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Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review.

Juneja SC, Veillette C - Arthritis (2013)

Bottom Line: This review summarizes the genetic alterations and knockdown approaches published in the literature to assess the role of key proteoglycans and glycoproteins in the structural development, function, and repair of tendon, ligament, and enthesis.The genes reviewed are for small leucine-rich proteoglycans (lumican, fibromodulin, biglycan, decorin, and asporin); dermatan sulfate epimerase (Dse) that alters structure of glycosaminoglycan and hence the function of small leucine-rich proteoglycans by converting glucuronic to iduronic acid; matricellular proteins (thrombospondin 2, secreted phosphoprotein 1 (Spp1), secreted protein acidic and rich in cysteine (Sparc), periostin, and tenascin X) including human tenascin C variants; and others, such as tenomodulin, leukocyte cell derived chemotaxin 1 (chondromodulin-I, ChM-I), CD44 antigen (Cd44), lubricin (Prg4), and aggrecan degrading gene, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 5 (Adamts5).Understanding these genes represents drug targets for disrupting pathological mechanisms that lead to tendinopathy, ligamentopathy, enthesopathy, enthesitis and tendon/ligament injury, that is, osteoarthritis and ankylosing spondylitis.

View Article: PubMed Central - PubMed

Affiliation: Arthritis Program, Division of Orthopaedic Surgery, Toronto Western Hospital, Toronto, ON, Canada M5T 2S8.

ABSTRACT
This review summarizes the genetic alterations and knockdown approaches published in the literature to assess the role of key proteoglycans and glycoproteins in the structural development, function, and repair of tendon, ligament, and enthesis. The information was collected from (i) genetically altered mice, (ii) in vitro knockdown studies, (iii) genetic variants predisposition to injury, and (iv) human genetic diseases. The genes reviewed are for small leucine-rich proteoglycans (lumican, fibromodulin, biglycan, decorin, and asporin); dermatan sulfate epimerase (Dse) that alters structure of glycosaminoglycan and hence the function of small leucine-rich proteoglycans by converting glucuronic to iduronic acid; matricellular proteins (thrombospondin 2, secreted phosphoprotein 1 (Spp1), secreted protein acidic and rich in cysteine (Sparc), periostin, and tenascin X) including human tenascin C variants; and others, such as tenomodulin, leukocyte cell derived chemotaxin 1 (chondromodulin-I, ChM-I), CD44 antigen (Cd44), lubricin (Prg4), and aggrecan degrading gene, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 5 (Adamts5). Understanding these genes represents drug targets for disrupting pathological mechanisms that lead to tendinopathy, ligamentopathy, enthesopathy, enthesitis and tendon/ligament injury, that is, osteoarthritis and ankylosing spondylitis.

No MeSH data available.


Related in: MedlinePlus

Remodeling of the PDL of incisors is defective in Postn−/− mice. H&E-stained PDL section from 12week Postn+/+ (a) and Postn−/− (b) mice. Arrows indicate the shear zone, which is the boundary between the TR (tooth-related) and AR (alveolus-related) regions. The shear zone is clearly visible in 12 week old Postn+/+ mouse (a) and absent in Postn−/− mouse (b). TEM of the incisor PDL shows evidence of digestion of collagen fibers in Postn+/+ (c) but undigested and abundant collagen bundles in Postn−/− mice (d). De, dentin; Al, alveolar bone. (Reprinted from Kii et al., 2006 [102], with permission, Elsevier 2006, and thanks to Dr. A. Kudo for his generous approval.)
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fig4: Remodeling of the PDL of incisors is defective in Postn−/− mice. H&E-stained PDL section from 12week Postn+/+ (a) and Postn−/− (b) mice. Arrows indicate the shear zone, which is the boundary between the TR (tooth-related) and AR (alveolus-related) regions. The shear zone is clearly visible in 12 week old Postn+/+ mouse (a) and absent in Postn−/− mouse (b). TEM of the incisor PDL shows evidence of digestion of collagen fibers in Postn+/+ (c) but undigested and abundant collagen bundles in Postn−/− mice (d). De, dentin; Al, alveolar bone. (Reprinted from Kii et al., 2006 [102], with permission, Elsevier 2006, and thanks to Dr. A. Kudo for his generous approval.)

Mentions: Tendon, enthuses, and ligament defects in response to genetic alterations: role of proteoglycans and glycoproteins.


Defects in tendon, ligament, and enthesis in response to genetic alterations in key proteoglycans and glycoproteins: a review.

