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Proteoglycan in Articular Cartilage

Categorization of proteoglycans depends on the nature of their glycosaminoglycan chains (chondroitin sulfate, dermatan sulfate, heparan sulfate and keratan sulfate), and is also characterized by size. 

Aggrecan is a large aggregating proteoglycan of articular cartilage. It is also found in aorta tissue, discs, tendons and in the perineuronal net. It is responsible for hydrating cartilage, giving it compressibility and resilience during joint loading, thereby playing a major role in the normal function of cartilage. Depletion of glycosaminoglycan-bearing aggrecan fragments is one of the earliest events in cartilage destruction.  Keratocan is an extracellular matrix protein that belongs to the small leucine-rich proteoglycan family which also includes lumican, biglycan, decorin, mimecan and fibromodulin.

Members of this family are known to play a role in regulating cellular processes such as proliferation and modulation of osteo-progenitor lineage differentiation.

 

Aggrecan consists of two globular domains (G1 and G2) at the N-terminal end and one globular domain (G3) at the C-terminal end. Glycosaminoglycan (Keratan Sulfate and Chondroitin Sulfate) chains are distributed between G2 and G3 domains. The Link Protein (LP) acts as a stabilizing protein between G1 and hyaluronan.

Categorization of proteoglycans depends on the nature of their glycosaminoglycan chains (chondroitin sulfate, dermatan sulfate, heparan sulfate and keratan sulfate), and is also characterized by size. 
Aggrecan is a large aggregating proteoglycan of articular cartilage. It is also found in aorta tissue, discs, tendons and in the perineuronal net. It is responsible for hydrating cartilage, giving it compressibility and resilience during joint loading, thereby playing a major role in the normal function of cartilage. Depletion of glycosaminoglycan-bearing aggrecan fragments is one of the earliest events in cartilage destruction.  Keratocan is an extracellular matrix protein that belongs to the small leucine-rich proteoglycan family which also includes lumican, biglycan, decorin, mimecan and fibromodulin.
Members of this family are known to play a role in regulating cellular processes such as proliferation and modulation of osteo-progenitor lineage differentiation.


 

MD Biosciences Aggrecan & Cartilage Products

 

Selection of References to our Aggrecan Metabolite Products

Fragmentation of decorin, biglycan, lumican and keratocan is elevated in degener- ate human meniscus, knee and hip articular cartilages compared with age-matched macroscopically normal and control tissues. Melrose J, Fuller ES, Roughley PJ, Smith MM, Kerr B, Hughes CE, Caterson B, Little CB. (2008) Arthritis Res Ther. 10(4):R79. 

Matrix morphogenesis in cornea is mediated by the modification of keratan sulfate by GlcNAc 6-O-sulfotransferase. Hayashida Y, Akama TO, Beecher N, Lewis P, Young RD, Meek KM, Kerr B, Hughes CE, Caterson B, Tanigami A, Nakayama J, Fukada MN, Tano Y, Nishida K, Quantock AJ. (2006) Proc Natl Acad Sci U S A. 5;103(36):13333-8. 

Immunolocalisation and expression of keratocan in tendon. Rees SG, Waggett AD, Kerr BC, Probert J, Gealy EC, Dent CM, Caterson B, Hughes CE. (2008) Osteoarthritis Cartilage. 

Fragmentation of decorin, biglycan, lumican and keratocan is elevated in degener- ate human meniscus, knee and hip articular cartilages compared with age-matched macroscopically normal and control tissues. Melrose J, Fuller ES, Roughley PJ, Smith MM, Kerr B, Hughes CE, Caterson B, Little CB. (2008) Arthritis Res Ther. 10(4):R79. 

Differential expression of the keratan sulphate proteoglycan, keratocan, during chick corneal embryogenesis. Gealy EC, Kerr BC, Young RD, Tudor D, Hayes AJ, Hughes CE, Caterson B, Quantock AJ, Ralphs JR. (2007) Histochem Cell Biol. Dec;128(6):551-5. 

