Challenges and Solutions for Purification of ADAMTS Proteases: An Overview.

[en] ADAMTS are secreted metalloproteinases implicated in many key biological processes. The 19 different members of this family share an identical domain composition at the level of their amino-terminal portion, whereas the identity and number of the domains forming their carboxy-terminal half are divergent and define distinct ADAMTS subfamilies. Due to their large size, extensive glycosylation, the presence of specific domains, their tendency to form aggregates, their relatively low abundance in tissues and the presence of many disulfide bonds, ADAMTS are very hard to isolate, express, and purify, as either native or recombinant active enzymes. This chapter provides an overview of critical steps to take into account when obtaining these proteases for biochemical and functional investigation.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Colige, Alain ; Université de Liège - ULiège > Cancer-Connective Tissue Biology

Language :

English

Title :

Challenges and Solutions for Purification of ADAMTS Proteases: An Overview.

Publication date :

2020

Journal title :

Methods in Molecular Biology

Peer reviewed :

Peer reviewed

Available on ORBi :

since 15 May 2020

Statistics

Number of views

70 (7 by ULiège)

Number of downloads

116 (6 by ULiège)

More statistics

Scopus citations^®

Scopus citations^®
without self-citations

OpenCitations

Bibliography

Apte, S.S., Parks, W.C., Metalloproteinases: A parade of functions in matrix biology and an outlook for the future (2015) Matrix Biol, 44-46, pp. 1-6. , https://doi.org/10.1016/j.matbio.2015.04. 005
Kelwick, R., Desanlis, I., Wheeler, G.N., Edwards, D.R., The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family (2015) Genome Biol, 16 (113). , https://doi.org/10.1186/s13059-015-0676-3
Dubail, J., Apte, S.S., Insights on ADAMTS proteases and ADAMTS-like proteins from mammalian genetics (2015) Matrix Biol, 44-46, pp. 24-37. , https://doi.org/10.1016/j.matbio.2015.03.001
Flannery, C.R., Zeng, W., Corcoran, C., Collins-Racie, L.A., Chockalingam, P.S., Hebert, T., Mackie, S.A., Morris, E.A., Autocatalytic cleavage of ADAMTS-4 (Aggrecanase-1) reveals multiple glycosamino-glycan-binding sites (2002) J Biol Chem, 277 (45), pp. 42775-42780
Rao, N., Ke, Z., Liu, H., Ho, C.J., Kumar, S., Xiang, W., Zhu, Y., Ge, R., ADAMTS4 and its proteolytic fragments differentially affect melanoma growth and angiogenesis in mice (2013) Int J Cancer, 133 (2), pp. 294-306. , https://doi.org/10.1002/ijc.28037
Colige, A., Vandenberghe, I., Thiry, M., Lambert, C.A., van Beeumen, J., Li, S.W., Prockop, D.J., Nusgens, B.V., Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3 (2002) J Biol Chem, 277 (8), pp. 5756-5766
Bekhouche, M., Colige, A., The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology (2015) Matrix Biol, 44, pp. 46-53. , https://doi.org/10.1016/j.matbio.2015.04.001
Colige, A., Ruggiero, F., Vandenberghe, I., Dubail, J., Kesteloot, F., van Beeumen, J., Beschin, A., Nusgens, B., Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropep-tide of fibrillar procollagens types I-III and V (2005) J Biol Chem, 280 (41), pp. 34397-34408
Bekhouche, M., Leduc, C., Dupont, L., Janssen, L., Delolme, F., Vadon-Le Goff, S., Smargiasso, N., Colige, A., Determination of the substrate repertoire of ADAMTS2, 3, and 14 significantly broadens their functions and identifies extracellular matrix organization and TGF-β signaling as primary targets (2016) FASEB J, 30 (5), pp. 1741-1756. , https://doi.org/10.1096/fj.15-279869
Janssen, L., Dupont, L., Bekhouche, M., Noel, A., Leduc, C., Voz, M., Peers, B., Colige, A., ADAMTS3 activity is mandatory for embryonic lymphangiogenesis and regulates placental angiogenesis (2016) Angiogenesis, 19 (1), pp. 53-65. , https://doi.org/10.1007/s10456-015-9488-z
Brouillard, P., Dupont, L., Helaers, R., Coulie, R., Tiller, G.E., Peeden, J., Colige, A., Vikkula, M., Loss of ADAMTS3 activity causes Hen-nekam lymphangiectasia-lymphedema syndrome 3 (2017) Hum Mol Genet, 26 (21), pp. 4095-4104
Bourhis, J.M., Vadon-Le Goff, S., Afrache, H., Mariano, N., Kronenberg, D., Thielens, N., Moali, C., Hulmes, D.J., Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation (2013) Proc Natl Acad Sci U S A, 110 (16), pp. 6394-6399
Jeltsch, M., Jha, S.K., Tvorogov, D., Anisimov, A., Lepp€Anen, V.M., Holopainen, T., Kivel€A, R., Alitalo, K., CCBE1 enhances lymphangiogenesis via A disintegrin and metalloprotease with thrombospondin motifs-3-mediated vascular endothelial growth factor-C activation (2014) Circulation, 129 (19), pp. 1962-1971
Lee, N.V., Rodriguez-Manzaneque, J.C., Thai, S.-M., Twal, W.O., Luque, A., Lyons, K.M., Argraves, W.S., Iruela-Arispe, M.L., Fibulin-1 acts as a cofactor for the matrix metalloprotease ADAMTS-1 (2005) J Biol Chem, 280 (41), pp. 34796-34804. , https://doi.org/10.1074/jbc.M506980200
McCulloch, D.R., Nelson, C.M., Dixon, L.J., Silver, D.L., Wylie, J.D., Lindner, V., Sasaki, T., Apte, S.S., ADAMTS metalloproteases generate active versican fragments that regulate interdigital web regression (2009) Dev Cell, 17, pp. 687-698
Doucet, A., Kleifeld, O., Kizhakkedathu, J.N., Overall, C.M., Identification of proteolytic products and natural protein N-termini by terminal amine isotopic labeling of substrates (TAILS) (2011) Methods Mol Biol, 753, pp. 273-287. , https://doi.org/10.1007/978-1-61779-148-2_18
Kleifeld, O., Doucet, A., Auf Dem Keller, U., Prudova, A., Schilling, O., Kainthan, R.K., Starr, A.E., Overall, C.M., Isotopic labeling of terminal amines in complex samples identifies protein N-termini and protease cleavage products (2010) Nat Biotechnol, 28 (3), pp. 281-288. , https://doi.org/10.1038/nbt.1611