Zhang, S. L. Baader, M. Sixt, J. Kappler, and U. Rauch
Neurocan-GFP Fusion Protein: A New Approach to Detect Hyaluronan on Tissue Sections and Living Cells
J. Histochem. Cytochem.,
July 1, 2004;
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L. Y. W. Bourguignon, P. A. Singleton, F. Diedrich, R. Stern, and E. Gilad
CD44 Interaction with Na+-H+ Exchanger (NHE1) Creates Acidic Microenvironments Leading to Hyaluronidase-2 and Cathepsin B Activation and Breast Tumor Cell Invasion
J. Biol. Chem.,
June 25, 2004;
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J. J. Peluso, A. Pappalardo, G. Fernandez, and C. A. Wu
Involvement of an Unnamed Protein, RDA288, in the Mechanism through which Progesterone Mediates Its Antiapoptotic Action in Spontaneously Immortalized Granulosa Cells
Endocrinology,
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B. K. Jha, N. Mitra, R. Rana, A. Surolia, D. M. Salunke, and K. Datta
pH and Cation-induced Thermodynamic Stability of Human Hyaluronan Binding Protein 1 Regulates Its Hyaluronan Affinity
J. Biol. Chem.,
May 28, 2004;
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N. Itano, T. Sawai, F. Atsumi, O. Miyaishi, S. Taniguchi, R. Kannagi, M. Hamaguchi, and K. Kimata
Selective Expression and Functional Characteristics of Three Mammalian Hyaluronan Synthases in Oncogenic Malignant Transformation
J. Biol. Chem.,
April 30, 2004;
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S. Takeo, M. Fujise, T. Akiyama, H. Habuchi, N. Itano, T. Matsuo, T. Aigaki, K. Kimata, and H. Nakato
In Vivo Hyaluronan Synthesis upon Expression of the Mammalian Hyaluronan Synthase Gene in Drosophila
J. Biol. Chem.,
April 30, 2004;
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T. Murai, Y. Miyazaki, H. Nishinakamura, K. N. Sugahara, T. Miyauchi, Y. Sako, T. Yanagida, and M. Miyasaka
Engagement of CD44 Promotes Rac Activation and CD44 Cleavage during Tumor Cell Migration
J. Biol. Chem.,
February 6, 2004;
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J. Bakkers, C. Kramer, J. Pothof, N. E. M. Quaedvlieg, H. P. Spaink, and M. Hammerschmidt
Has2 is required upstream of Rac1 to govern dorsal migration of lateral cells during zebrafish gastrulation
Development,
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R. F. Thorne, J. W. Legg, and C. M. Isacke
The role of the CD44 transmembrane and cytoplasmic domains in co-ordinating adhesive and signalling events
J. Cell Sci.,
January 22, 2004;
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[Abstract]
[Full Text]
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S. Esnault and J. S. Malter
Hyaluronic Acid or TNF-{alpha} Plus Fibronectin Triggers Granulocyte Macrophage-Colony-Stimulating Factor mRNA Stabilization in Eosinophils Yet Engages Differential Intracellular Pathways and mRNA Binding Proteins
J. Immunol.,
December 15, 2003;
171(12):
6780 - 6787.
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C. D. Blundell, D. J. Mahoney, A. Almond, P. L. DeAngelis, J. D. Kahmann, P. Teriete, A. R. Pickford, I. D. Campbell, and A. J. Day
The Link Module from Ovulation- and Inflammation-associated Protein TSG-6 Changes Conformation on Hyaluronan Binding
J. Biol. Chem.,
December 5, 2003;
278(49):
49261 - 49270.
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S. Karvinen, S. Pasonen-Seppanen, J. M. T. Hyttinen, J.-P. Pienimaki, K. Torronen, T. A. Jokela, M. I. Tammi, and R. Tammi
Keratinocyte Growth Factor Stimulates Migration and Hyaluronan Synthesis in the Epidermis by Activation of Keratinocyte Hyaluronan Synthases 2 and 3
J. Biol. Chem.,
December 5, 2003;
278(49):
49495 - 49504.
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A. Zoltan-Jones, L. Huang, S. Ghatak, and B. P. Toole
Elevated Hyaluronan Production Induces Mesenchymal and Transformed Properties in Epithelial Cells
J. Biol. Chem.,
November 14, 2003;
278(46):
45801 - 45810.
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R. J. McKallip, M. Fisher, Y. Do, A. K. Szakal, U. Gunthert, P. S. Nagarkatti, and M. Nagarkatti
Targeted Deletion of CD44v7 Exon Leads to Decreased Endothelial Cell Injury but Not Tumor Cell Killing Mediated by Interleukin-2-activated Cytolytic Lymphocytes
J. Biol. Chem.,
October 31, 2003;
278(44):
43818 - 43830.
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F. Baluska, J. Samaj, P. Wojtaszek, D. Volkmann, and D. Menzel
Cytoskeleton-Plasma Membrane-Cell Wall Continuum in Plants. Emerging Links Revisited
Plant Physiology,
October 1, 2003;
133(2):
482 - 491.
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J. Sanceau, S. Truchet, and B. Bauvois
Matrix Metalloproteinase-9 Silencing by RNA Interference Triggers the Migratory-adhesive Switch in Ewing's Sarcoma Cells
J. Biol. Chem.,
September 19, 2003;
278(38):
36537 - 36546.
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L. Y. W. Bourguignon, P. A. Singleton, H. Zhu, and F. Diedrich
Hyaluronan-mediated CD44 Interaction with RhoGEF and Rho Kinase Promotes Grb2-associated Binder-1 Phosphorylation and Phosphatidylinositol 3-Kinase Signaling Leading to Cytokine (Macrophage-Colony Stimulating Factor) Production and Breast Tumor Progression
J. Biol. Chem.,
August 8, 2003;
278(32):
29420 - 29434.
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B. K. Jha, D. M. Salunke, and K. Datta
Structural Flexibility of Multifunctional HABP1 May Be Important for Regulating Its Binding to Different Ligands
J. Biol. Chem.,
July 18, 2003;
278(30):
27464 - 27472.
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S. Misra, S. Ghatak, A. Zoltan-Jones, and B. P. Toole
Regulation of Multidrug Resistance in Cancer Cells by Hyaluronan
J. Biol. Chem.,
July 3, 2003;
278(28):
25285 - 25288.
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E. Eriksson, L. Dons, A. G. Rothfuchs, P. Heldin, H. Wigzell, and M. E. Rottenberg
CD44-Regulated Intracellular Proliferation of Listeria monocytogenes
Infect. Immun.,
July 1, 2003;
71(7):
4102 - 4111.
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P. E. Pummill and P. L. DeAngelis
Alteration of Polysaccharide Size Distribution of a Vertebrate Hyaluronan Synthase by Mutation
J. Biol. Chem.,
May 23, 2003;
278(22):
19808 - 19814.
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J. T. Posey, M. S. Soloway, S. Ekici, M. Sofer, F. Civantos, R. C. Duncan, and V. B. Lokeshwar
Evaluation of the Prognostic Potential of Hyaluronic Acid and Hyaluronidase (HYAL1) for Prostate Cancer
Cancer Res.,
May 15, 2003;
63(10):
2638 - 2644.
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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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