BEU11403 Biomaterials_Lecture 2.pdf

8/12/2019 BEU11403 Biomaterials_Lecture 2.pdf

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BEU11403-BiomaterialsChapter 2: Assembly of BiologicalMacromolecules

Chin Fhong, Soon(PhD, MIET, MIEEE-EMBS)

Microelectronics and Nanotechnology-Shamsuddin ResearchCenter


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Lecture outline

Collagen Fibronectin Laminin Fibrinogen Glycoproteins


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Basement membrane


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Collagen

Major insoluble fibrous protein of theextracellular matrix and connective tissueMost abundant protein in animalsMade by fibroblasts and some epithelial cellstensile strength and elasticity

Tendons Cartilage Bone

half total body proteins (by weight)


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Collagen


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Collagen Components

Triple helix of polypeptidesEach polypeptide is a left-handed helix tooInsoluble glycoprotein

protein + carbohydrate

Protein high glycine high proline hydroxylysine

hydroxyproline (gly-X-Y)

Carbohydrate, glucose, galactose


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Extracellular Matrix contains proteins collagen,elastin, fibronectin, and laminin

Collagen is strong, resisting tensile forces (in abundance in the Achilles heel)

Y is usually hydroxyproline


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Collagen


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Collagen Structure

Collagen Protein3 polypeptide (a) chains, left hand helix, forms fibers

many different (vertebrate) collagens by differentcombinations of -chains

Type I, II, III main fibers, flexible

Type I bone, skin, tendons

90% of all collagen

Type II cartiladge


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Collagen Fibers

Type I, II, III cross striated e.g. tendons - type I fibrils, have a 67-nm period striations

and are oriented longitudinally (direction of the stress) showing overlapping packing of individual collagen

molecules reticular fibrestype III, support individual cells

Type IV fine unstriated sheet-like supportive meshwork mature basal laminae tracks for embryonic migration

barriers for cell migrationType V-XII

smaller diameter fibers than I-III no striations


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Collagen Type Function

Collagen Type I - skin, tendon, vascular,ligature, organs, bone (main component ofbone)

Collagen Type II - cartilage (maincomponent of cartilage)

Collagen Type III - reticular fibers with type I.

Collagen Type IV - forms bases of cell

basement membraneCollagen Type V - hair and nail


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PhD Research Results

Figure 3.12. Micrographs of immuno-staining against collagen type IV, laminin and fibronectin for HaCaT cells

cultured on (a, d, g) negative controls,(b, e, f)controls and (c, f, i) liquid crystal substrates, respectively. (Scale

bar: 20 m). (Enlarged exert, scale bar: 25 m).


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Staining of LamininNegative control Control

Figure 3.13. Immunoperoxidase staining of laminin for HaCaT cellscultured on a negative control (left), control (middle) and liquid crystal

substrate (right).


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Collagen Synthesis

Endoplasmic Reticulum mRNA attached to ER protein synthesized into ER lumen cotranslational and post-translational modifications 3 proto--chains form soluble procollagen

moved to golgi apparatusGolgi Apparatus

packed into secretion vesicles fuse with membrane

Outside Cell procollagen processed by enzymes outside cell assemble into collagen fibers collagen fibrils form lateral Interactions of triple helices

Coand Posttranslational modification(PTM) is a step in protein biosynthesis. Proteins are createdby ribosomestranslatingmRNAinto polypeptide chains. These polypeptide chains undergo PTM, (such asfolding, cutting and other processes), before becoming the mature protein product.
http://en.wikipedia.org/wiki/Ribosomeshttp://en.wikipedia.org/wiki/Translation_(biology)http://en.wikipedia.org/wiki/MRNAhttp://en.wikipedia.org/wiki/Protein_biosynthesishttp://en.wikipedia.org/wiki/Ribosomeshttp://en.wikipedia.org/wiki/Translation_(biology)http://en.wikipedia.org/wiki/MRNAhttp://en.wikipedia.org/wiki/MRNAhttp://en.wikipedia.org/wiki/Translation_(biology)http://en.wikipedia.org/wiki/Ribosomeshttp://en.wikipedia.org/wiki/Protein_biosynthesis


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Collagen synthesis


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Elastin

Elastic fiber is composed of theprotein fibrillinand elastinmade of simple aminoacidssuchas glycine, valine, alanine,

and proline.Elastin lacks collagensrepetitive sequeencing at thefibril stage.