Caterson, B, Christner, JE, Baker, JR, Couchman, JR. (1985) Production and character- ization of monoclonal antibodies directed against connective tissue proteoglycans Fed Proc 44,386-393 

Couchman, J.R., Caterson, B., Christner, J.E. and Baker, J.R. (1984). Mapping by Monoclonal Antibody Detection of Glycosaminoglycans in Connective Tissues. Nature 307: 650-652 

Rees SG, Flannery CR, Little CB, Hughes CE, Caterson B & Dent CM (2000). Catabolism of aggrecan, decorin and biglycan in tendon. Biochem J. 350: 181-188. 

Hayes AJ, Hall A, Brown L, Tubo R & Caterson B (2007). Macromolecular organization and in vitro growth characteristics of scaffold-free neocartilage grafts. J Histochem Cytochem. 55(8):853-66. 

Hayes AJ, Hughes CE & Caterson B (2008). Antibodies and immunohistochemisrty in extracellular matrix research. Methods 45: 10-21 

Stefan Milz, Frank Regner, Reinhard Putz, and Michael Benjamin. Expression of a Wide Range of Extracellular Matrix Molecules in the Tendon and Trochlea of the Human Superior Oblique MuscleInvestigative Ophthalmology and Visual Science. 2002;43:1330-1334 

Hedlund, H, Hedbom, E, Heinegard, D, Mengarelli-Widholm, S, Reinholt, FP, Svensson, O. (1999) Association of the aggrecan keratan sulfate-rich region with collagen in bovine articular cartilage J Biol Chem 274,5777-5781 

Caterson B, Christner JE & Baker JR (1983). Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibod- ies to cartilage proteoglycan. J Biol Chem. 258(14): 8848-54. 

Thonar EJ, Lenz ME, Klintworth GK, Caterson B, Pachman LM, Glickman P, Katz R, Huff J & Kuettner KE (1985). Quantification of keratan sulfate in blood as a marker of cartilage catabolism. Arthritis & Rheum. 28(12): 1367-76. 

Mehmet H, Scudder P, Tang PW, Hounsell EF, Caterson B & Feizi T (1986). The anti- genic determinants recognized by three monoclonal antibodies to keratan sulphate involve sulphated hepta- or larger oligosaccharides of the poly(N-acetyllactosamine) series. Eur J Biochem. 157(2): 385-91. 

Funderburgh JL, Caterson B & Conrad GW (1987). Distribution of proteoglycans antigenically related to corneal keratan sulfate proteoglycan. J Biol Chem. 262(24):11634-40. 

Rees SG, Flannery CR, Little CB, Hughes CE, Caterson B & Dent CM (2000). Catabolism of aggrecan, decorin and biglycan in tendon. Biochem J. 350: 181-188. 

Young RD, Akama TO, Liskova P, Ebenezer ND, Allan B, Kerr B, Caterson B, Fukuda MN, Quantock AJ (2007a). Differential immunogold localisation of sulphated and unsul- phated keratan sulphate proteoglycans in normal and macular dystrophy cornea using sulphation motif-specific antibodies. Histochem Cell Biol. 127(1):115-20 

Young RD, Gealy EC, Liles M, Caterson B, Ralphs JR & Quantock AJ (2007b). Keratan sulfate glycosaminoglycan and the association with collagen fibrils in rudimen- tary lamellae in the developing avian cornea. Invest Ophthalmol Vis Sci. 2007 Jul;48(7):3083-8. 

Hayes AJ, Hall A, Brown L, Tubo R & Caterson B (2007). Macromolecular organization and in vitro growth characteristics of scaffold-free neocartilage grafts. J Histochem Cytochem. 55(8):853-66. 

Hayes AJ, Hughes CE & Caterson B (2008). Antibodies and immunohistochemisrty in extracellular matrix research. Methods 45: 10-21 

A.J. Hayes et al. (2008) Methods 45:10–21

Couchman JR, Caterson B, Christner JB, Baker JR (1984) Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. Nature 307:650–652

Caterson B, Christner JE, Baker JR, Couchman JR (1985) Production and characterization of monoclonal antibodies directed against connective tissue proteoglycans. Fed Proc 44:386–393

Anthony J. Hayes, Amanda Hall, Liesbeth Brown, Ross Tubo, and Bruce Caterson (2007) Macromolecular Organization and In Vitro Growth Characteristics of Scaffold-free Neocartilage GraftsJournal of Histochemistry & Cytochemistry Volume 55(8): 853–866