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Results: 11 to 12 of 12

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Structure formation in the C terminus of type III collagen guides disulfide cross-linking.
Boudko SP, Engel J
(2004) J Mol Biol 335: 1289-97
MeSH Terms: Calorimetry, Differential Scanning, Circular Dichroism, Collagen Type III, Cross-Linking Reagents, Disulfides, Escherichia coli, Mass Spectrometry, Oxidation-Reduction, Peptide Fragments, Protein Conformation, Protein Folding, Recombinant Proteins, Ultracentrifugation, Viral Proteins
Show Abstract · Added November 2, 2017
In type III collagen the main triple-helical domain is followed by a disulfide knot and the C-terminal propeptide, which are both essential for nucleation, stabilization and registration of the triple helix. We demonstrate that oxidative inter-chain disulfide bridging does not occur between the knot sequences GlyProCysCysGly of dissociated randomly coiled chains. N-terminal fusion of the obligatory trimeric domain of mini-fibritin is able to direct this process efficiently, demonstrating a folded precursor mechanism in which the thiol groups have to be properly placed for the formation of native disulfide bonds. The natural C-propeptide domain may act in a similar way as the mini-fibritin domain. After disulfide linkage and triple-helix formation the catalyzing mini-fibritin domain was removed by thrombin cleavage. In this way a short but stable triple-helical collagen fragment was expressed in Escherichia coli for structural and functional studies.
0 Communities
1 Members
0 Resources
14 MeSH Terms
Absence of angiotensin II type 1 receptor in bone marrow-derived cells is detrimental in the evolution of renal fibrosis.
Nishida M, Fujinaka H, Matsusaka T, Price J, Kon V, Fogo AB, Davidson JM, Linton MF, Fazio S, Homma T, Yoshida H, Ichikawa I
(2002) J Clin Invest 110: 1859-68
MeSH Terms: Animals, Bone Marrow Transplantation, Cell Movement, Collagen Type I, Collagen Type III, Extracellular Matrix, Fibrosis, Hematopoietic Stem Cells, Kidney, Kidney Diseases, Macrophages, Male, Matrix Metalloproteinase 2, Mice, Mice, Inbred C57BL, Mice, Knockout, Phagocytosis, Receptor, Angiotensin, Type 1, Receptors, Angiotensin, Respiratory Burst, Tissue Inhibitor of Metalloproteinase-1, Transforming Growth Factor beta, Transforming Growth Factor beta1, Ureteral Obstruction
Show Abstract · Added December 10, 2013
We examined the in vivo function of the angiotensin II type 1 receptor (Agtr1) on macrophages in renal fibrosis. Fourteen days after the induction of unilateral ureteral obstruction (UUO), wild-type mice reconstituted with marrow lacking the Agtr1 gene (Agtr1(-/-)) developed more severe interstitial fibrosis with fewer interstitial macrophages than those in mice reconstituted with Agtr1(+/+) marrow. These differences were not observed at day 5 of UUO. The expression of profibrotic genes - including TGF-beta1, alpha1(I) collagen, and alpha1(III) collagen - was substantially higher in the obstructed kidneys of mice with Agtr1(-/-) marrow than in those with Agtr1(+/+) marrow at day 14 but not at day 5 of UUO. Mice with Agtr1(-/-) marrow were characterized by reduced numbers of peripheral-blood monocytes and macrophage progenitors in bone marrow. In vivo assays revealed a significantly impaired phagocytic capability in Agtr1(-/-) macrophages. In vivo treatment of Agtr1(+/+) mice with losartan reduced phagocytic capability of Agtr1(+/+) macrophages to a level comparable to that of Agtr1(-/-) macrophages. Thus, during urinary tract obstruction, the Agtr1 on bone marrow-derived macrophages functions to preserve the renal parenchymal architecture, and this function depends in part on its modulatory effect on phagocytosis.
1 Communities
5 Members
0 Resources
24 MeSH Terms