CD30

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Tumor necrosis factor receptor superfamily, member 8
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TNFRSF8 ; CD30; D1S166E; Ki-1
External IDs OMIM153243 MGI99908 HomoloGene949 GeneCards: TNFRSF8 Gene
RNA expression pattern
PBB GE TNFRSF8 206729 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 943 21941
Ensembl ENSG00000120949 ENSMUSG00000028602
UniProt P28908 Q60846
RefSeq (mRNA) NM_001243 NM_009401
RefSeq (protein) NP_001234 NP_033427
Location (UCSC) Chr 1:
12.06 – 12.14 Mb
Chr 4:
145.27 – 145.32 Mb
PubMed search [1] [2]

CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor family and tumor marker.

Function

This receptor is expressed by activated, but not by resting, T and B cells. TRAF2 and TRAF5 can interact with this receptor, and mediate the signal transduction that leads to the activation of NF-kappaB. It is a positive regulator of apoptosis, and also has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.[1]

Clinical significance

CD30 is associated with anaplastic large cell lymphoma. It is expressed in embryonal carcinoma but not in seminoma and is thus a useful marker in distinguishing between these germ cell tumors.[2] CD30 and CD15 are also expressed on classical Hodgkin Lymphoma Reed-Sternberg cells.[3]

Cancer treatment

CD30 is the target of the FDA approved therapeutic Brentuximab Vedotin (Adcetris), designed and developed by Seattle Genetics. It is approved for use in:

  1. Hodgkin lymphoma (HL) (brentuximab vedotin) after failure of autologous stem cell transplant (ASCT)
  2. HL in patients who are not ASCT candidates after failure of at least 2 multiagent chemotherapy regimens
  3. Systemic anaplastic large cell lymphoma (sALCL) after failure of at least 1 multiagent chemotherapy regimen[4]

Interactions

CD30 has been shown to interact with TRAF5,[5] TRAF1,[6] TRAF2[5][6] and TRAF3.[6]

References

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Further reading

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External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.