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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2013-01-29 02:27:10 UTC
HMDB IDHMDB00632
Secondary Accession Numbers
  • HMDB06265
Metabolite Identification
Common NameDermatan
DescriptionDermatan is a naturally occurring glycosaminoglycan found mostly in the skin and in connective tissue. It differs from chondroitin sulfate A (see chondroitin sulfateS) by containing Iduronic acid in place of glucuronic acid, its epimer, at carbon atom 5. (from Merck, 12th ed). Dermatan sulfate consists of sulfated N-acetylgalactosamine alternating with uronic acid residues. The latter are predominantly L-Iduronic acid, some of which are sulfated; there are also occasional glucuronic acid residues. Degradation proceeds stepwise from the nonreducing end by the sequential action of three exo-glycosidases (alpha-L-iduronidase, beta-glucuronidase, and beta-hexosaminidase) and two sulfatases (iduronate 2-sulfatase and N-acetylgalactosamine 4-sulfatase). An endoglycosidase, hyaluronidase, may also participate to a limited extent in the degradation process by cleaving next to the occasional glucuronic acid residues. -- OMMBID 136-2.
Structure
Thumb
Synonyms
  1. b-Heparin
  2. beta-Heparin
  3. Chondroitin sulfate B
  4. Chondroitin sulfate type B
  5. Chondroitin sulphate B
  6. Chondroitin sulphate type B
  7. Chondroitinsulfuric acid B
  8. Chondroitinsulfuric acid type B
  9. Dermatan 4-sulfate
  10. Dermatan 4-sulphate
  11. Dermatan hydrogen sulfate
  12. Dermatan hydrogen sulphate
  13. Dermatan sulfate
  14. Dermatan sulphate
  15. Desmin 370
  16. DS 435
  17. MF 701
Chemical FormulaNot Available
Average Molecular WeightNot Available
Monoisotopic Molecular WeightNot Available
IUPAC NameNot Available
Traditional IUPAC NameNot Available
CAS Registry Number24967-94-0
SMILES
InChI Identifier
InChI=1S/C18H31NO14S/c1-4-8-12(22)13(23)10(31-14(8)17(24)25)6-30-16-11(19-7(2)21)18(29-3)32-9(5-20)15(16)33-34(26,27)28/h8-16,18,20,22-23H,4-6H2,1-3H3,(H,19,21)(H,24,25)(H,26,27,28)/p-1/t8-,9+,10+,11+,12-,13-,14+,15-,16+,18+/m0/s1
InChI KeyDYTJJIPHSVVNGF-IPUVJUKZSA-M
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassCarbohydrates and Carbohydrate Conjugates
ClassDisaccharides
Sub ClassDihexoses
Other Descriptors
  • Aliphatic Heteropolycyclic Compounds
Substituents
  • 1,2 Diol
  • Acetal
  • Carboxamide Group
  • Carboxylic Acid
  • Dialkyl Ether
  • Glucosamine
  • Glycosyl Compound
  • Mannosamine
  • O Glycosyl Compound
  • Organic Sulfuric Acid Monoester
  • Oxane
  • Primary Alcohol
  • Secondary Alcohol
  • Secondary Carboxylic Acid Amide
  • Sulfate Ester
Direct ParentDihexoses
Ontology
StatusExpected and Not Quantified
Origin
  • Endogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locationsNot Available
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Spectra
SpectraNot Available
Biological Properties
Cellular LocationsNot Available
Biofluid LocationsNot Available
Tissue Location
  • Cartilage
  • Connective Tissue
  • Fibroblasts
  • Intestine
  • Kidney
  • Liver
  • Myelin
  • Neuron
  • Pancreas
  • Placenta
  • Platelet
  • Skin
  • Spleen
  • Testes
PathwaysNot Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB022153
KNApSAcK IDNot Available
Chemspider IDNot Available
KEGG Compound IDC00426
BioCyc IDCPD-7276
BiGG IDNot Available
Wikipedia LinkDermatan
NuGOwiki LinkHMDB00632
Metagene LinkHMDB00632
METLIN ID5605
PubChem Compound53477708
PDB IDNot Available
ChEBI IDNot Available
References
