プロテオグリカン
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/04/02 12:43:34」(JST)
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Not to be confused with peptidoglycan, glycoprotein, or glycopeptide.
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.
Contents
- 1 Types
- 2 Function
- 3 Synthesis
- 4 Clinical Significance
- 5 References
- 6 External links
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
Protein, glycoconjugate: glycoproteins and glycopeptides
|
|
Mucoproteins |
Mucin
|
- CD43
- CD164
- MUC1
- MUC2
- MUC3A
- MUC3B
- MUC4
- MUC5AC
- MUC5B
- MUC6
- MUC7
- MUC8
- MUC12
- MUC13
- MUC15
- MUC16
- MUC17
- MUC19
- MUC20
|
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Other
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- Haptoglobin
- Intrinsic factor
- Orosomucoid
- Peptidoglycan
- Phytohaemagglutinin
- Ovomucin
|
|
|
Proteoglycans |
CS/DS
|
- Decorin
- Biglycan
- Versican
|
|
HS/CS
|
|
|
CS
|
- Chondroitin sulfate proteoglycans: Aggrecan
- Neurocan
- Brevican
- CD44
- CSPG4
- CSPG5
- Platelet factor 4
- Structural maintenance of chromosomes 3
|
|
KS
|
- Fibromodulin
- Lumican
- Keratocan
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|
HS
|
|
|
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Other |
- Activin and inhibin
- ADAM
- Alpha 1-antichymotrypsin
- Apolipoprotein H
- CD70
- Asialoglycoprotein
- Avidin
- B-cell activating factor
- 4-1BB ligand
- Cholesterylester transfer protein
- Clusterin
- Colony-stimulating factor
- Hemopexin
- Lactoferrin
- Membrane glycoproteins
- Myelin protein zero
- Osteonectin
- Protein C
- Protein S
- Serum amyloid P component
- Sialoglycoprotein
- CD43
- Glycophorin
- Glycophorin C
- Thrombopoietin
- Thyroglobulin
- Thyroxine-binding proteins
- Transcortin
- Tumor necrosis factor alpha
- Uteroglobin
- Vitronectin
|
UpToDate Contents
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English Journal
- Growth factor-heparan sulfate "switches" regulating stages of branching morphogenesis.
- Nigam SK, Bush KT.Author information Department of Medicine, University of California, La Jolla, San Diego, CA, 92093-0693, USA, nigamlab@ucsd.edu.AbstractThe development of branched epithelial organs, such as the kidney, mammary gland, lung, pancreas, and salivary gland, is dependent upon the involvement and interaction of multiple regulatory/modulatory molecules, including soluble growth factors, extracellular matrix components, and their receptors. How the function of these molecules is coordinated to bring about the morphogenetic events that regulate iterative tip-stalk generation (ITSG) during organ development remains to be fully elucidated. A common link to many growth factor-dependent morphogenetic pathways is the involvement of variably sulfated heparan sulfates (HS), the glycosaminoglycan backbone of heparan sulfate proteoglycans (HSPG) on extracellular surfaces. Genetic deletions of HS biosynthetic enzymes (e.g., C5-epimerase, Hs2st), as well as considerable in vitro data, indicate that variably sulfated HS are essential for kidney development, particularly in Wolffian duct budding and early ureteric bud (UB) branching. A role for selective HS modifications by enzymes (e.g., Ext, Ndst, Hs2st) in stages of branching morphogenesis is also strongly supported for mammary gland ductal branching, which is dependent upon a set of growth factors similar to those involved in UB branching. Taken together, these studies provide support for the notion that the specific spatio-temporal HS binding of growth factors during the development of branched epithelial organs (such as the kidney, mammary gland, lung and salivary gland) regulates these complex processes by potentially acting as "morphogenetic switches" during the various stages of budding, branching, and other developmental events central to epithelial organogenesis. It may be that two or more growth factor-selective HS interactions constitute a functionally equivalent morphogenetic switch; this may help to explain the paucity of severe branching phenotypes with individual growth factor knockouts.
