- 関
- cell surface glycoprotein、surface glycoprotein
WordNet
- a thin pliable sheet of material
- a pliable sheet of tissue that covers or lines or connects the organs or cells of animals or plants (同)tissue layer
- a conjugated protein having a carbohydrate component
PrepTutorEJDIC
- (生物の)膜,皮膜
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/08/14 19:52:59」(JST)
[Wiki en表示]
Not to be confused with peptidoglycan or proteoglycan.
N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins.
[1]
Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to polypeptide side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. In proteins that have segments extending extracellularly, the extracellular segments are often glycosylated. Glycoproteins are often important integral membrane proteins, where they play a role in cell–cell interactions. Glycoproteins are also formed in the cytosol, but their functions and the pathways producing these modifications in this compartment are less well understood.[2]
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Contents
- 1 N-glycosylation and O-glycosylation
- 2 Monosaccharides
- 3 Examples
- 4 Hormones
- 5 Functions
- 6 Analysis
- 7 See also
- 8 References
- 9 External links
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N-glycosylation and O-glycosylation
There are two types of glycoproteins:
- In N-glycosylation (see on the right), the addition of sugar chains can happen at the amide nitrogen on the side-chain of the asparagine.
- In O-glycosylation, the addition of sugar chains can happen on the hydroxyl oxygen on the side-chain of hydroxylysine, hydroxyproline, serine, or threonine.
Monosaccharides
Eight sugars commonly found in glycoproteins.
Monosaccharides commonly found in eukaryotic glycoproteins include:[3]:526
The principal sugars found in human glycoproteins[4]
| Sugar |
Type |
Abbreviation |
| β-D-Glucose |
Hexose |
Glc |
| β-D-Galactose |
Hexose |
Gal |
| β-D-Mannose |
Hexose |
Man |
| α-L-Fucose |
Deoxyhexose |
Fuc |
| N-Acetylgalactosamine |
Aminohexose |
GalNAc |
| N-Acetylglucosamine |
Aminohexose |
GlcNAc |
| N-Acetylneuraminic acid |
Aminononulosonic acid
(Sialic acid) |
NeuNAc |
| Xylose |
Pentose |
Xyl |
The sugar group(s) can assist in protein folding or improve proteins' stability.
Examples
One example of glycoproteins found in the body is mucins, which are secreted in the mucus of the respiratory and digestive tracts. The sugars attached to mucins give them considerable water-holding capacity and also make them resistant to proteolysis by digestive enzymes.
Glycoproteins are important for white blood cell recognition, especially in mammals.[citation needed] Examples of glycoproteins in the immune system are:
- molecules such as antibodies (immunoglobulins), which interact directly with antigens.
- molecules of the major histocompatibility complex (or MHC), which are expressed on the surface of cells and interact with T cells as part of the adaptive immune response.
Other examples of glycoproteins include:
- glycoprotein IIb/IIIa, an integrin found on platelets that is required for normal platelet aggregation and adherence to the endothelium.
- components of the zona pellucida, which surrounds the oocyte, and is important for sperm-egg interaction.
- structural glycoproteins, which occur in connective tissue. These help bind together the fibers, cells, and ground substance of connective tissue. They may also help components of the tissue bind to inorganic substances, such as calcium in bone.
- Glycoprotein-41 (gp41) and glycoprotein-120 (gp120) are HIV viral coat proteins.
Soluble glycoproteins often show a high viscosity, for example, in egg white and blood plasma.
- Miraculin, which alters human tongue receptors to recognize sour foods as sweet.
