RANK
| RANK | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 587 amino acids | |
| Secondary to quaternary structure | single pass membrane protein | |
| Identifier | ||
| Gene name | TNFRSF11A | |
| External IDs | ||
| Occurrence | ||
| Parent taxon | Mammals | |
When R preceptor A ctivator of N F- κ B ( RANK ) is a transmembrane protein , which on the outer cell membrane of mature and adult osteoclasts (ie cells that break down bone) expressed is and together with its ligand RANKL ( R preceptor a ctivator of N F- κ B L igand) and a further regulator protein osteoprotegerin (OPG) is a key role in the regulation of bone remodeling takes. RANK is found in mammals . When people can mutations in TNFRSF11A - gene for familial osteopetrosis , osteolysis or Paget's disease of bone lead.
The osteoclast activity is controlled via several, sometimes very complex regulatory mechanisms. One is the activation or expression of so-called RANK receptors and RANK ligands. The signaling molecule RANKL secreted by bone-building osteoblasts binds to the membrane receptor of macrophages. Through this coupling of the RANKL, the macrophages differentiate into osteoclasts. This process can be antagonized by the OPG secreted by the osteoblasts . OPG is the natural opponent for RANKL. The OPG prevents the RANKL from attaching to the RANK receptor on the macrophage surface. In this way, the osteoblasts own production of osteoprotegerin counteracts osteoclast differentiation via the RANKL pathway.
Estrogens are described as a natural suppressor of RANKL . This explains the frequency of osteoporosis in postmenopausal women, as the natural suppressor of osteoclast differentiation (estrogen) is no longer available in sufficient quantities.
literature
- JC Rosen: Restoring aging bones. In: Scientific American. March 1, 2003, pp. 47-53.
- Clifford J. Rosen (Ed.): Osteoporosis. Diagnostic and Therapeutic Principles. Humana Press, Totowa, NJ, 1996, ISBN 0-89603-374-0 .
swell
- ↑ Homologues at OMA
- ↑ B. Zdzisinska, M. Kandefer-Szerszen: The role of RANK / RANKL and OPG in multiple myeloma. In: Postepy Hig Med Dosw. 60, 2006, pp. 471-482. PMID 17013366 .
- ↑ AR Pettit et al .: RANKL protein is expressed at the pannus-bone interface at sites of articular bone erosion in rheumatoid arthritis. In: Rheumatology . 45, 2006, pp. 1068-1076. PMID 16490750 .
- ↑ UniProt Q9Y6Q6