Fibres are only 5 to 7 mm inlength.

High hydrophobic and elastic.
http://en.wikipedia.org/wiki/Fibrillinhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Glycinehttp://en.wikipedia.org/wiki/Valinehttp://en.wikipedia.org/wiki/Alaninehttp://en.wikipedia.org/wiki/Prolinehttp://en.wikipedia.org/wiki/Prolinehttp://en.wikipedia.org/wiki/Alaninehttp://en.wikipedia.org/wiki/Valinehttp://en.wikipedia.org/wiki/Glycinehttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Fibrillin


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Fibronectin


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FibronectinDimerconnected at C-terminus

MW 440 kDa nearly identical subunits

composed of types I (F1), II (F2),and III (F3) fibronectin modules

S-S linkages

rigid and flexible domainsfibronectin fibrils have elasticproperties and can stretch fibrilsup to four-fold their relaxedlength.

fibrillogenesis - transformationfrom the compact (soluble) formto the extended fibrillar (insoluble)form of fibronectin, requiresapplication of mechanical forcesgenerated by cells.
http://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=mboc4&part=A3532&rendertype=figure&id=A3572http://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=mboc4&part=A3532&rendertype=figure&id=A3572


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Two types of fibronectin are presentin vertebrates:[

soluble plasma fibronectin (formerly called "cold-insoluble globulin", or CIg) isa major protein

component of bloodplasma(300 g/ml) and isproduced in the liverby hepatocytes.

insoluble cellular fibronectin is a majorcomponent of the extracellular matrix. It issecretedby various cells, primarily fibroblasts, as asoluble protein dimerand is then assembled intoan insoluble matrix in a complex cell-mediatedprocess.
http://en.wikipedia.org/wiki/Vertebrateshttp://en.wikipedia.org/wiki/Vertebrateshttp://en.wikipedia.org/wiki/Blood_plasmahttp://en.wikipedia.org/wiki/Blood_plasmahttp://en.wikipedia.org/wiki/Liverhttp://en.wikipedia.org/wiki/Blood_plasmahttp://en.wikipedia.org/wiki/Hepatocyteshttp://en.wikipedia.org/wiki/Hepatocyteshttp://en.wikipedia.org/wiki/Hepatocyteshttp://en.wikipedia.org/wiki/Liverhttp://en.wikipedia.org/wiki/Hepatocyteshttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Fibroblastshttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Fibroblastshttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Fibroblastshttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Hepatocyteshttp://en.wikipedia.org/wiki/Liverhttp://en.wikipedia.org/wiki/Blood_plasmahttp://en.wikipedia.org/wiki/Vertebrates


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Fibronectinis a high-molecularweight(~440kDa) glycoproteinof the extracellularmatrixthat binds to membrane-spanning receptorproteinscalled integrins.Similar to integrins, fibronectinbinds extracellular matrix components suchas collagen, fibrin, and heparansulfateproteoglycans(e.g. syndecans).