Hormones
Hormones that are glycoproteins include:
- Follicle-stimulating hormone
- Luteinizing hormone
- Thyroid-stimulating hormone
- Human chorionic gonadotropin
- Alpha-fetoprotein
- Erythropoietin (EPO)
Functions
Some functions served by glycoproteins[3]:524
| Function |
Glycoproteins |
| Structural molecule |
Collagens |
| Lubricant and protective agent |
Mucins |
| Transport molecule |
Transferrin, ceruloplasmin |
| Immunologic molecule |
Immunoglobins, histocompatibility antigens |
| Hormone |
Human chorionic gonadotropin (HCG), thyroid-stimulating hormone (TSH) |
| Enzyme |
Various, e.g., alkaline phosphatase |
| Cell attachment-recognition site |
Various proteins involved in cell–cell (e.g., sperm–oocyte), virus–cell, bacterium–cell, and hormone–cell interactions |
| Antifreeze protein |
Certain plasma proteins of coldwater fish |
| Interact with specific carbohydrates |
Lectins, selectins (cell adhesion lectins), antibodies |
| Receptor |
Various proteins involved in hormone and drug action |
| Affect folding of certain proteins |
Calnexin, calreticulin |
| Regulation of development |
Notch and its analogs, key proteins in development |
| Hemostasis (and thrombosis) |
Specific glycoproteins on the surface membranes of platelets |
Analysis
A variety of methods used in detection, purification, and structural analysis of glycoproteins are[3]:525[5]
Some important methods used to study glycoproteins
| Method |
Use |
| Periodic acid-Schiff stain |
Detects glycoproteins as pink bands after electrophoretic separation. |
| Incubation of cultured cells with glycoproteins as radioactive decay bands |
Leads to detection of a radioactive sugar after electrophoretic separation. |
| Treatment with appropriate endo- or exoglycosidase or phospholipases |
Resultant shifts in electrophoretic migration help distinguish among proteins with N-glycan, O-glycan, or GPI linkages and also between high mannose and complex N-glycans. |
| Agarose-lectin column chromatography, lectin affinity chromatography |
To purify glycoproteins or glycopeptides that bind the particular lectin used. |
| Lectin affinity electrophoresis |
Resultant shifts in electrophoretic migration help distinguish and characterize glycoforms, i.e. variants of a glycoprotein differing in carbohydrate. |
| Compositional analysis following acid hydrolysis |
Identifies sugars that the glycoprotein contains and their stoichiometry. |
| Mass spectrometry |
Provides information on molecular mass, composition, sequence, and sometimes branching of a glycan chain. |
| NMR spectroscopy |
To identify specific sugars, their sequence, linkages, and the anomeric nature of glycosidic chain. |
| Dual Polarisation Interferometry |
Measures the mechanisms underlying the biomolecular interactions, including reaction rates, affinities and associated conformational changes. |
| Methylation (linkage) analysis |
To determine linkage between sugars. |
| Amino acid or cDNA sequencing |
Determination of amino acid sequence. |
See also
- P-glycoprotein
- Glycopeptide
- Proteoglycan
- Glycocalyx
- Ero1
- Gp120
- Gp41
- Miraculin
- Female sperm storage
References
- ^ Ruddock & Molinari (2006) Journal of Cell Science 119, 4373–4380
- ^ Funakoshi Y, Suzuki T (January 2009). "Glycobiology in the cytosol: The bitter side of a sweet world". Biochim. Biophys. Acta 1790 (2): 81–94. doi:10.1016/j.bbagen.2008.09.009. PMID 18952151.
- ^ a b c Robert K. Murray, Daryl K. Granner & Victor W. Rodwell: "Harper's Illustrated Biochemistry 27th Ed.", McGraw–Hill, 2006
- ^ https://www.sigmaaldrich.com/img/assets/15880/glycan_classification.pdf
- ^ Anne Dell, Howard R Morris: "Glycoprotein structure determination by mass spectrometry", Science 291(5512), 2351–2356 (2001), Review
External links
- Structure of Glycoprotein and Carbohydrate Chain – Home Page for Learning Environmental Chemistry
- Biochemistry 5thE 11.3. Carbohydrates Can Be Attached to Proteins to Form Glycoproteins
- Carbohydrate Chemistry and Glycobiology: A Web Tour SPECIAL WeB SUPPLEMENT Science 23 March 2001 Vol 291, Issue 5512, Pages 2263–2502
- Glycoproteins at the US National Library of Medicine Medical Subject Headings (MeSH)
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Protein, glycoconjugate: glycoproteins and glycopeptides
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| Mucoproteins |
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Mucin
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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
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| Proteoglycans |
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CS/DS
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Decorin · Biglycan · Versican
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HS/CS
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Testican · Perlecan
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CS
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Chondroitin sulfate proteoglycans: Aggrecan · Neurocan · Brevican · CD44 · CSPG4 · CSPG5 · Platelet factor 4 · Structural maintenance of chromosomes 3
|
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KS
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Fibromodulin · Lumican · Keratocan
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HS
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Syndecan 1
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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