Juneja SC, Veillette C - Arthritis (2013)

Remodeling of the PDL of incisors is defective in Postn−/− mice. H&E-stained PDL section from 12week Postn+/+ (a) and Postn−/− (b) mice. Arrows indicate the shear zone, which is the boundary between the TR (tooth-related) and AR (alveolus-related) regions. The shear zone is clearly visible in 12 week old Postn+/+ mouse (a) and absent in Postn−/− mouse (b). TEM of the incisor PDL shows evidence of digestion of collagen fibers in Postn+/+ (c) but undigested and abundant collagen bundles in Postn−/− mice (d). De, dentin; Al, alveolar bone. (Reprinted from Kii et al., 2006 [102], with permission, Elsevier 2006, and thanks to Dr. A. Kudo for his generous approval.)
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3842050&req=5

fig4: Remodeling of the PDL of incisors is defective in Postn−/− mice. H&E-stained PDL section from 12week Postn+/+ (a) and Postn−/− (b) mice. Arrows indicate the shear zone, which is the boundary between the TR (tooth-related) and AR (alveolus-related) regions. The shear zone is clearly visible in 12 week old Postn+/+ mouse (a) and absent in Postn−/− mouse (b). TEM of the incisor PDL shows evidence of digestion of collagen fibers in Postn+/+ (c) but undigested and abundant collagen bundles in Postn−/− mice (d). De, dentin; Al, alveolar bone. (Reprinted from Kii et al., 2006 [102], with permission, Elsevier 2006, and thanks to Dr. A. Kudo for his generous approval.)
Mentions: Tendon, enthuses, and ligament defects in response to genetic alterations: role of proteoglycans and glycoproteins.

Bottom Line: This review summarizes the genetic alterations and knockdown approaches published in the literature to assess the role of key proteoglycans and glycoproteins in the structural development, function, and repair of tendon, ligament, and enthesis.The genes reviewed are for small leucine-rich proteoglycans (lumican, fibromodulin, biglycan, decorin, and asporin); dermatan sulfate epimerase (Dse) that alters structure of glycosaminoglycan and hence the function of small leucine-rich proteoglycans by converting glucuronic to iduronic acid; matricellular proteins (thrombospondin 2, secreted phosphoprotein 1 (Spp1), secreted protein acidic and rich in cysteine (Sparc), periostin, and tenascin X) including human tenascin C variants; and others, such as tenomodulin, leukocyte cell derived chemotaxin 1 (chondromodulin-I, ChM-I), CD44 antigen (Cd44), lubricin (Prg4), and aggrecan degrading gene, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 5 (Adamts5).Understanding these genes represents drug targets for disrupting pathological mechanisms that lead to tendinopathy, ligamentopathy, enthesopathy, enthesitis and tendon/ligament injury, that is, osteoarthritis and ankylosing spondylitis.

View Article: PubMed Central - PubMed

Affiliation: Arthritis Program, Division of Orthopaedic Surgery, Toronto Western Hospital, Toronto, ON, Canada M5T 2S8.

ABSTRACT
This review summarizes the genetic alterations and knockdown approaches published in the literature to assess the role of key proteoglycans and glycoproteins in the structural development, function, and repair of tendon, ligament, and enthesis. The information was collected from (i) genetically altered mice, (ii) in vitro knockdown studies, (iii) genetic variants predisposition to injury, and (iv) human genetic diseases. The genes reviewed are for small leucine-rich proteoglycans (lumican, fibromodulin, biglycan, decorin, and asporin); dermatan sulfate epimerase (Dse) that alters structure of glycosaminoglycan and hence the function of small leucine-rich proteoglycans by converting glucuronic to iduronic acid; matricellular proteins (thrombospondin 2, secreted phosphoprotein 1 (Spp1), secreted protein acidic and rich in cysteine (Sparc), periostin, and tenascin X) including human tenascin C variants; and others, such as tenomodulin, leukocyte cell derived chemotaxin 1 (chondromodulin-I, ChM-I), CD44 antigen (Cd44), lubricin (Prg4), and aggrecan degrading gene, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 5 (Adamts5). Understanding these genes represents drug targets for disrupting pathological mechanisms that lead to tendinopathy, ligamentopathy, enthesopathy, enthesitis and tendon/ligament injury, that is, osteoarthritis and ankylosing spondylitis.

No MeSH data available.


Related in: MedlinePlus