ADAMTS Proteoglycanases in the Physiological and Pathological Central Nervous System

Overview

Journal J Neuroinflammation

Publisher Biomed Central

Date 2013 Nov 2

PMID 24176075

Citations 49

Authors

Sighild Lemarchant

Mathilde Pruvost

Joan Montaner

Evelyne Emery

Denis Vivien

Katja Kanninen

Jari Koistinaho

Affiliations

Soon will be listed here.

Abstract

ADAMTS-1, -4, -5 and -9 belong to 'a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)' family and more precisely to the proteoglycanases subgroup based on their common ability to degrade chondroitin sulfate proteoglycans. They have been extensively investigated for their involvement in inflammation-induced osteoarthritis, and a growing body of evidence indicates that they may be of key importance in the physiological and pathological central nervous system (CNS). In this review, we discuss the deregulated expression of ADAMTS proteoglycanases during acute CNS injuries, such as stroke and spinal cord injury. Then, we provide new insights on ADAMTS proteoglycanases mediating synaptic plasticity, neurorepair, angiogenesis and inflammation mechanisms. Altogether, this review allows us to propose that ADAMTS proteoglycanases may be original therapeutic targets for CNS injuries.

Citing Articles

The Role of Perineuronal Nets in Physiology and Disease: Insights from Recent Studies.

Auer S, Schicht M, Hoffmann L, Budday S, Frischknecht R, Blumcke I Cells. 2025; 14(5).

PMID: 40072050 PMC: 11898492. DOI: 10.3390/cells14050321.

Astrocytes originated from neural stem cells drive the regenerative remodeling of pathologic CSPGs in spinal cord injury.

Hosseini S, Nemati S, Karimi-Abdolrezaee S Stem Cell Reports. 2024; 19(10):1451-1473.

PMID: 39303705 PMC: 11561464. DOI: 10.1016/j.stemcr.2024.08.007.

Secretome analysis of oligodendrocytes and precursors reveals their roles as contributors to the extracellular matrix and potential regulators of inflammation.

Godoy M, Pandey V, Wohlschlegel J, Zhang Y bioRxiv. 2024; .

PMID: 39091874 PMC: 11291107. DOI: 10.1101/2024.07.22.604699.

Identifying hub genes of sepsis-associated and hepatic encephalopathies based on bioinformatic analysis-focus on the two common encephalopathies of septic cirrhotic patients in ICU.

Li J, Yang D, Ge S, Liu L, Huo Y, Hu Z BMC Med Genomics. 2024; 17(1):19.

PMID: 38212812 PMC: 10785360. DOI: 10.1186/s12920-023-01774-7.

A view of the genetic and proteomic profile of extracellular matrix molecules in aging and stroke.

Chmelova M, Androvic P, Kirdajova D, Tureckova J, Kriska J, Valihrach L Front Cell Neurosci. 2023; 17:1296455.

PMID: 38107409 PMC: 10723838. DOI: 10.3389/fncel.2023.1296455.

References

Diamantis I, Luthi M, Hosli M, Reichen J . Cloning of the rat ADAMTS-1 gene and its down regulation in endothelial cells in cirrhotic rats. Liver. 2000; 20(2):165-72. DOI: 10.1034/j.1600-0676.2000.020002165.x. View

Cua R, Lau L, Keough M, Midha R, Apte S, Yong V . Overcoming neurite-inhibitory chondroitin sulfate proteoglycans in the astrocyte matrix. Glia. 2013; 61(6):972-84. DOI: 10.1002/glia.22489. View

Siebert J, Osterhout D . The inhibitory effects of chondroitin sulfate proteoglycans on oligodendrocytes. J Neurochem. 2011; 119(1):176-88. DOI: 10.1111/j.1471-4159.2011.07370.x. View

Wagsater D, Bjork H, Zhu C, Bjorkegren J, Valen G, Hamsten A . ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques. Atherosclerosis. 2007; 196(2):514-22. DOI: 10.1016/j.atherosclerosis.2007.05.018. View

Hamel M, Ajmo J, Leonardo C, Zuo F, Sandy J, Gottschall P . Multimodal signaling by the ADAMTSs (a disintegrin and metalloproteinase with thrombospondin motifs) promotes neurite extension. Exp Neurol. 2008; 210(2):428-40. PMC: 2614334. DOI: 10.1016/j.expneurol.2007.11.014. View