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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biochemical families: proteins (amino acids/intermediates) · nucleic acids (constituents/intermediates) · carbohydrates (glycoproteins, alcohols, glycosides)
lipids (fatty acids/intermediates, phospholipids, steroids, sphingolipids, eicosanoids) · tetrapyrroles/intermediates
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Metabolism: carbohydrate metabolism · glycoprotein enzymes
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| Anabolism |
Dolichol kinase · GCS1 · Oligosaccharyltransferase
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| Catabolism |
Neuraminidase · Beta-galactosidase · Hexosaminidase · mannosidase (alpha-Mannosidase, beta-mannosidase) · Aspartylglucosaminidase · Fucosidase · NAGA
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| Transport |
SLC17A5
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| M6P tagging |
N-acetylglucosamine-1-phosphate transferase
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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(LSD) Inborn error of carbohydrate metabolism: glycoproteinosis (E77, 271.8)
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| Anabolism |
Dolichol kinase deficiency · Congenital disorder of glycosylation
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Post-translational modification
of lysosomal enzymes |
Mucolipidosis: I-cell disease/II · Pseudo-Hurler polydystrophy/III
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| Catabolism |
Aspartylglucosaminuria · Fucosidosis · mannosidosis (Alpha-mannosidosis, Beta-mannosidosis) · Sialidosis · Schindler disease
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| Other |
solute carrier family (Salla disease) · Galactosialidosis
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- Novel electrochemical aptamer biosensor based on an enzyme-gold nanoparticle dual label for the ultrasensitive detection of epithelial tumour marker MUC1.
- Hu R, Wen W, Wang Q, Xiong H, Zhang X, Gu H, Wang S.Author information Hubei Collaborative Innovation Center for Advanced Organic Chemical Materials, Ministry of Education Key Laboratory for the Synthesis and Application of Organic Functional Molecules & College of Chemistry and Chemical Engineering, Hubei University, Wuhan 430062, PR China.AbstractA novel platform based on a hairpin oligonucleotide (HO) switch, gold nanoparticles (AuNPs), and enzyme signal amplification for the ultrasensitive detection of mucin 1 protein (MUC1) was developed in this assay. This HO aptamers and horseradish peroxidase (HRP) were immobilised on the AuNPs to yield HO-AuNP-HRP conjugates. AuNPs were used as labels and bridges between the HO and HRP. HRP was also used as label for catalysing the oxidation of o-phenylenediamine by H2O2. The reaction product was 2,3-diaminophenazine (DAP), which was reduced and could be detected at surface of modified electrode. The reduction signal of DAP was used as a probe for the sensitive detection. After the recognition between oligonucleotide and MUC1, biotin was exposed. Biotin, along with the conjugate, was captured by streptavidin onto the surface of modified electrode. Therefore, the detection of target MUC1 which was a membrane-associated glycoprotein of the mucin family could be sensitively transduced via detection of the electrochemical reduction signal of DAP. Compared to other aptasensors, this biosensor has a good linear correlation ranges from 8.8 nM to 353.3 nM and a lower detection limit of 2.2 nM for MUC1. The proposed method provided a new electrochemical approach for the detection of MUC1.
- Biosensors & bioelectronics.Biosens Bioelectron.2014 Mar 15;53:384-9. doi: 10.1016/j.bios.2013.10.015. Epub 2013 Oct 24.
- A novel platform based on a hairpin oligonucleotide (HO) switch, gold nanoparticles (AuNPs), and enzyme signal amplification for the ultrasensitive detection of mucin 1 protein (MUC1) was developed in this assay. This HO aptamers and horseradish peroxidase (HRP) were immobilised on the AuNPs to yiel
- PMID 24189297
- The dengue virus non-structural 1 protein: Risks and benefits.
- Amorim JH1, Alves RP2, Boscardin SB3, Ferreira LC2.Author information 1Vaccine Development Laboratory, Department of Microbiology, University of São Paulo, Brazil. Electronic address: jhamorim@usp.br.2Vaccine Development Laboratory, Department of Microbiology, University of São Paulo, Brazil.3Laboratory of Antigen Targeting to Dendritic Cells, Department of Parasitology, University of São Paulo, Brazil.AbstractThe dengue virus (DENV) non-structural 1 (NS1) protein plays a critical role in viral RNA replication and has a central position in DENV pathogenesis. DENV NS1 is a glycoprotein expressed in infected mammalian cells as soluble monomers that dimerize in the lumen of the endoplasmic reticulum; NS1 is subsequently transported to the cell surface, where it remains membrane associated or is secreted into the extracellular milieu as a hexameric complex. During the last three decades, the DENV NS1 protein has also been intensively investigated as a potential target for vaccines and antiviral drugs. In addition, NS1 is the major diagnostic marker for dengue infection. This review highlights some important issues regarding the role of NS1 in DENV pathogenesis and its biotechnological applications, both as a target for the development of safe and effective vaccines and antiviral drugs and as a tool for the generation of accurate diagnostic methods.
