MFGE8

MFGE8
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases MFGE8, milk fat globule-EGF factor 8 protein, BA46, EDIL1, HMFG, HsT19888, MFG-E8, MFGM, OAcGD3S, SED1, SPAG10, hP47
External IDs MGI: 102768 HomoloGene: 4334 GeneCards: MFGE8
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

4240

17304

Ensembl

ENSG00000140545

ENSMUSG00000030605

UniProt

Q08431

P21956

RefSeq (mRNA)

NM_001114614
NM_001310319
NM_001310320
NM_001310321
NM_005928

NM_001045489
NM_008594

RefSeq (protein)

NP_001108086.1
NP_001297248.1
NP_001297249.1
NP_001297250.1
NP_005919.2

NP_032620.2

Location (UCSC) Chr 15: 88.9 – 88.91 Mb Chr 7: 79.13 – 79.15 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Milk fat globule-EGF factor 8 protein (Mfge8), also known as lactadherin, is a protein which in humans is encoded by the MFGE8 gene.[3][4]

Species distribution

Mfge8 is secreted protein found in vertebrates, including mammals as well as birds.

Function

MFGE8 may function as a cell adhesion protein to connect smooth muscle to elastic fiber in arteries.[5] An amyloid fragment of MFGE8 known as medin accumulates in the aorta with aging.[6] MFGE8 in the vasculature of adults can induce recovery from ischemia by facilitating angiogenesis.[7] It has been suggested that antagonizing MFGE8-induced angiogenesis could be a way of fighting cancer.[8]

MFGE8 contains a phosphatidylserine (PS) binding domain, as well as an Arginine-Glycine-Aspartic acid motif, which enables the binding to integrins. MFGE8 binds PS, which is exposed on the surface of apoptotic cells. Opsonization of the apoptotic cells and binding to integrins on the surface of phagocytic cells, mediates the engulfment of the dead cell.

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. "Entrez Gene: MFGE8 milk fat globule-EGF factor 8 protein".
  4. Collins C, Nehlin JO, Stubbs JD, Kowbel D, Kuo WL, Parry G (January 1997). "Mapping of a newly discovered human gene homologous to the apoptosis associated-murine mammary protein, MFG-E8, to chromosome 15q25". Genomics. 39 (1): 117–8. doi:10.1006/geno.1996.4425. PMID 9027496.
  5. Larsson A, Peng S, Persson H, Rosenbloom J, Abrams WR, Wassberg E, Thelin S, Sletten K, Gerwins P, Westermark P (June 2006). "Lactadherin binds to elastin--a starting point for medin amyloid formation?". Amyloid. 13 (2): 78–85. doi:10.1080/13506120600722530. PMID 16911961.
  6. Peng S, Glennert J, Westermark P (June 2005). "Medin-amyloid: a recently characterized age-associated arterial amyloid form affects mainly arteries in the upper part of the body". Amyloid. 12 (2): 96–102. doi:10.1080/13506120500107006. PMID 16011985.
  7. Silvestre JS, Théry C, Hamard G, Boddaert J, Aguilar B, Delcayre A, Houbron C, Tamarat R, Blanc-Brude O, Heeneman S, Clergue M, Duriez M, Merval R, Lévy B, Tedgui A, Amigorena S, Mallat Z (May 2005). "Lactadherin promotes VEGF-dependent neovascularization". Nat. Med. 11 (5): 499–506. doi:10.1038/nm1233. PMID 15834428.
  8. Raymond A, Ensslin MA, Shur BD (April 2009). "SED1/MFG-E8: a bi-motif protein that orchestrates diverse cellular interactions". J. Cell. Biochem. 106 (6): 957–66. doi:10.1002/jcb.22076. PMC 2742659Freely accessible. PMID 19204935.

Further reading


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