Synthesis ReferenceNagasawa, Kinzo; Inoue, Yuko. Desulfation of glycosaminoglycuronan sulfates. Methods in Carbohydrate Chemistry (1980), 8 287-9.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Longas MO, Wisch P, Lebwohl MG, Fleischmajer R: Glycosaminoglycans of skin and urine in pseudoxanthoma elasticum: evidence for chondroitin 6-sulfate alteration. Clin Chim Acta. 1986 Mar 28;155(3):227-36. Pubmed: 3085984
  2. Akimoto S, Hayashi H, Ishikawa H: Disaccharide analysis of the skin glycosaminoglycans in systemic sclerosis. Br J Dermatol. 1992 Jan;126(1):29-34. Pubmed: 1536759
  3. Habuchi H, Tsuji M, Nakanishi Y, Suzuki S: Separation and properties of five glycosaminoglycan sulfatases from rat skin. J Biol Chem. 1979 Aug 25;254(16):7570-8. Pubmed: 468769
  4. Ungefroren H, Ergun S, Krull NB, Holstein AF: Expression of the small proteoglycans biglycan and decorin in the adult human testis. Biol Reprod. 1995 May;52(5):1095-105. Pubmed: 7626709
  5. Sobel RA, Ahmed AS: White matter extracellular matrix chondroitin sulfate/dermatan sulfate proteoglycans in multiple sclerosis. J Neuropathol Exp Neurol. 2001 Dec;60(12):1198-207. Pubmed: 11764092
  6. Poulsen JH, Cramers MK: Dermatan sulphate in urine reflects the extent of skin affection in psoriasis. Clin Chim Acta. 1982 Dec 9;126(2):119-26. Pubmed: 6817946
  7. Minami R, Abo K, Tsugawa S, Oyanagi K, Nakao T: Acidic glycosaminoglycans in liver from five patients with mucopolysaccharidosis and mucolipidosis. Tohoku J Exp Med. 1981 Jun;134(2):215-20. Pubmed: 6797102
  8. Zimmermann DR, Dours-Zimmermann MT, Schubert M, Bruckner-Tuderman L, Heitz PU: [Expression of the extracellular matrix proteoglycan, versican, in human skin] Verh Dtsch Ges Pathol. 1994;78:481-4. Pubmed: 7534020
  9. Ji SL, Du HY, Chi YQ, Cui HF, Cao JC, Geng MY, Guan HS: Effects of dermatan sulfate derivatives on platelet surface P-selectin expression and protein C activity in blood of inflammatory bowel disease patients. World J Gastroenterol. 2004 Dec 1;10(23):3485-9. Pubmed: 15526370
  10. Orii T, Sukegawa K, Minami R, Matsuura Y, Tsugawa S: Atypical Hurler syndrome without alpha-L-iduronidase deficiency. Tohoku J Exp Med. 1976 Oct;120(2):113-23. Pubmed: 136068
  11. Grigoriu BD, Depontieu F, Scherpereel A, Gourcerol D, Devos P, Ouatas T, Lafitte JJ, Copin MC, Tonnel AB, Lassalle P: Endocan expression and relationship with survival in human non-small cell lung cancer. Clin Cancer Res. 2006 Aug 1;12(15):4575-82. Pubmed: 16899604
  12. Nagashima K, Endo H, Sakakibara K, Konishi Y, Miyachi K, Wey JJ, Suzuki Y, Onisawa J: Morphological and biochemical studies of a case of mucopolysaccharidosis II (Hunter's syndrome). Acta Pathol Jpn. 1976 Jan;26(1):115-32. Pubmed: 132078
  13. Wasserman L, Abramovici A, Shlesinger H, Goldman JA, Allalouf D: Histochemical localization of acidic glycosaminoglycans in normal human placentae. Placenta. 1983 Jan-Apr;4(1):101-8. Pubmed: 6406996
  14. Laitio M, Terho T: Polysaccharides of metaplastic mucosa and carcinoma of the gallbladder. Lab Invest. 1975 Feb;32(2):183-9. Pubmed: 46329
  15. Desnoyers L, Arnott D, Pennica D: WISP-1 binds to decorin and biglycan. J Biol Chem. 2001 Dec 14;276(50):47599-607. Epub 2001 Oct 11. Pubmed: 11598131
  16. Celie JW, Keuning ED, Beelen RH, Drager AM, Zweegman S, Kessler FL, Soininen R, van den Born J: Identification of L-selectin binding heparan sulfates attached to collagen type XVIII. J Biol Chem. 2005 Jul 22;280(29):26965-73. Epub 2005 May 24. Pubmed: 15917223
  17. Scott JE: Proteoglycan-collagen interactions. Ciba Found Symp. 1986;124:104-24. Pubmed: 3816415
