|COPE Homepage||Bottom of page||Previous entry:
Teratocarcinoma-derived growth factor-3
please help me to continue my work.
Make a donation you can afford.
[receptor for hyaluronic acid-mediated motility; Receptor for HA-Mediated Motility] The approved gene symbol is HMMR [hyaluran-mediated motility receptor].
RHAMM has been identified as one of the cell surface receptors for hyaluronan by Hardwick et al (1992). Entwiste et al (1995) have characterized the murine gene.
Hyaluronan is a ubiquitous component of the extracellular matrix that also occurs transiently in the nucleus and cytoplasm. It mediates promotion of cell motility, adhesion, and proliferation by interacting with one of its receptors (CD44, RHAMM, and ICAM-1) (Entwistle et al, 1996). Binding of hyaluronan to RHAMM promotes cell migration in association with tyrosine phosphorylation and focal adhesion turnover (Hall et al, 1994). Blockade of either hyaluronan or RHAMM inhibits fibroblast motility stimulated by TGF-beta-1 (Samuel et al, 1993), and macrophage motility after bleomycin-lung injury (Zaman et al, 2005).
Foley et al (2012) have reported that macrophage chemotaxis stimulated by SP-A [surfactant protein A] requires RHAMM and also TLR-2, TGF-beta, and hyaluronan. This pathway of innate immune response regulation involves SPA stimulation via TLR-2, which drives TGF-beta-1 production that, in turn, stimulates macrophage chemotaxis in a manner dependent on RHAMM and hyaluronan.
Turley et al (1993) have reported that RHAMM is not detectable on most normal B-cells located in blood, spleen, or lymph node, but it is detectable on bone marrow and thymic B-cells and a variety of malignant B-cells, including multiple myeloma cells, where it may play a role in malignant invasion and metastatic growth (Pilarski et al, 1994). Crainie et al (1999) have reported that splice variants of RHAMM, designated RHAMMFL, RHAMM-48, and RHAMM-147, are overexpressed in multiple myeloma cells and other B-lymphocyte malignancies relative to resting B-cells or B-cells activated in vivo, raising the possibility that RHAMM and its variants may contribute to the malignant process. Maxwell et al (2004) have reported that RHAMM expression and isoform balance predict aggressive disease and poor survival in multiple myeloma.
RHAMM is expressed also on a subset of thymocytes. Mature peripheral T-cells from blood, spleen, and lymph nodes do not normally express RHAMM but transiently express RHAMM upon culture with PHA, PMA, or IL2. Stimulation by mitogenic CD2 antibodies with or without CD28 antibody cease to express RHAMM (Pilarski et al, 1993).
Turley et al (1994) have reported expression of RHAMM on astrocytes and microglial cells, showing also that these cells exhibit RHAMM-dependent motility. Lynn et al (2001) have reported expression of RHAMM in neurons and oligodendrocytes. Nagy et al (1995) have reported expression of RHAMM on neurons and a participation of RHAMM in the mediation of neurite motility and migration. RHAMM may be important also in the growth and/or regenerative capacity of central noradrenergic fibers originating from the locus coeruleus (Nagy et al, 1998). Lynn et al (2001) have localized RHAMM to mitochondria in neurons. RHAMM binds calmodulin and may be involved calmodulin-mediated cell signaling to cytoskeletal elements and/or mitochondria.
Ahrens et al (2000) have reported that the expression of RHAMM is increased during melanoma progression but that CD44 is the principal hyaluronic acid surface receptor on melanoma cells.
Savani et al (1995) have reported expression of RHAMM on bovine aortic smooth muscle cells and an involvement of the receptor in cell migration after wounding injury. Lokeshwar and Selzer (2000) have reported that RHAMM is a functional hyaluronic acid receptor on some types of endothelial cells of different vascular origin.
Assmann et al (1998) have described the expression of two human alternatively spliced RHAMM isoforms in human breast carcinoma cell lines. These forms are not expressed on the cell surface but intracellularly and do not seem to function as conventional motility receptors for hyaluronan in human breast cancer cells. Assmann et al (1998) have suggested the term IHABP [intracellular hyaluronic acid binding protein] for RHAMM. Note: the IHABP gene described by Hofmann et al (1998) is identical with the HABP4 [hyaluronan binding protein 4], but IHABP is listed in some databanks as a synonym for RHAMM.
Zhou et al (2002) have identified a 86 kDa and a 70 kDa isoform of RHAMM that are expressed in a tumor-specific manner in astrocytomas, where they associate with microtubules.
Tolg et al (2003) have implicated RHAMM in aggressive fibromatosis (desmoid tumor), a locally invasive soft tissue neoplasm. As shown by the study of RHAMM knock-out mice, loss of RHAMM attenuates the formation of such tumors.
In the nomenclature of CD antigens RHAMM has been given the designation CD168.
For additional information on CD antigens see also: CD antigens MiniCOPE Dictionary.
Copyright © 2012 by H IBELGAUFTS. All rights reserved.
ENTRY LAST MODIFIED: July 2012
See REFERENCES for entry RHAMM.
Click BACKLINKS to see which COPE entries contain the term RHAMM .
|COPE Homepage||Top of Page|
|SUPPORT COPE | Intro | Subdictionaries | New Entries | Contribute data | COPE Credentials|
|COPE is interested in contacts with corporate sponsors appreciating and committed to communication biology|