FRP-1 is described as a cell-fusion regulatory system composed of disulfide-linked heavy and light chains. The heavy chain is stated to be identical to 4F2/CD98 heavy chain and is described as multifunctional.
First-pass extracted concept
fusion regulatory protein-1
Aliases
4F2/CD98 heavy chain, FRP-1
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Evidence Snippets
Two molecules that regulate cell fusion have been identified and designated fusion regulatory protein-1 (FRP-1) and FRP-2. FRP-1 is a complex composed of a glycosylated heavy chain and a nonglycosylated light chain that are disulfide linked. FRP-1 heavy chain is identical to 4F2/CD98 heavy chain, whereas FRP-2 is identical to integrin alpha3 subunit.
Supporting Sources
Linked Claims
The FRP-1 system is involved in virus-mediated cell fusion and multinucleated giant cell formation of blood monocytes.
The FRP-1 heavy chain is a multifunctional molecule that acts as a fusion regulator, amino acid transporter, integrin regulator, comitogenic factor, Na+-Ca2+ exchanger, and oncogenic protein.
FRP-1 heavy chain is identical to 4F2/CD98 heavy chain.
Novel pathways for monocyte-dependent regulation of T-cell activation are mediated by the FRP-1 system.
FRP-1 light chains require association with the heavy chain to exhibit amino acid transport activity.
Monoclonal antibodies against human FRP-1 heavy chain induce polykaryocytes that have properties as osteoclasts.
FRP-1 is a complex of a glycosylated heavy chain and a nonglycosylated light chain that are disulfide linked.