- Pediatric nephrology (Berlin, Germany).Pediatr Nephrol.2014 Apr;29(4):727-35. doi: 10.1007/s00467-013-2725-z. Epub 2014 Feb 2.
- The development of branched epithelial organs, such as the kidney, mammary gland, lung, pancreas, and salivary gland, is dependent upon the involvement and interaction of multiple regulatory/modulatory molecules, including soluble growth factors, extracellular matrix components, and their receptors.
- PMID 24488503
- Natural and synthetic polymers for wounds and burns dressing.
- Mogoşanu GD1, Grumezescu AM2.Author information 1Department of Pharmacognosy & Phytotherapy, Faculty of Pharmacy, University of Medicine and Pharmacy of Craiova, 2 Petru Rareş Street, 200349 Craiova, Romania.2Department of Science and Engineering of Oxidic Materials and Nanomaterials, Faculty of Applied Chemistry and Materials Science, Politehnica University of Bucharest, 1-7 Polizu Street, 011061 Bucharest, Romania. Electronic address: grumezescu@yahoo.com.AbstractIn the last years, health care professionals faced with an increasing number of patients suffering from wounds and burns difficult to treat and heal. During the wound healing process, the dressing protects the injury and contributes to the recovery of dermal and epidermal tissues. Because their biocompatibility, biodegradability and similarity to macromolecules recognized by the human body, some natural polymers such as polysaccharides (alginates, chitin, chitosan, heparin, chondroitin), proteoglycans and proteins (collagen, gelatin, fibrin, keratin, silk fibroin, eggshell membrane) are extensively used in wounds and burns management. Obtained by electrospinning technique, some synthetic polymers like biomimetic extracellular matrix micro/nanoscale fibers based on polyglycolic acid, polylactic acid, polyacrylic acid, poly-ɛ-caprolactone, polyvinylpyrrolidone, polyvinyl alcohol, polyethylene glycol, exhibit in vivo and in vitro wound healing properties and enhance re-epithelialization. They provide an optimal microenvironment for cell proliferation, migration and differentiation, due to their biocompatibility, biodegradability, peculiar structure and good mechanical properties. Thus, synthetic polymers are used also in regenerative medicine for cartilage, bone, vascular, nerve and ligament repair and restoration. Biocompatible with fibroblasts and keratinocytes, tissue engineered skin is indicated for regeneration and remodeling of human epidermis and wound healing improving the treatment of severe skin defects or partial-thickness burn injuries.
- International journal of pharmaceutics.Int J Pharm.2014 Mar 25;463(2):127-36. doi: 10.1016/j.ijpharm.2013.12.015. Epub 2013 Dec 22.
- In the last years, health care professionals faced with an increasing number of patients suffering from wounds and burns difficult to treat and heal. During the wound healing process, the dressing protects the injury and contributes to the recovery of dermal and epidermal tissues. Because their bioc
- PMID 24368109
- A5.5 SMOC2 modulates chondrogenesis by interfering with WNT and BMP signalling.
- Cailotto F, Luyten FP, Lories RJ.Author information Laboratory of Tissue Homeostasis and Disease, Skeletal Biology and Engineering Research Center, Department of Development & Regeneration, KU Leuven, Belgium.AbstractBACKGROUND AND OBJECTIVES: A proteomic analysis of cartilage revealed an increase in SPARC-related modular calcium binding protein-2 (SMOC2) in patients with osteoarthritis (OA). SMOC2 was originally isolated from a chondrogenic extract of articular cartilage together with GDF5 and FRZB, proteins associated with OA. We investigated SMOC2 in chondrocyte differentiation.
- Annals of the rheumatic diseases.Ann Rheum Dis.2014 Mar 1;73 Suppl 1:A65. doi: 10.1136/annrheumdis-2013-205124.147.
- BACKGROUND AND OBJECTIVES: A proteomic analysis of cartilage revealed an increase in SPARC-related modular calcium binding protein-2 (SMOC2) in patients with osteoarthritis (OA). SMOC2 was originally isolated from a chondrogenic extract of articular cartilage together with GDF5 and FRZB, proteins as
- PMID 24489274
Japanese Journal
Related Links
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