Apte S . A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. Int J Biochem Cell Biol. 2004; 36(6):981-5. DOI: 10.1016/j.biocel.2004.01.014. View

Lau L, Keough M, Haylock-Jacobs S, Cua R, Doring A, Sloka S . Chondroitin sulfate proteoglycans in demyelinated lesions impair remyelination. Ann Neurol. 2012; 72(3):419-32. DOI: 10.1002/ana.23599. View

Hill J, Jin K, Mao X, Xie L, Greenberg D . Intracerebral chondroitinase ABC and heparan sulfate proteoglycan glypican improve outcome from chronic stroke in rats. Proc Natl Acad Sci U S A. 2012; 109(23):9155-60. PMC: 3384160. DOI: 10.1073/pnas.1205697109. View

Miguel R, Pollak A, Lubec G . Metalloproteinase ADAMTS-1 but not ADAMTS-5 is manifold overexpressed in neurodegenerative disorders as Down syndrome, Alzheimer's and Pick's disease. Brain Res Mol Brain Res. 2005; 133(1):1-5. DOI: 10.1016/j.molbrainres.2004.09.008. View

10.

Pardeshi C, Belgamwar V . Direct nose to brain drug delivery via integrated nerve pathways bypassing the blood-brain barrier: an excellent platform for brain targeting. Expert Opin Drug Deliv. 2013; 10(7):957-72. DOI: 10.1517/17425247.2013.790887. View

11.

Lim N, Kashiwagi M, Visse R, Jones J, Enghild J, Brew K . Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications. Biochem J. 2010; 431(1):113-22. PMC: 3003256. DOI: 10.1042/BJ20100725. View

12.

Jungers K, Le Goff C, Somerville R, Apte S . Adamts9 is widely expressed during mouse embryo development. Gene Expr Patterns. 2005; 5(5):609-17. DOI: 10.1016/j.modgep.2005.03.004. View

13.

Yuan W, Matthews R, Sandy J, Gottschall P . Association between protease-specific proteolytic cleavage of brevican and synaptic loss in the dentate gyrus of kainate-treated rats. Neuroscience. 2002; 114(4):1091-101. DOI: 10.1016/s0306-4522(02)00347-0. View

14.

Lin E, Liu C . The role of ADAMTSs in arthritis. Protein Cell. 2011; 1(1):33-47. PMC: 4418016. DOI: 10.1007/s13238-010-0002-5. View

15.

Cross A, Haddock G, Stock C, Allan S, Surr J, Bunning R . ADAMTS-1 and -4 are up-regulated following transient middle cerebral artery occlusion in the rat and their expression is modulated by TNF in cultured astrocytes. Brain Res. 2006; 1088(1):19-30. DOI: 10.1016/j.brainres.2006.02.136. View

16.

Lafuente J, Ortuzar N, Bengoetxea H, Bulnes S, Argandona E . Vascular endothelial growth factor and other angioglioneurins: key molecules in brain development and restoration. Int Rev Neurobiol. 2012; 102:317-46. DOI: 10.1016/B978-0-12-386986-9.00012-0. View

17.

Tortorella M, Pratta M, Liu R, Abbaszade I, Ross H, Burn T . The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage. J Biol Chem. 2000; 275(33):25791-7. DOI: 10.1074/jbc.M001065200. View

18.

Flannery C, Zeng W, Corcoran C, Collins-Racie L, Chockalingam P, Hebert T . Autocatalytic cleavage of ADAMTS-4 (Aggrecanase-1) reveals multiple glycosaminoglycan-binding sites. J Biol Chem. 2002; 277(45):42775-80. DOI: 10.1074/jbc.M205309200. View

19.

Tom V, Sandrow-Feinberg H, Miller K, Santi L, Connors T, Lemay M . Combining peripheral nerve grafts and chondroitinase promotes functional axonal regeneration in the chronically injured spinal cord. J Neurosci. 2009; 29(47):14881-90. PMC: 2824589. DOI: 10.1523/JNEUROSCI.3641-09.2009. View

20.

Howell M, Torres-Collado A, Iruela-Arispe M, Gottschall P . Selective decline of synaptic protein levels in the frontal cortex of female mice deficient in the extracellular metalloproteinase ADAMTS1. PLoS One. 2012; 7(10):e47226. PMC: 3469530. DOI: 10.1371/journal.pone.0047226. View