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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/01/10 02:47:28」(JST)

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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.^[1]

Composition

Biglycan consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains consisting of either chondroitin sulfate (CS) or 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.^[2] 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.^[3]

Nomenclature

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).^[4]

Diversity

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.

Interactions

Biglycan interacts with collagen, both via the core protein and GAG chains.^[5]^[6] It has been reported that biglycan interacts more strongly with collagen type II than collagen type I.^[7]^[8] Biglycan has been reported to compete with decorin for the same binding site on collagen.^[5]

Similarity to decorin

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

Function

Biglycan is believed to play a role in the mineralisation of bone. Knock-out mice that have had the gene for biglycan suppressed 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 growth factors BMP-4 and influences its bioactivity.^[11] It has also been reported that the presence of biglycan is necessary for BMP-4 to exert its effects on osteoblasts.^[12] There is also evidence that biglycan binds to TGF-beta 1

Interactions

Biglycan has been shown to interact with SGCA.^[13]

References

^ Traupe H, van den Ouweland AM, van Oost BA, Vogel W, Vetter U, Warren ST et al. (June 1992). "Fine mapping of the human biglycan (BGN) gene within the Xq28 region employing a hybrid cell panel". Genomics 13 (2): 481–3. doi:10.1016/0888-7543(92)90279-2. PMID 1612609.
^ Roughley PJ, White RJ (September 1989). "Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II". The Biochemical Journal 262 (3): 823–7. PMC 1133347. PMID 2590169.
^ Roughley PJ, White RJ, Magny MC, Liu J, Pearce RH, Mort JS (October 1993). "Non-proteoglycan forms of biglycan increase with age in human articular cartilage". The Biochemical Journal 295 (2): 421–6. PMC 1134898. PMID 8240239.
^ Fisher LW, Termine JD, Young MF (March 1989). "Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species". The Journal of Biological Chemistry 264 (8): 4571–6. PMID 2647739.
^ ^a ^b Schönherr E, Witsch-Prehm P, Harrach B, Robenek H, Rauterberg J, Kresse H (February 1995). "Interaction of biglycan with type I collagen". The Journal of Biological Chemistry 270 (6): 2776–83. doi:10.1074/jbc.270.6.2776. PMID 7852349.
^ Pogány G, Hernandez DJ, Vogel KG (August 1994). "The in vitro interaction of proteoglycans with type I collagen is modulated by phosphate". Archives of Biochemistry and Biophysics 313 (1): 102–11. doi:10.1006/abbi.1994.1365. PMID 8053669.
^ Vynios DH, Papageorgakopoulou N, Sazakli H, Tsiganos CP (September 2001). "The interactions of cartilage proteoglycans with collagens are determined by their structures". Biochimie 83 (9): 899–906. doi:10.1016/S0300-9084(01)01332-3. PMID 11698112.
^ Bidanset DJ, Guidry C, Rosenberg LC, Choi HU, Timpl R, Hook M (March 1992). "Binding of the proteoglycan decorin to collagen type VI". The Journal of Biological Chemistry 267 (8): 5250–6. PMID 1544908.
^ Cheng F, Heinegård D, Malmström A, Schmidtchen A, Yoshida K, Fransson LA (October 1994). "Patterns of uronosyl epimerization and 4-/6-O-sulphation in chondroitin/dermatan sulphate from decorin and biglycan of various bovine tissues". Glycobiology 4 (5): 685–96. doi:10.1093/glycob/4.5.685. PMID 7881183.
^ Xu T, Bianco P, Fisher LW, Longenecker G, Smith E, Goldstein S et al. (September 1998). "Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice". Nature Genetics 20 (1): 78–82. doi:10.1038/1746. PMID 9731537.
^ Moreno M, Muñoz R, Aroca F, Labarca M, Brandan E, Larraín J (April 2005). "Biglycan is a new extracellular component of the Chordin-BMP4 signaling pathway". The EMBO Journal 24 (7): 1397–405. doi:10.1038/sj.emboj.7600615. PMC 1142540. PMID 15775969.
^ Chen XD, Fisher LW, Robey PG, Young MF (June 2004). "The small leucine-rich proteoglycan biglycan modulates BMP-4-induced osteoblast differentiation". The FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology 18 (9): 948–58. doi:10.1096/fj.03-0899com. PMID 15173106.
^ Bowe MA, Mendis DB, Fallon JR (2000). "The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle.". J Cell Biol 148 (4): 801–10. doi:10.1083/jcb.148.4.801. PMC 2169361. PMID 10684260.

