Abstract
Multidomain matrix-associated zinc extracellular proteases ADAMTS and ADAMTS-like proteins have important biological activities in cells and tissues. Beyond their traditional role in procollagen and von Willebrand factor processing and proteoglycan cleavage, ADAMTS/ADAMTSL likely participate in or at least have some role in ECM assembly as some of these proteins bind ECM proteins including fibrillins, fibronectin, and LTBPs. In this chapter, we present four biophysical techniques largely used for the characterization, multimerization, and interaction of proteins: surface plasmon resonance spectroscopy, dynamic light scattering, atomic force microscopy, and circular dichroism spectroscopy.
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References
Apte SS (2004) A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. Int J Biochem Cell Biol 36:981–985
Kelwick R, Desanlis I, Wheeler GN et al (2015) The ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs) family. Genome Biol 16:113
Isogai Z, Aspberg A, Keene DR et al (2002) Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks. J Biol Chem 277:4565–4572
Hubmacher D, Apte SS (2011) Genetic and functional linkage between ADAMTS superfamily proteins and fibrillin-1: a novel mechanism influencing microfibril assembly and function. Cell Mol Life Sci 68:3137–3148
Tsutsui K, Manabe R, Yamada T et al (2010) ADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-1 and promotes fibrillin-1 fibril formation. J Biol Chem 285:4870–4882
Hubmacher D, Wang LW, Mecham RP et al (2015) Adamtsl2 deletion results in bronchial fibrillin microfibril accumulation and bronchial epithelial dysplasia – a novel mouse model providing insights into geleophysic dysplasia. Dis Model Mech 8:487–499
Wang LW, Kutz WE, Mead TJ et al (2019) Adamts10 inactivation in mice leads to persistence of ocular microfibrils subsequent to reduced fibrillin-2 cleavage. Matrix Biol. https://doi.org/10.1016/j.matbio.2018.09.004
Robertson IB, Horiguchi M, Zilberberg L et al (2015) Latent TGF-beta-binding proteins. Matrix Biol 47:44–53
Bekhouche M, Leduc C, Dupont L et al (2016) Determination of the substrate repertoire of ADAMTS2, 3, and 14 significantly broadens their functions and identifies extracellular matrix organization and TGF-beta signaling as primary targets. FASEB J 30:1741–1756
Schnellmann R, Sack R, Hess D et al (2018) A selective extracellular matrix proteomics approach identifies fibronectin proteolysis by a disintegrin-like and metalloprotease domain with thrombospondin type 1 motifs (ADAMTS16) and its impact on spheroid morphogenesis. Mol Cell Proteomics 17:1410–1425
Sengle G, Tsutsui K, Keene DR et al (2012) Microenvironmental regulation by fibrillin-1. PLoS Genet 8:e1002425
Le Goff C, Cormier-Daire V (2011) The ADAMTS(L) family and human genetic disorders. Hum Mol Genet 20:R163–R167
Kutz WE, Wang LW, Bader HL et al (2011) ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts. J Biol Chem 286:17156–17167
Hubmacher D, Schneider M, Berardinelli SJ et al (2017) Unusual life cycle and impact on microfibril assembly of ADAMTS17, a secreted metalloprotease mutated in genetic eye disease. Sci Rep 7:41871
Nelea V, Nakano Y, Kaartinen MT (2008) Size distribution and molecular associations of plasma Fibronectin and Fibronectin crosslinked by transglutaminase 2. Protein J 27:223–233
Hubmacher D, El-Hallous EI, Nelea V et al (2008) Biogenesis of extracellular microfibrils: multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assembly. Proc Natl Acad Sci U S A 105:6548–6553
Yeo GC, Baldock C, Wise SG et al (2014) A negatively charged residue stabilizes the tropoelastin N-terminal region for elastic fiber assembly. J Biol Chem 289:34815–34826
Eckersley A, Mellody KT, Pilkington S et al (2018) Structural and compositional diversity of fibrillin microfibrils in human tissues. J Biol Chem 293:5117–5133
Sherratt MJ, Holmes DF, Shuttleworth CA et al (2004) Substrate-dependent morphology of supramolecular assemblies: fibrillin and type-VI collagen microfibrils. Biophys J 86:3211–3222
Nelea V, Kaartinen MT (2010) Periodic beaded-filament assembly of fibronectin on negatively charged surface. J Struct Biol 170:50–59