Fibronectin exists as a protein dimer, consisting of twonearly identical monomers linked by a pair of disulfidebonds.[1] The fibronectin protein is produced from asingle gene, but alternative splicing of its pre-mRNAleads to the creation of several isoforms.
http://en.wikipedia.org/wiki/Molecular_weighthttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Molecular_weighthttp://en.wikipedia.org/wiki/Extracellular_matrixhttp://en.wikipedia.org/wiki/Molecular_weighthttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Cell_membranehttp://en.wikipedia.org/wiki/Extracellular_matrixhttp://en.wikipedia.org/wiki/Receptor_proteinshttp://en.wikipedia.org/wiki/Receptor_proteinshttp://en.wikipedia.org/wiki/Receptor_proteinshttp://en.wikipedia.org/wiki/Integrinshttp://en.wikipedia.org/wiki/Integrinshttp://en.wikipedia.org/wiki/Cell_membranehttp://en.wikipedia.org/wiki/Receptor_proteinshttp://en.wikipedia.org/wiki/Receptor_proteinshttp://en.wikipedia.org/wiki/Integrinshttp://en.wikipedia.org/wiki/Collagenhttp://en.wikipedia.org/wiki/Fibrinhttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Proteoglycanshttp://en.wikipedia.org/wiki/Proteoglycanshttp://en.wikipedia.org/wiki/Proteoglycanshttp://en.wikipedia.org/wiki/Proteoglycanshttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Syndecanshttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Proteoglycanshttp://en.wikipedia.org/wiki/Syndecanshttp://en.wikipedia.org/wiki/Monomershttp://en.wikipedia.org/wiki/Monomershttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Disulfide_bondshttp://en.wikipedia.org/wiki/Disulfide_bondshttp://en.wikipedia.org/wiki/Fibronectinhttp://en.wikipedia.org/wiki/Monomershttp://en.wikipedia.org/wiki/Disulfide_bondshttp://en.wikipedia.org/wiki/Disulfide_bondshttp://en.wikipedia.org/wiki/Fibronectinhttp://en.wikipedia.org/wiki/Alternative_splicinghttp://en.wikipedia.org/wiki/Pre-mRNAhttp://en.wikipedia.org/wiki/Pre-mRNAhttp://en.wikipedia.org/wiki/Alternative_splicinghttp://en.wikipedia.org/wiki/Isoformshttp://en.wikipedia.org/wiki/Isoformshttp://en.wikipedia.org/wiki/Pre-mRNAhttp://en.wikipedia.org/wiki/Pre-mRNAhttp://en.wikipedia.org/wiki/Isoformshttp://en.wikipedia.org/wiki/Isoformshttp://en.wikipedia.org/wiki/Pre-mRNAhttp://en.wikipedia.org/wiki/Pre-mRNAhttp://en.wikipedia.org/wiki/Pre-mRNAhttp://en.wikipedia.org/wiki/Alternative_splicinghttp://en.wikipedia.org/wiki/Alternative_splicinghttp://en.wikipedia.org/wiki/Alternative_splicinghttp://en.wikipedia.org/wiki/Fibronectinhttp://en.wikipedia.org/wiki/Fibronectinhttp://en.wikipedia.org/wiki/Fibronectinhttp://en.wikipedia.org/wiki/Disulfide_bondshttp://en.wikipedia.org/wiki/Disulfide_bondshttp://en.wikipedia.org/wiki/Disulfide_bondshttp://en.wikipedia.org/wiki/Monomershttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Protein_dimerhttp://en.wikipedia.org/wiki/Syndecanshttp://en.wikipedia.org/wiki/Proteoglycanshttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Heparan_sulfatehttp://en.wikipedia.org/wiki/Fibrinhttp://en.wikipedia.org/wiki/Collagenhttp://en.wikipedia.org/wiki/Integrinshttp://en.wikipedia.org/wiki/Receptor_proteinshttp://en.wikipedia.org/wiki/Receptor_proteinshttp://en.wikipedia.org/wiki/Cell_membranehttp://en.wikipedia.org/wiki/Extracellular_matrixhttp://en.wikipedia.org/wiki/Extracellular_matrixhttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Molecular_weighthttp://en.wikipedia.org/wiki/Molecular_weight


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Binding Domains

cell binding segment RGDS arg-gly-asp-ser

binds integrin receptor in membrane then mechanically couples to the actin

cytoskeletondomains bind

heparin sulphate collagen

hyaluronic acid Gangliosides fibronectin


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Fibronectin Functionsoluble protein in blood plasma (200250 kDa monomer)

blood clotting process, link to fibrin

insoluble protein in extracellular matrix (ECM) ECM fibronectin differs from plasma fibronectin by the presence

of additional polypeptide segments and in altering morphology oftransformed cells and hemagglutination.

Cell AdhesionMigration Pathwaysblocking fibronectin with antibodyprevents neural crest migrationextension of axons and dendritesbranching


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Fibronectin plays a major role in celladhesion, growth, migration,and differentiation, and it is important for

processes such as woundhealingand embryonic development. Alteredfibronectin expression, degradation, andorganization has been associated with a

