関: chondroitin sulfate proteoglycan

WordNet

convert into a sulfate
a salt or ester of sulphuric acid (同)sulphate

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/02/22 15:30:00」(JST)

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Aggrecan, the major proteoglycan in cartilage, has 2316 amino acids

Proteoglycans are proteins^[1] that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s).^[2] The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate-GlcA-Gal-Gal-Xyl-PROTEIN). The Ser residue is generally in the sequence -Ser-Gly-X-Gly- (where X can be any amino acid residue but proline), although not every protein with this sequence has an attached glycosaminoglycan. The chains are long, linear carbohydrate polymers that are negatively charged under physiological conditions due to the occurrence of sulfate and uronic acid groups. Proteoglycans occur in the connective tissue.

Types

Proteoglycans are categorized by their relative size (large and small) and the nature of their glycosaminoglycan chains.^[3]

Types include:

Glycosaminoglycans	Small proteoglycans	Large proteoglycans
chondroitin sulfate/dermatan sulfate	decorin, 36 kDa biglycan, 38 kDa	versican, 260-370 kDa, present in many adult tissues including blood vessels and skin
heparan sulfate/chondroitin sulfate	testican, 44 kDa	perlecan, 400-470 kDa
chondroitin sulfate	bikunin, 25 kDa	neurocan, 136 kDa aggrecan, 220 kDa, the major proteoglycan in cartilage brevican, 145kDa
keratan sulfate	fibromodulin, 42 kDa lumican, 38 kDa

Certain members are considered members of the "small leucine-rich proteoglycan family" (SLRP).^[4] These include decorin, biglycan, fibromodulin and lumican.

Function

Proteoglycans are a major component of the animal extracellular matrix, the "filler" substance existing between cells in an organism. Here they form large complexes, both to other proteoglycans, to hyaluronan, and to fibrous matrix proteins (such as collagen). They are also involved in binding cations (such as sodium, potassium and calcium) and water, and also regulating the movement of molecules through the matrix. Evidence also shows they can affect the activity and stability of proteins and signalling molecules within the matrix.^{[citation needed]} Individual functions of proteoglycans can be attributed to either the protein core or the attached GAG chain. They can also serve as lubricants.

Synthesis

The protein component of proteoglycans is synthesized by ribosomes and translocated into the lumen of the rough endoplasmic reticulum. Glycosylation of the proteoglycan occurs in the Golgi apparatus in multiple enzymatic steps. First a special link tetrasaccharide is attached to a serine side chain on the core protein to serve as a primer for polysaccharide growth. Then sugars are added one at a time by glycosyl transferase. The completed proteoglycan is then exported in secretory vesicles to the extracellular matrix of the tissue.

Clinical Significance

An inability to break down proteoglycans is characteristic of a group of genetic disorders, called mucopolysaccharidoses. The inactivity of specific lysosomal enzymes that normally degrade glycosaminoglycans leads to the accumulation of proteoglycans within cells. This leads to a variety of disease symptoms, depending upon the type of proteoglycan that is not degraded.

References

^ Proteoglycans at the US National Library of Medicine Medical Subject Headings (MeSH)
^ Gerhard Meisenberg; William H. Simmons (2006). Principles of medical biochemistry. Elsevier Health Sciences. pp. 243–. ISBN 978-0-323-02942-1. Retrieved 6 February 2011.
^ Iozzo, RV; Schaefer, L (March 2015). "Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.". Matrix biology : journal of the International Society for Matrix Biology. 42: 11–55. doi:10.1016/j.matbio.2015.02.003. PMID 25701227.
^ Hans-Joachim Gabius; Sigrun Gabius (February 2002). Glycosciences: Status and Perspectives. John Wiley and Sons. pp. 209–. ISBN 978-3-527-30888-0. Retrieved 6 February 2011.

External links

Diagram at nd.edu

UpToDate Contents

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English Journal

Expression of chondroitin/dermatan sulfate glycosyltransferases during early zebrafish development.

Filipek-Górniok B, Holmborn K, Haitina T, Habicher J, Oliveira MB, Hellgren C, Eriksson I, Kjellén L, Kreuger J, Ledin J.SourceDepartment of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Uppsala, Sweden.
Developmental dynamics : an official publication of the American Association of Anatomists.Dev Dyn.2013 Aug;242(8):964-75. doi: 10.1002/dvdy.23981. Epub 2013 Jun 18.
Background: Chondroitin/dermatan sulfate (CS/DS) proteoglycans present in the extracellular matrix have important structural and regulatory functions. Results: Six human genes have previously been shown to catalyze CS/DS polymerization. Here we show that one of these genes, chpf, is represented by t
PMID 23703795

Epiphycan from salmon nasal cartilage is a novel type of large leucine-rich proteoglycan.

Tatara Y, Kakizaki I, Kuroda Y, Suto S, Ishioka H, Endo M.SourceDepartment of Glycotechnology, Center for Advanced Medical Research and.
Glycobiology.Glycobiology.2013 Aug;23(8):993-1003. doi: 10.1093/glycob/cwt038. Epub 2013 May 22.
Chum salmon (Oncorhynchus keta) nasal cartilage was examined by next-generation DNA sequencing and mass spectrometric analyses, and 14 types of proteoglycans including epiphycan (EPY) were found. A cDNA encoding EPY was cloned and sequenced. The cDNA encoded 589 amino acids comprised a glycosaminogl
PMID 23704297

Human Ng2+ adipose stem cells loaded in vivo on a new crosslinked hyaluronic acid-Lys scaffold fabricate a skeletal muscle tissue.

Desiderio V, De Francesco F, Schiraldi C, De Rosa A, La Gatta A, Paino F, d'Aquino R, Ferraro GA, Tirino V, Papaccio G.SourceDipartimento di Medicina Sperimentale, Sezione di Istologia ed Embriologia Medica, Tissue Engineering and Regenerative (TERM), Seconda Università degli Studi di Napoli, Napoli, Italy.
Journal of cellular physiology.J Cell Physiol.2013 Aug;228(8):1762-73. doi: 10.1002/jcp.24336.
Mesenchymal stem cell (MSC) therapy holds promise for treating diseases and tissue repair. Regeneration of skeletal muscle tissue that is lost during pathological muscle degeneration or after injuries is sustained by the production of new myofibers. Human Adipose stem cells (ASCs) have been reported
PMID 23359523

Japanese Journal

Organization of glycosaminoglycan sulfation in the biosynthesis of proteochondroitin sulfate and proteodermatan sulfate

SILBERT J. E.
Glycoconj. J. 13, 907-912, 1996
NAID 30012306700

EFFECT OF COLCHICINE AND CYTOCHALASIN B ON THE SECRETION OF PROTEOCHONDROITIN SULFATE AND PROTEINFREE CHONDROITIN SULFATE SYNTHESIZED IN CARTILAGE SLICES

HONDA ATSUSHI,TAKAKUBO FUMIE,MURAKAMI NAOTO,MORI YO
Journal of pharmacobio-dynamics 2(5), 327-330, 1979-09
… The present study suggested that the microtubule system was partly involved in the secretion of proteochondroitin sultate and protein-tree chondroitin sultate synthesized in chondrocytes. …
NAID 110003635762