Djokic J, Fagotto-Kaufmann C, Bartels R et al (2013) Fibulin-3,-4, and-5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers. J Biol Chem 288:22821–22835
Reinhardt DP, Mechling DE, Boswell BA et al (1997) Calcium determines the shape of fibrillin. J Biol Chem 272:7368–7373
Lauer-Fields JL, Minond D, Sritharan T et al (2007) Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity - Suggestion of a common topological specificity for functionally diverse proteases. J Biol Chem 282:142–150
Douzi B (2017) Protein-protein Interactions: surface plasmon resonance. Methods Mol Biol 1615:257–275
Goldburg WI (1999) Dynamic light scattering. Am J Physiol 67:1152–1160
Stetefeld J, McKenna SA, Patel TR (2016) Dynamic light scattering: a practical guide and applications in biomedical sciences. Biophys Rev 8:409–427
Koppel DE (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy - method of cumulants. J Chem Phys 57:4814–4820
Provencher SW (1982) Contin - a general-purpose constrained regularization program for inverting noisy linear algebraic and integral-equations. Comput Phys Commun 27:229–242
Provencher SW (1982) A constrained regularization method for inverting data represented by linear algebraic or integral-equations. Comput Phys Commun 27:213–227
Hansma HG, Kim KJ, Laney DE et al (1997) Properties of biomolecules measured from atomic force microscope images: a review. J Struct Biol 119:99–108
Santos NC, Castanho MARB (2004) An overview of the biophysical applications of atomic force microscopy. Biophys Chem 107:133–149
Whited AM, Park PSH (2014) Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands. Biochim Biophys Acta 1838:56–68
Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1:2876–2890
Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89:392–400
Sreerama N, Woody RW (1993) A self-consistent method for the analysis of protein secondary structure from circular-dichroism. Biophys J 64:A170–A170
Sreerama N, Venyaminov SY, Woody RW (1999) Estimation of the number of alpha-helical and beta-strand segments in proteins using CD spectroscopy. Biophys J 76:A381–A381
Provencher SW, Glockner J (1981) Estimation of globular protein secondary structure from circular-dichroism. Biochemistry 20:33–37
Vanstokkum IHM, Spoelder HJW, Bloemendal M et al (1990) Estimation of protein secondary structure and error analysis from circular-dichroism spectra. Anal Biochem 191:110–118
Compton LA, Johnson WC (1986) Analysis of protein circular-dichroism spectra for secondary structure using a simple matrix multiplication. Anal Biochem 155:155–167
Manavalan P, Johnson WC (1987) Variable selection method improves the prediction of protein secondary structure from circular-dichroism spectra. Anal Biochem 167:76–85
Sreerama N, Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287:252–260
Andrade MA, Chacon P, Merelo JJ et al (1993) Evaluation of secondary structure of proteins from Uv circular-dichroism spectra using an unsupervised learning neural-network. Protein Eng 6:383–390
Abdul-Gader A, Miles AJ, Wallace BA (2011) A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy. Bioinformatics 27:1630–1636
Evans P, Bateman OA, Slingsby C et al (2007) A reference dataset for circular dichroism spectroscopy tailored for the beta gamma-crystallin lens proteins. Exp Eye Res 84:1001–1008
Lees JG, Miles AJ, Wien F et al (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22:1955–1962
Sreerama N, Venyaminov SY, Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal Biochem 287:243–251
Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32:W668–W673
Lobley A, Whitmore L, Wallace BA (2002) DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18:211–212
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Nelea, V., Reinhardt, D.P. (2020). Biophysical Techniques to Analyze Elastic Tissue Extracellular Matrix Proteins Interacting with ADAMTS Proteins. In: Apte, S. (eds) ADAMTS Proteases. Methods in Molecular Biology, vol 2043. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9698-8_18
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DOI: https://doi.org/10.1007/978-1-4939-9698-8_18
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