number of pathologies, including cancerand fibrosis.
http://en.wikipedia.org/wiki/Cell_adhesionhttp://en.wikipedia.org/wiki/Cell_adhesionhttp://en.wikipedia.org/wiki/Cell_growthhttp://en.wikipedia.org/wiki/Cell_migrationhttp://en.wikipedia.org/wiki/Cellular_differentiationhttp://en.wikipedia.org/wiki/Wound_healinghttp://en.wikipedia.org/wiki/Wound_healinghttp://en.wikipedia.org/wiki/Embryonic_developmenthttp://en.wikipedia.org/wiki/Gene_expressionhttp://en.wikipedia.org/wiki/Protein_degradationhttp://en.wikipedia.org/wiki/Pathologieshttp://en.wikipedia.org/wiki/Fibrosishttp://en.wikipedia.org/wiki/Fibrosishttp://en.wikipedia.org/wiki/Pathologieshttp://en.wikipedia.org/wiki/Protein_degradationhttp://en.wikipedia.org/wiki/Gene_expressionhttp://en.wikipedia.org/wiki/Embryonic_developmenthttp://en.wikipedia.org/wiki/Wound_healinghttp://en.wikipedia.org/wiki/Wound_healinghttp://en.wikipedia.org/wiki/Cellular_differentiationhttp://en.wikipedia.org/wiki/Cell_migrationhttp://en.wikipedia.org/wiki/Cell_growthhttp://en.wikipedia.org/wiki/Cell_adhesionhttp://en.wikipedia.org/wiki/Cell_adhesion


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Laminin


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Laminin Structure

cross-shaped glycoprotein3 polypeptides , 1, 2

carbohydrate (13% by weight)

separate binding domains collagen IV

heparin

heparin sulphate

cell binding cell specific binding - liver, nerve

cell surface receptor


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Lamininsare major proteins in the basallamina(one of the layers of the basementmembrane), a protein network foundation

for most cells and organs. The laminins arean important and biologically active part ofthe basal lamina, influencing celldifferentiation, migration, and adhesion, as

well as phenotype and survival
http://en.wikipedia.org/wiki/Basal_laminahttp://en.wikipedia.org/wiki/Basal_laminahttp://en.wikipedia.org/wiki/Basement_membranehttp://en.wikipedia.org/wiki/Basement_membranehttp://en.wikipedia.org/wiki/Basement_membranehttp://en.wikipedia.org/wiki/Basement_membranehttp://en.wikipedia.org/wiki/Basal_laminahttp://en.wikipedia.org/wiki/Basal_lamina


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Laminin Functioncell adhesionmigration pathwaysstimulates growth of axonsdevelopment and regenerationdifferentiation

basal laminaemost abundant linking glycoproteinIntegrin- Structure Integrin Function cell membrane receptor forECM linkers binds RGDS. Integrins consists of 2 subunits alpha() and beta () transmembrane linked to cell cytoskeleton actinmicrofilaments via talin and vinculin focal contacts

For Review see Integrin signaling revisited. Schwartz MA. TrendsCell Biol 2001 Dec;11(12):466-70


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The structures of actin cytoskeleton, focal adhesioncomplexes, integrin receptors, and adhesion proteins.

Cytoplasm

Bilayer lipid membrane

Actin filament

paxillinVinculin

-actinin

Talin

Capping protein

Integrin receptors

Laminin protein

ECMCell

Actin filament


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Fibrinogen


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Fibrinogen

is a soluble, 340 kDaplasmaglycoprotein,that is convertedby thrombininto fibrinduring blood clot

formation. Fibrinogen is synthesized inthe liverby the hepatocytes. Theconcentration of fibrinogen in the bloodplasma is 200400 mg/dL.
http://en.wikipedia.org/wiki/KDahttp://en.wikipedia.org/wiki/Blood_plasmahttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Thrombinhttp://en.wikipedia.org/wiki/Fibrinhttp://en.wikipedia.org/wiki/Coagulationhttp://en.wikipedia.org/wiki/Coagulationhttp://en.wikipedia.org/wiki/Liverhttp://en.wikipedia.org/wiki/Hepatocytehttp://en.wikipedia.org/wiki/Hepatocytehttp://en.wikipedia.org/wiki/Liverhttp://en.wikipedia.org/wiki/Coagulationhttp://en.wikipedia.org/wiki/Coagulationhttp://en.wikipedia.org/wiki/Fibrinhttp://en.wikipedia.org/wiki/Thrombinhttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Blood_plasmahttp://en.wikipedia.org/wiki/KDa


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Glycoproteins

Glyco proteins - a protein with a carbohydrateattached to it. More protein to carbohydrate. eg:enzymes, hormones, cell membranecomponents.


