Basigin

Source: Wikipedia, the free encyclopedia.
BSG
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Ensembl
UniProt
RefSeq (mRNA)

NM_001728
NM_198589
NM_198590
NM_198591
NM_001322243

NM_001077184
NM_009768

RefSeq (protein)

NP_001309172
NP_001719
NP_940991
NP_940992
NP_940993

NP_001070652
NP_033898

Location (UCSC)Chr 19: 0.57 – 0.58 MbChr 10: 79.54 – 79.55 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Basigin (BSG) also known as extracellular matrix metalloproteinase inducer (EMMPRIN) or cluster of differentiation 147 (CD147) is a protein that in humans is encoded by the BSG gene.[5][6][7] This protein is a determinant for the Ok blood group system. There are three known antigens in the Ok system; the most common being Oka (also called OK1), OK2 and OK3. Basigin has been shown to be an essential receptor on red blood cells for the human malaria parasite, Plasmodium falciparum.[8] The common isoform of basigin (basigin-2) has two immunoglobulin domains, and the extended form basigin-1 has three.[9]

Function

Basigin is a member of the immunoglobulin superfamily, with a structure related to the putative primordial form of the family. As members of the immunoglobulin superfamily play fundamental roles in intercellular recognition involved in various immunologic phenomena, differentiation, and development, basigin is thought also to play a role in intercellular recognition (Miyauchi et al., 1991; Kanekura et al., 1991).[10][11]

It has a variety of functions. In addition to its metalloproteinase-inducing ability, basigin also regulates several distinct functions, such as spermatogenesis, expression of the monocarboxylate transporter and the responsiveness of lymphocytes.[6] Basigin is a type I

leukocytes. The human basigin protein contains 269 amino acids that form two heavily glycosylated C2 type immunoglobulin-like domains at the N-terminal extracellular portion. A second form of basigin has also been characterized that contains one additional immunoglobulin-like domain in its extracellular portion.[6]

Interactions

Basigin has been shown to

Basigin has been shown to form a complex with monocarboxylate transporters in the retina of mice. Basigin appears to be required for proper placement of MCTs in the membrane. In the Basigin null mouse, the failure of MCTs to integrate with the membrane may be directly linked to a failure of nutrient transfer in the retinal pigmented epithelium (the lactates transported by MCTs 1, 3, and 4 are essential nutrients for the developing RPE), resulting in loss of sight in the null animal.[17]

Basigin interacts with the fourth

epithelial-mesenchymal transition[citation needed] suppressor complex that if disrupted results in the induction of invasive prostate epithelial cell behavior associated with poor prostate cancer survival.[19]

Modulators

It have been shown that

Statins altered CD147 expression, structure and function.[21]

Role in malaria

It has recently (November 2011) been found that basigin is a receptor that is essential to erythrocyte invasion by most strains of

Rh5, a better vaccine for malaria might be found.[8] Basigin is bound by the PfRh5 protein on the surface of the malaria parasite.[citation needed
]

Role in SARS-CoV-2 infection (COVID-19)

The host-cell-expressed basigin (CD147) may bind spike protein of SARS-CoV-2 and possibly be involved in host cell invasion.[22] Subsequently, meplazumab, a humanized anti-CD147 antibody, was tested in patients with SARS-CoV-2 pneumonia.[23]

Some of these claims have been challenged by another group of scientists who found no evidence of a direct role for basigin in either binding the viral spike protein or promoting lung cell infection.[24]

More recent studies suggests CD147 as SARS-CoV-2 entry receptor of platelets and megakaryocytes, leading to hyperactivation and thrombosis, that differs from common cold coronavirus CoV-OC43. Incubation of megakaryocyte cells with SARS-CoV-2 resulted in a significant increase in the proinflammatory transcripts LGALS3BP and S100A9. Notably, CD147 antibody-mediated blocking significantly reduced the expression of S100A9, and S100A8 on megakaryocytes following incubation with SARS-CoV-2. These data indicate that megakaryocytes and platelets actively take up SARS-CoV-2 virions, likely via an ACE-2-independent mechanism.[25]

Another study states that platelets challenged with SARS-CoV-2 undergo activation, dependent on the CD147 receptor.[26] Yet SARS-CoV-2 does not replicate in human platelets.

Yet another study describes high-interaction coupling of N-RBD of SARS-CoV-2 and CD147 as the main way of infecting

Acquired Immune Deficiency Syndrome.[27]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172270Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023175Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. S2CID 24602674
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  6. ^ .
  7. .
  8. ^ .
  9. ^ . Retrieved 13 February 2023.
  10. ^ "Entrez Gene: BSG basigin (Ok blood group)".
  11. S2CID 37384660
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  12. .
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  18. ^ "WikiGenes: MRC2 - mannose receptor C, type 2 Homo sapiens".
  19. S2CID 9946106
    .
  20. ^ Yi F, Jiang L, Xu H, Dai F, Zhou L. "Atorvastatin suppresses CD147 and MMP-3 expression and improves histological and neurological outcomes in an animal model of intracerebral hemorrhage" (PDF). International Journal of Clinical and Experimental Medicine. 11 (9): 9301–9311.
  21. PMID 29253870
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Further reading

External links