External links

biglycan at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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English Journal

Potential use of human adipose mesenchymal stromal cells for intervertebral disc regeneration: a preliminary study on biglycan-deficient murine model of chronic disc degeneration.

Marfia G, Campanella R, Navone S, Zucca I, Scotti A, Figini M, Di Vito C, Alessandri G, Riboni L, Parati E.
Arthritis research & therapy.Arthritis Res Ther.2014 Oct 8;16(5):457. [Epub ahead of print]
IntroductionBiglycan is an important proteoglycan of the extracellular matrix of intervertebral disc (IVD), and its decrease with aging has been correlated with IVD degeneration. Biglycan deficient (Bgn ¿/0) mice lack this protein and undergo spontaneous IVD degeneration with aging, thus representi
PMID 25293819

Asymmetric cell-matrix and biomechanical abnormalities in elastin insufficiency induced aortopathy.

Krishnamurthy VK1, Evans AN, Wansapura JP, Osinska H, Maddy KE, Biechler SV, Narmoneva DA, Goodwin RL, Hinton RB.
Annals of biomedical engineering.Ann Biomed Eng.2014 Oct;42(10):2014-28. doi: 10.1007/s10439-014-1072-y. Epub 2014 Aug 7.
Aortopathy is characterized by vascular smooth muscle cell (VSMC) abnormalities and elastic fiber fragmentation. Elastin insufficient (Eln (+/-) ) mice demonstrate latent aortopathy similar to human disease. We hypothesized that aortopathy manifests primarily in the aorto-pulmonary septal (APS) side
PMID 25099772

Extracellular matrix components of oral mucosa differ from skin and resemble that of foetal skin.

Glim JE1, Everts V2, Niessen FB3, Ulrich MM4, Beelen RH5.
Archives of oral biology.Arch Oral Biol.2014 Oct;59(10):1048-55. doi: 10.1016/j.archoralbio.2014.05.019. Epub 2014 Jun 16.
OBJECTIVE: Wounds of both the oral mucosa and early-to-mid gestation foetuses have a propensity to heal scarless. Repair of skin wounds in adults, however, regularly results in scar formation. The extracellular matrix (ECM) plays an important role in the process of healing. The fate of scarless or s
PMID 24973518

Japanese Journal

Identification, cDNA cloning, and expression analysis of dermatopontin in the goldfish Carassius auratus

Komatsu Norihiko,Ogawa Nobuhiro,Iimura Kurin [他]
Fisheries science 80(6), 1249-1256, 2014-11
NAID 40020282194

Biglycan は腫瘍血管内皮における新規血管新生関連因子である

山本和幸,大賀則孝,樋田泰浩,間石奈湖,川本泰輔,秋山廣輔,大澤崇宏,近藤美弥子,加賀基知三,平野聡,篠原信雄,進藤正信,樋田京子
北海道醫學雜誌 = Acta medica Hokkaidonensia 88(2), 103, 2013-04-01
NAID 10031165903

ISO-1-2 Tumor-Stromal interaction-the role of extracellular matrix protein, Biglycan, in shaping the high-grade serous ovarian cancer progression(Group 1 Oncology 1,IS Award Candidate,International Session)

Tsai Ching-Chou,Carroll Amy,Yeung Tsz-Lun,Leung Cecilia,Wong Kwong-Kwok,Mok Samuel C.
日本産科婦人科學會雜誌 65(2), 973, 2013-02-01
NAID 110009639659

「ビグリカン」

Biglycan
	; PDB rendering based on 2ft3.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	2ft3
Identifiers
Symbols	BGN ; DSPG1; PG-S1; PGI; SLRR1A
External IDs	OMIM: 301870 MGI: 88158 HomoloGene: 1293 GeneCards: BGN Gene
Gene ontology
Molecular function	• extracellular matrix structural constituent; • glycosaminoglycan binding; • extracellular matrix binding;
Cellular component	• extracellular region; • proteinaceous extracellular matrix; • Golgi lumen; • cell surface; • transport vesicle; • extracellular matrix; • sarcolemma; • lysosomal lumen; • extracellular vesicular exosome;
Biological process	• blood vessel remodeling; • carbohydrate metabolic process; • biological_process; • peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; • extracellular matrix organization; • glycosaminoglycan metabolic process; • chondroitin sulfate metabolic process; • chondroitin sulfate biosynthetic process; • chondroitin sulfate catabolic process; • dermatan sulfate biosynthetic process; • small molecule metabolic process;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