  18. Burkhardt D, Michel BA, Baici A, Kissling R, Theiler R: Comparison of chondroitin sulphate composition of femoral head articular cartilage from patients with femoral neck fractures and osteoarthritis and controls. Rheumatol Int. 1995;14(6):235-41. Pubmed: 7597379
  19. Wasserman L, Shlesinger H, Goldman JA, Allalouf D: Pattern of glycosaminoglycan distribution in tissue and blood vessels of human placenta. Gynecol Obstet Invest. 1983;15(4):242-50. Pubmed: 6220947
  20. Melching LI, Roughley PJ: The synthesis of dermatan sulphate proteoglycans by fetal and adult human articular cartilage. Biochem J. 1989 Jul 15;261(2):501-8. Pubmed: 2775229

Enzymes

General function:
Involved in sulfotransferase activity
Specific function:
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Gene Name:
CHST11
Uniprot ID:
Q9NPF2
Molecular weight:
41002.97
General function:
Involved in sulfotransferase activity
Specific function:
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Gene Name:
CHST12
Uniprot ID:
Q9NRB3
Molecular weight:
48413.945
General function:
Involved in catalytic activity
Specific function:
Not Available
Gene Name:
ARSB
Uniprot ID:
P15848
Molecular weight:
Not Available
General function:
Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Specific function:
Plays an important role in the degradation of dermatan and keratan sulfates.
Gene Name:
GUSB
Uniprot ID:
P08236
Molecular weight:
74731.46
General function:
Carbohydrate transport and metabolism
Specific function:
Not Available
Gene Name:
IDUA
Uniprot ID:
P35475
Molecular weight:
Not Available
General function:
Involved in catalytic activity
Specific function:
Required for the lysosomal degradation of heparan sulfate and dermatan sulfate.
Gene Name:
IDS
Uniprot ID:
P22304
Molecular weight:
Not Available
General function:
Involved in sulfotransferase activity
Specific function:
Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. GlcUA to IdoUA. Appears to have an important role in the formation of the cerbellar neural network during postnatal brain development.
Gene Name:
CHST14
Uniprot ID:
Q8NCH0
Molecular weight:
42996.535
General function:
Involved in acetylglucosaminyltransferase activity
Specific function:
Catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes
Gene Name:
XYLT1
Uniprot ID:
Q86Y38
Molecular weight:
107568.4
General function:
Involved in acetylglucosaminyltransferase activity
Specific function:
Probably catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes. Its enzyme activity has not been demonstrated
Gene Name:
XYLT2
Uniprot ID:
Q9H1B5
Molecular weight:
96766.3
General function:
Involved in sulfotransferase activity
Specific function:
Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N-resulfated heparin
Gene Name:
UST
Uniprot ID:
Q9Y2C2
Molecular weight:
47672.6
General function:
Involved in sulfotransferase activity
Specific function:
Sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo.
Gene Name:
CHST15
Uniprot ID:
Q7LFX5
Molecular weight:
64925.66
General function:
Involved in metalloendopeptidase activity
Specific function:
Activates progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin
Gene Name:
MMP24
Uniprot ID:
Q9Y5R2
Molecular weight:
73230.9
General function:
Involved in chondroitin-glucuronate 5-epimerase activity
Specific function:
Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues.
Gene Name:
DSE
Uniprot ID:
Q9UL01
Molecular weight:
109772.235
General function:
Involved in serine-type endopeptidase activity
Specific function:
Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis
Gene Name:
KLK6
Uniprot ID:
Q92876
Molecular weight:
26855.5