Neuropilin-1 and Leucine-rich Repeat containing Protein 15

Neuropilin-1 and Leucine-rich Repeat containing Protein 15
Andere Namen

LRRC15, LIB, Leucine rich repeat containing 15

Masse/Länge Primärstruktur 581 Aminosäuren, 64.366 Da
Bezeichner
Externe IDs
Vorkommen
Homologie-Familie Hovergen
Orthologe
Mensch Maus
Entrez 131578 74488
Ensembl ENSG00000172061 ENSMUSG00000052316
UniProt Q8TF66 Q80X72
Refseq (mRNA) NM_130830 NM_028973
Refseq (Protein) NP_570843 NP_083249
PubMed-Suche 131578 74488

Neuropilin-1 and Leucine-rich Repeat containing Protein 15 (LRRC15) ist ein Membranprotein und Resistenzfaktor, das als Reaktion auf Tumoren und virale Infektionen vermehrt gebildet wird. Vermutlich ist LLRC15 beteiligt an der Resistenz gegen schwere Verläufe einer Infektion mit SARS-CoV-2.[1][2][3]

Eigenschaften

LRRC15 dient Zell-Zell-Kontakten und der Bindung an die extrazelluläre Matrix.[4] In normalen Geweben wird LLRC15 kaum gebildet.[5] Dagegen tritt es in Anwesenheit von Tumoren sowohl in den umgebenden Fibroblasten als auch auf manchen Tumorzellen mesenchymalen Ursprungs auf (Sarkom, Melanom, Glioblastom).[5] Daher wird LRRC15 zur Behandlung von Tumoren untersucht.[4] Das Spike-Glykoprotein von SARS-CoV-2 bindet an LRRC15.[6] Nach Bindung an LRRC15 unterdrückt LRRC15 die Biosynthese von Kollagen und fördert die Biosynthese von verschiedenen antiviralen Proteinen wie IFIT, OAS und Proteinen der Mx-Familie.[7]

LRRC15 bindet von der extrazellulären Matrix Laminin, Fibronectin und Kollagen.[8] Die Genexpression von LRRC15 wird durch den Botenstoff der Immunantwort TGF-β induziert.[5]

Struktur

LRRC15 besteht zum größten Teil aus parallel angeordneten β-Faltblatt-Strukturen.[8] Das Signalpeptid am N-Terminus (Position 1–21) wird durch Proteasen abgespalten.[9] Die mit Abstand größte Proteindomäne liegt extrazellulär (22–538), wohingegen die Transmembrandomäne (539–559) und die intrazelluläre Proteindomäne (560–581) deutlich kürzer sind.[9] Es ist an N75 und N369 glykosyliert.[8] Der Name stammt von 17 Leucine-rich Repeats in der extrazellulären Domäne.[9]

Einzelnachweise

  1. ↑ Studie aus Australien, veröffentlicht bei Plos Biology
  2. ↑ Studie aus Cambridge (UK), veröffentlicht bei Plos Biology
  3. ↑ Studie der Brown University (USA), veröffentlicht bei Plos Biology
  4. ↑ a b U. Ray, C. L. Pathoulas, P. Thirusangu, J. W. Purcell, N. Kannan, V. Shridhar: Exploiting LRRC15 as a Novel Therapeutic Target in Cancer. In: Cancer Research. Band 82, Nummer 9, Mai 2022, S. 1675–1681, doi:10.1158/0008-5472.CAN-21-3734, PMID 35260879, PMC 9064950 (freier Volltext).
  5. ↑ a b c J. W. Purcell, S. G. Tanlimco, J. Hickson, M. Fox, M. Sho, L. Durkin, T. Uziel, R. Powers, K. Foster, T. McGonigal, S. Kumar, J. Samayoa, D. Zhang, J. P. Palma, S. Mishra, D. Hollenbaugh, K. Gish, S. E. Morgan-Lappe, E. D. Hsi, D. T. Chao: LRRC15 Is a Novel Mesenchymal Protein and Stromal Target for Antibody-Drug Conjugates. In: Cancer Research. Band 78, Nummer 14, Juli 2018, S. 4059–4072, doi:10.1158/0008-5472.CAN-18-0327, PMID 29764866.
  6. ↑ R. L. Berkowitz, D. A. Ostrov: The Elusive Coreceptors for the SARS-CoV-2 Spike Protein. In: Viruses. Band 15, Nummer 1, Dezember 2022, S. , doi:10.3390/v15010067, PMID 36680105, PMC 9862613 (freier Volltext).
  7. ↑ Lipin Loo, Matthew A. Waller, Cesar L. Moreno, Alexander J. Cole, Alberto Ospina Stella, Oltin-Tiberiu Pop, Ann-Kristin Jochum, Omar Hasan Ali, Christopher E. Denes, Zina Hamoudi, Felicity Chung, Anupriya Aggarwal, Jason K. K. Low, G. Gregory Neely: Fibroblast-expressed LRRC15 is a receptor for SARS-CoV-2 spike and controls antiviral and antifibrotic transcriptional programs. In: PLOS Biology, 9. Februar 2023. doi:10.1371/journal.pbio.3001967.
  8. ↑ a b c GeneCards: LLRC15. In: genecards.org. Abgerufen am 11. Februar 2023.
  9. ↑ a b c Uniprot: UniProt LRC15_HUMAN. In: uniprot.org. Abgerufen am 11. Februar 2023 (englisch).

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