[66]The inter-α-trypsin inhibitor
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Cited by (61)
Matrix-degrading protease ADAMTS-5 cleaves inter-αinhibitor and releases active heavy chain 2 in synovial fluids from arthritic patients
2019, Journal of Biological ChemistryCitation Excerpt :In addition, indirect evidence based on sequence identity suggests that the related HC5 (UniProt C9J2H1) (8) and possibly HC6 (UniProt Q6UXX5), but not HC4 (UniProt Q14624), can also become attached to the bikunin CS chain. IαI is produced primarily in the liver and is found in plasma at concentrations up to ∼0.5 mg/ml (9). This protein is involved in diverse biological processes such as ovulation, cell migration, and inflammation (10) in addition to playing roles in the stabilization and remodeling of extracellular matrix (ECM) (11).
Characterization of complexes formed between TSG-6 and inter-α- inhibitor that act as intermediates in the covalent transfer of heavy chains onto hyaluronan
2005, Journal of Biological ChemistryCitation Excerpt :MgCl2 at the nominal concentration of5 mm was chosen as the standard. The above experiments therefore allowed us to determine the conditionsunder which optimal amounts of TSG-6·IαI complex could be formed.Under the standard conditions chosen (i.e. 80 μg/ml TSG-6 and 320μg/ml IαI in 20 mm HEPES-HCl (pH 7.5), 150 mmNaCl, and 5 mm MgCl2), which are close to physiological,IαI was at a concentration similar to that found in normal human serum(i.e. 400–500 μg/ml(42)). Effect of Divalent Metal Ions onTSG-6·IαI Complex Formation—Asdescribed above, TSG-6·IαI complexes could be formed in thepresence of MgCl2, but did not form in the absence of added metalion (Supplemental Fig. S2).
The TSG-6 and IαI interaction promotes a transesterification cleaving the protein-glycosaminoglycan-protein (PGP) cross-link
2005, Journal of Biological ChemistryBiological Function of SHAP-Hyaluronan Covalent Complex
2004, Chemistry and Biology of HyaluronanImpaired fertility in female mice lacking urinary trypsin inhibitor
2001, Biochemical and Biophysical Research CommunicationsBinding of Zn<sup>2+</sup> to the plasma protein inter-α-inhibitor
1999, Clinica Chimica Acta