ArticleProtein science : a publication of the Protein Society2005
Beta2-microglobulin isoforms display an heterogeneous affinity for type I collagen.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 61 citations in OpenAlex.
- Helical superstructures between amyloid and collagen in cardiac fibrils from a patient with AL amyloidosis.Nature communications · 2024Article
- Pathogenic D76N Variant of βBiology · 2021Article
- Collagen I Weakly Interacts with the β-Sheets of βJournal of the American Chemical Society · 2020Article
- The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations.Frontiers in molecular biosciences · 2020Review
- Extracellular matrix components modulate different stages in βThe Journal of biological chemistry · 2019Article
- Progression of dialysis-related amyloidoma towards pathologic fracture.Skeletal radiology · 2019Article
- Influence of heparin molecular size on the induction of C- terminal unfolding in β2-microglobulin.Molecular biology research communications · 2016Article
- Dialysis-related amyloidosis: challenges and solutions.International journal of nephrology and renovascular disease · 2016Review
- Systemic amyloidosis: lessons from β2-microglobulin.The Journal of biological chemistry · 2015Review
- Transthyretin-derived amyloidosis: probably a common cause of lumbar spinal stenosis.Upsala journal of medical sciences · 2014Article
- A simulated intermediate state for folding and aggregation provides insights into ΔN6 β2-microglobulin amyloidogenic behavior.PLoS computational biology · 2014Article
- Article
- Misfolding of amyloidogenic proteins and their interactions with membranes.Biomolecules · 2013Review
- Understanding the complex mechanisms of β2-microglobulin amyloid assembly.The FEBS journal · 2011Review
- Conformational conversion during amyloid formation at atomic resolution.Molecular cell · 2011Article
- Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils.PloS one · 2011Article
- Systemic amyloidosis: a challenge for the rheumatologist.Nature reviews. Rheumatology · 2010Review
- Protein folding and misfolding on surfaces.International journal of molecular sciences · 2008Article
- Molecular dynamics simulation suggests possible interaction patterns at early steps of beta2-microglobulin aggregation.Biophysical journal · 2007Article
- Natively folded HypF-N and its early amyloid aggregates interact with phospholipid monolayers and destabilize supported phospholipid bilayers.Biophysical journal · 2006Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been claimed that beta2-microglobulin (beta2-m) interacts with type I and type II collagen, and this property has been linked to the tissue specificity of the beta2-m amyloid deposits that target the osteo-articular system. The binding parameters of the interaction between collagen and beta2-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 beta2-m. Wild-type beta2-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 beta2-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 beta2-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 beta2-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.
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