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ProteoglycansProteo glycans - Disaccharide chains attached to a proteincore. Rem - glycan refers to glucosamino glycans. Morecarbohydrates than proteins. (95% to 55%) eg: heparin,heparan, keratan, dermatan, chondroitin


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GlycoproteinsGlycoproteinsare proteinsthat contain oligosaccharidechains (glycans) covalentlyattached

to polypeptideside-chains.The carbohydrate is attached to the protein in a cotranslationalor posttranslationalmodification. This process is known as glycosylation. Secreted extracellular proteinsare oftenglycosylated. In proteins that have segments extending extracellularly, the extracellularsegments are also glycosylated. Glycoproteins are often important integral membraneproteins, where they play a role in cellcell interactions. Glycoproteins are also formed inthe cytosol, but their functions and the pathways producing these modifications in thiscompartment are less well understood
http://en.wikipedia.org/wiki/Peptidehttp://en.wikipedia.org/wiki/Proteinhttp://en.wikipedia.org/wiki/Oligosaccharidehttp://en.wikipedia.org/wiki/Glycanshttp://en.wikipedia.org/wiki/Covalent_bondhttp://en.wikipedia.org/wiki/Peptidehttp://en.wikipedia.org/wiki/Posttranslational_modificationhttp://en.wikipedia.org/wiki/Glycosylationhttp://en.wikipedia.org/wiki/Glycosylationhttp://en.wikipedia.org/wiki/Translation_(genetics)http://en.wikipedia.org/wiki/Secretory_proteinhttp://en.wikipedia.org/wiki/Secretory_proteinhttp://en.wikipedia.org/wiki/Secretory_proteinhttp://en.wikipedia.org/wiki/Posttranslational_modificationhttp://en.wikipedia.org/wiki/Posttranslational_modificationhttp://en.wikipedia.org/wiki/Glycosylationhttp://en.wikipedia.org/wiki/Secretory_proteinhttp://en.wikipedia.org/wiki/Integral_membrane_proteinshttp://en.wikipedia.org/wiki/Integral_membrane_proteinshttp://en.wikipedia.org/wiki/Integral_membrane_proteinshttp://en.wikipedia.org/wiki/Integral_membrane_proteinshttp://en.wikipedia.org/wiki/Cytosolhttp://en.wikipedia.org/wiki/Cytosolhttp://en.wikipedia.org/wiki/Cytosolhttp://en.wikipedia.org/wiki/Cytosolhttp://en.wikipedia.org/wiki/Integral_membrane_proteinshttp://en.wikipedia.org/wiki/Integral_membrane_proteinshttp://en.wikipedia.org/wiki/Secretory_proteinhttp://en.wikipedia.org/wiki/Glycosylationhttp://en.wikipedia.org/wiki/Posttranslational_modificationhttp://en.wikipedia.org/wiki/Posttranslational_modificationhttp://en.wikipedia.org/wiki/Translation_(genetics)http://en.wikipedia.org/wiki/Peptidehttp://en.wikipedia.org/wiki/Covalent_bondhttp://en.wikipedia.org/wiki/Glycanshttp://en.wikipedia.org/wiki/Oligosaccharidehttp://en.wikipedia.org/wiki/Protein


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Glycoaminoglycans

Glycosaminoglycans(GAGs)or mucopolysaccharidesare longunbranched polysaccharidesconsisting of arepeating disaccharideunit. The repeating unit

(except for keratan) consistsof an amino sugar(N-acetylglucosamineor N-acetylgalactosamine) along with a uronicsugar(glucuronic acidor iduronic acid)or galactose.[3]Glycosaminoglycans are highly

polar and attract water. They are thereforeuseful to the body as a lubricant or as a shockabsorber.
http://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Disaccharidehttp://en.wikipedia.org/wiki/Disaccharidehttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Disaccharidehttp://en.wikipedia.org/wiki/Keratan_sulfatehttp://en.wikipedia.org/wiki/Disaccharidehttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/Uronic_acidhttp://en.wikipedia.org/wiki/Glucuronic_acidhttp://en.wikipedia.org/wiki/Glucuronic_acidhttp://en.wikipedia.org/wiki/Iduronic_acidhttp://en.wikipedia.org/wiki/Iduronic_acidhttp://en.wikipedia.org/wiki/Uronic_acidhttp://en.wikipedia.org/wiki/Uronic_acidhttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Glycosaminoglycanhttp://en.wikipedia.org/wiki/Glucuronic_acidhttp://en.wikipedia.org/wiki/Iduronic_acidhttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Glycosaminoglycanhttp://en.wikipedia.org/wiki/Glycosaminoglycanhttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Iduronic_acidhttp://en.wikipedia.org/wiki/Iduronic_acidhttp://en.wikipedia.org/wiki/Iduronic_acidhttp://en.wikipedia.org/wiki/Glucuronic_acidhttp://en.wikipedia.org/wiki/Glucuronic_acidhttp://en.wikipedia.org/wiki/Glucuronic_acidhttp://en.wikipedia.org/wiki/Uronic_acidhttp://en.wikipedia.org/wiki/Uronic_acidhttp://en.wikipedia.org/wiki/Uronic_acidhttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-Acetylgalactosaminehttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/Keratan_sulfatehttp://en.wikipedia.org/wiki/Disaccharidehttp://en.wikipedia.org/wiki/Polysaccharide