英: biglycan
同: プロテオグリカンI, proteoglycan I, PG-I

[pmid1612609-1] Traupe H, van den Ouweland AM, van Oost BA, Vogel W, Vetter U, Warren ST et al. (June 1992). "Fine mapping of the human biglycan (BGN) gene within the Xq28 region employing a hybrid cell panel". Genomics 13 (2): 481–3. doi:10.1016/0888-7543(92)90279-2. PMID 1612609.

[pmid2590169-2] Roughley PJ, White RJ (September 1989). "Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II". The Biochemical Journal 262 (3): 823–7. PMC 1133347. PMID 2590169.

[pmid8240239-3] Roughley PJ, White RJ, Magny MC, Liu J, Pearce RH, Mort JS (October 1993). "Non-proteoglycan forms of biglycan increase with age in human articular cartilage". The Biochemical Journal 295 (2): 421–6. PMC 1134898. PMID 8240239.

[pmid2647739-4] Fisher LW, Termine JD, Young MF (March 1989). "Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species". The Journal of Biological Chemistry 264 (8): 4571–6. PMID 2647739.

[pmid7852349-5] Schönherr E, Witsch-Prehm P, Harrach B, Robenek H, Rauterberg J, Kresse H (February 1995). "Interaction of biglycan with type I collagen". The Journal of Biological Chemistry 270 (6): 2776–83. doi:10.1074/jbc.270.6.2776. PMID 7852349.

[pmid8053669-6] Pogány G, Hernandez DJ, Vogel KG (August 1994). "The in vitro interaction of proteoglycans with type I collagen is modulated by phosphate". Archives of Biochemistry and Biophysics 313 (1): 102–11. doi:10.1006/abbi.1994.1365. PMID 8053669.

[pmid11698112-7] Vynios DH, Papageorgakopoulou N, Sazakli H, Tsiganos CP (September 2001). "The interactions of cartilage proteoglycans with collagens are determined by their structures". Biochimie 83 (9): 899–906. doi:10.1016/S0300-9084(01)01332-3. PMID 11698112.

[pmid1544908-8] Bidanset DJ, Guidry C, Rosenberg LC, Choi HU, Timpl R, Hook M (March 1992). "Binding of the proteoglycan decorin to collagen type VI". The Journal of Biological Chemistry 267 (8): 5250–6. PMID 1544908.

[pmid7881183-9] Cheng F, Heinegård D, Malmström A, Schmidtchen A, Yoshida K, Fransson LA (October 1994). "Patterns of uronosyl epimerization and 4-/6-O-sulphation in chondroitin/dermatan sulphate from decorin and biglycan of various bovine tissues". Glycobiology 4 (5): 685–96. doi:10.1093/glycob/4.5.685. PMID 7881183.

[pmid9731537-10] Xu T, Bianco P, Fisher LW, Longenecker G, Smith E, Goldstein S et al. (September 1998). "Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice". Nature Genetics 20 (1): 78–82. doi:10.1038/1746. PMID 9731537.

[pmid15775969-11] Moreno M, Muñoz R, Aroca F, Labarca M, Brandan E, Larraín J (April 2005). "Biglycan is a new extracellular component of the Chordin-BMP4 signaling pathway". The EMBO Journal 24 (7): 1397–405. doi:10.1038/sj.emboj.7600615. PMC 1142540. PMID 15775969.

[pmid15173106-12] Chen XD, Fisher LW, Robey PG, Young MF (June 2004). "The small leucine-rich proteoglycan biglycan modulates BMP-4-induced osteoblast differentiation". The FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology 18 (9): 948–58. doi:10.1096/fj.03-0899com. PMID 15173106.

[pmid10684260-13] Bowe MA, Mendis DB, Fallon JR (2000). "The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle.". J Cell Biol 148 (4): 801–10. doi:10.1083/jcb.148.4.801. PMC 2169361. PMID 10684260.

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biglycan

Wikipedia preview

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Contents

Composition

Nomenclature

Diversity

Interactions

Similarity to decorin

Function

Interactions

References

External links

UpToDate Contents

English Journal

Japanese Journal

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「ビグリカン」