Biglycan

Source: Wikipedia, the free encyclopedia.
BGN
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Ensembl

ENSG00000182492

ENSMUSG00000031375

UniProt

P21810

P28653

RefSeq (mRNA)

NM_001711

NM_007542

RefSeq (protein)

NP_001702

NP_031568

Location (UCSC)Chr X: 153.49 – 153.51 MbChr X: 72.53 – 72.54 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Biglycan is a small leucine-rich repeat proteoglycan (SLRP) which is found in a variety of extracellular matrix tissues, including bone, cartilage and tendon. In humans, biglycan is encoded by the BGN gene[5] which is located on the X chromosome.

The name "biglycan" was proposed in an article by Fisher, Termine and Young in an article in the Journal of Biological Chemistry in 1989 because the proteoglycan contained two GAG chains; formerly it was known as proteoglycan-I (PG-I).[6]

Structure

Biglycan consists of a protein core containing leucine-rich repeat regions and two

dermatan sulfate (DS), with DS being more abundant in most connective tissues. The CS/DS chains are attached at amino acids 5 and 10 in human biglycan.[7] The composition of the GAG chains has been reported as varying according to tissue of origin. Non-glycanated forms of biglycan (no GAG chains) increase with age in human articular cartilage.[8]

The composition of GAG chains of biglycan and decorin originating from the same tissue has been reported to be similar.[9]

The structure of biglycan core protein is highly conserved across species; over 90% homology has been reported for rat, mouse, bovine and human biglycan core proteins.

Function

Biglycan is believed to play a role in the mineralization of bone.

Knock-out mice that have had the gene for biglycan suppressed (Bgn -/-) have an osteoporosis-like phenotype with reduced growth rate and lower bone mass than mice that can express biglycan.[10]

Biglycan core protein binds to the

TGF-beta 1
.

Interactions

Biglycan interacts with

collagen type I.[15][16] Biglycan has been reported to compete with decorin for the same binding site on collagen.[13]

Biglycan has been shown to

interact with SGCA.[17]

Biglycan is a particularly important proteoglycan for binding to lipoprotein in human blood vessels, thus being a significant cause of atherosclerosis.[18]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000182492 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031375 – Ensembl, 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. PMID 1612609
    .
  6. PMID 2647739
    .
  7. PMID 2590169
    .
  8. PMID 8240239
    .
  9. PMID 7881183
    .
  10. S2CID 8383857
    .
  11. PMID 15775969
    .
  12. S2CID 30042377
    .
  13. ^
    PMID 7852349
    .
  14. PMID 8053669
    .
  15. PMID 11698112
    .
  16. PMID 1544908.[permanent dead link
    ]
  17. PMID 10684260
    .
  18. PMID 22176921
    .

External links
Retrieved from "https://en.wikipedia.org/w/index.php?title=Biglycan&oldid=1214468561"