- Virus research.Virus Res.2014 Mar 6;181C:53-60. doi: 10.1016/j.virusres.2014.01.001. Epub 2014 Jan 13.
- The dengue virus (DENV) non-structural 1 (NS1) protein plays a critical role in viral RNA replication and has a central position in DENV pathogenesis. DENV NS1 is a glycoprotein expressed in infected mammalian cells as soluble monomers that dimerize in the lumen of the endoplasmic reticulum; NS1 is
- PMID 24434336
- Active elimination of the marine biotoxin okadaic acid by P-glycoprotein through an in vitro gastrointestinal barrier.
- Ehlers A1, These A2, Hessel S3, Preiss-Weigert A2, Lampen A3.Author information 1Federal Institute for Risk Assessment, Department of Food Safety, Berlin, Germany. Electronic address: Anke.Ehlers@bfr.bund.de.2Federal Institute for Risk Assessment, Department of Safety in the Food Chain, Berlin, Germany.3Federal Institute for Risk Assessment, Department of Food Safety, Berlin, Germany.AbstractThe consumption of okadaic acid (OA) contaminated shellfish can induce acute toxic symptoms in humans such as diarrhea, nausea, vomiting and abdominal pain; carcinogenic and embryotoxic effects have also been described. Toxicokinetic studies with mice have shown that high cytotoxic doses of OA can pass the gastrointestinal barrier presumably by paracellular passage. However, in vitro studies using human intestinal Caco-2 cell monolayers to represent the intestinal barrier have shown that at low-dose exposure OA is transported against a concentration gradient suggesting an active efflux mechanism. Since P-glycoprotein (P-gp) transports a wide variety of substrates, we investigated its possible influence on the observed elimination of OA. We used two different cellular transwell models: (i) Caco-2 cell monolayer endogenously expressing human P-gp and simulating the intestinal barrier and (ii) MDCK-II cell monolayer stably over-expressing P-gp. Our study demonstrates clearly that OA at non-cytotoxic concentrations passes the monolayer barrier only to a low degree, and that it is actively eliminated by P-gp over the apical membrane. Therefore, our in vitro data indicate that humans appear to have efficient defense mechanisms to protect themselves against low-dose contaminated shellfish by exhibiting a low bioavailability as a result of active elimination of OA by P-gp.
- Toxicology letters.Toxicol Lett.2014 Mar 3;225(2):311-7. doi: 10.1016/j.toxlet.2013.12.019. Epub 2013 Dec 25.
- The consumption of okadaic acid (OA) contaminated shellfish can induce acute toxic symptoms in humans such as diarrhea, nausea, vomiting and abdominal pain; carcinogenic and embryotoxic effects have also been described. Toxicokinetic studies with mice have shown that high cytotoxic doses of OA can p
- PMID 24374049
Japanese Journal
- Interaction between TIM-1 and NPC1 Is Important for Cellular Entry of Ebola Virus
- Improvement of glycosylation structure by suppression of β-N-acetylglucosaminidases in silkworm(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
Related Links
- Definition of Membrane glycoprotein in the Medical Dictionary. Membrane glycoprotein explanation. Information about Membrane glycoprotein in Free online English dictionary. What is Membrane glycoprotein? Meaning of forum ...
- glycoprotein (glī'kōprō`tēn), organic compound composed of both a protein protein, any of the group of highly complex organic compounds found in all living cells and comprising the most abundant class of all biological molecules.
Related Pictures
★リンクテーブル★
[★]
- 英
- membrane glycoprotein
- 関
- 表面糖タンパク質、細胞表面糖タンパク質
[★]
- 関
- membrane glycoprotein、surface glycoprotein
[★]
- 関
- cell surface glycoprotein、membrane glycoprotein
[★]
血小板膜糖タンパク質IIb
- 関
- GP IIb、integrin alpha IIb、integrin alphaIIb
[★]
- 関
- platelet glycoprotein
[★]
リソソーム膜糖タンパク質
[★]