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2-Microglobulin isoforms display an heterogeneous affinity for type I collagen
1 Dipartimento di Biochimica, Università degli Studi di Pavia, Italy
2 Laboratorio di Biotecnologie, IRCCS Policlinico San Matteo Pavia, Italy
3 Dipartimento di Scienze e Tecnologie Biomediche Università degli Studi di Udine, Italy
(RECEIVED October 22, 2004; FINAL REVISION October 22, 2004; ACCEPTED November 25, 2004)
It has been claimed that 
2-microglobulin (2-m) interacts with type I and type II collagen, and this property has been linked to the tissue specificity of the 2-m amyloid deposits that target the osteo-articular system. The binding parameters of the interaction between collagen and 2-m were determined by band shift electrophoresis and surface plasma resonance by using bovine collagen of type I and type II and various isoforms of 2-m. Wild-type 2-m binds collagen type I with a Kd of 4.1 x 10–4 M and type II with 2.3 x 10–3 M. By the BIAcore system we monitored the binding properties of the conformers of the slow phase of folding of 2-m. The folding intermediates during the slow phase of folding do not display any significant difference with respect to the binding properties of the fully folded molecule. The affinity of 2-m truncated at the third N-terminal residue does not differ from that reported for the wild-type protein. Increased affinity for collagen type I is found in the case of N-terminal truncated species lacking of six residues. The Kd of this species is 3.4 x 10 –5 M at pH 7.4 and its affinity increases to 4.9 x 10–6 M at pH 6.4. Fluctuations of the affinity caused by 2-m truncation and pH change can cause modifications of protein concentration in the solvent that surrounds the collagen, and could contribute to generate locally a critical protein concentration able to prime the protein aggregation.
Keywords: 2-microglobulin; collagen; protein–protein interaction; amyloid
Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041194005.
Reprint requests to: Vittorio Bellotti, Dipartimento di Biochimica, Università degli Studi di Pavia, via Taramelli 3/b 27100 Pavia, Italy; e-mail: vbellot{at}unipv.it; fax: +39-0382-423108.
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