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GlycosylationGlycosylation(see also chemical glycosylation) is the reaction inwhich a carbohydrate, i.e. a glycosyl donor, is attached to ahydroxyl or other functional group of another molecule(a glycosyl acceptor). In biology glycosylationmainly refers inparticular to the enzymatic process thatattaches glycansto proteins, lipids, or other organic molecules.This enzymatic process produces one of thefundamentalbiopolymersfound in cells (along with DNA, RNA,and proteins). Glycosylation is a form of co-translationaland post-translational modification. Glycans serve a variety ofstructural and functional roles in membrane and secretedproteins. The majority of proteins synthesized intherough ERundergo glycosylation. It is an enzyme-directed site-specific process, as opposed to the non-enzymatic chemicalreaction of glycation
http://en.wikipedia.org/wiki/Carbohydratehttp://en.wikipedia.org/wiki/Carbohydratehttp://en.wikipedia.org/wiki/Chemical_glycosylationhttp://en.wikipedia.org/wiki/Glycosyl_donorhttp://en.wikipedia.org/wiki/Chemical_glycosylationhttp://en.wikipedia.org/wiki/Carbohydratehttp://en.wikipedia.org/wiki/Glycosyl_donorhttp://en.wikipedia.org/wiki/Glycosyl_acceptorhttp://en.wikipedia.org/wiki/Glycosyl_acceptorhttp://en.wikipedia.org/wiki/Glycanshttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Glycolipidhttp://en.wikipedia.org/wiki/Glycanshttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Glycolipidhttp://en.wikipedia.org/wiki/Glycosidehttp://en.wikipedia.org/wiki/Biopolymershttp://en.wikipedia.org/wiki/Proteinshttp://en.wikipedia.org/wiki/Biopolymershttp://en.wikipedia.org/wiki/DNAhttp://en.wikipedia.org/wiki/RNAhttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Endoplasmic_reticulumhttp://en.wikipedia.org/wiki/Enzymehttp://en.wikipedia.org/wiki/Endoplasmic_reticulumhttp://en.wikipedia.org/wiki/Enzymehttp://en.wikipedia.org/wiki/Glycationhttp://en.wikipedia.org/wiki/Glycationhttp://en.wikipedia.org/wiki/Glycationhttp://en.wikipedia.org/wiki/Enzymehttp://en.wikipedia.org/wiki/Endoplasmic_reticulumhttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Proteinshttp://en.wikipedia.org/wiki/RNAhttp://en.wikipedia.org/wiki/DNAhttp://en.wikipedia.org/wiki/Biopolymershttp://en.wikipedia.org/wiki/Glycosidehttp://en.wikipedia.org/wiki/Glycolipidhttp://en.wikipedia.org/wiki/Glycoproteinhttp://en.wikipedia.org/wiki/Glycanshttp://en.wikipedia.org/wiki/Glycosyl_acceptorhttp://en.wikipedia.org/wiki/Glycosyl_acceptorhttp://en.wikipedia.org/wiki/Glycosyl_acceptorhttp://en.wikipedia.org/wiki/Glycosyl_donorhttp://en.wikipedia.org/wiki/Glycosyl_donorhttp://en.wikipedia.org/wiki/Glycosyl_donorhttp://en.wikipedia.org/wiki/Carbohydratehttp://en.wikipedia.org/wiki/Chemical_glycosylationhttp://en.wikipedia.org/wiki/Chemical_glycosylation


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The end of chapter 2.

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BEU11403 Biomaterials_Lecture 2.pdf