Diabetes-induced alterations in tissue collagen and carboxymethyllysine in rat kidneys: Association with increased collagen-degrading proteinases and amelioration by Cu(II)-selective chelation.

[1]  K. Kompoliti Copper , 2015, Journal of the Neurological Sciences.

[2]  G. Cooper,et al.  Physicochemical studies on the copper(II) binding by glycated collagen telopeptides. , 2015, Organic & biomolecular chemistry.

[3]  S. Genuth,et al.  Skin Advanced Glycation End Products Glucosepane and Methylglyoxal Hydroimidazolone Are Independently Associated With Long-term Microvascular Complication Progression of Type 1 Diabetes , 2014, Diabetes.

[4]  M. Crespo-Alonso,et al.  Complex formation equilibria of Cu(II) and Zn(II) with triethylenetetramine and its mono- and di-acetyl metabolites. , 2013, Dalton transactions.

[5]  G. Cooper,et al.  Synthesis of monolysyl advanced glycation endproducts and their incorporation into collagen model peptides. , 2012, Organic letters.

[6]  G. Cooper,et al.  Selective divalent copper chelation for the treatment of diabetes mellitus. , 2012, Current medicinal chemistry.

[7]  J. Handa,et al.  Glycation‐altered proteolysis as a pathobiologic mechanism that links dietary glycemic index, aging, and age‐related disease (in nondiabetics) , 2012, Aging cell.

[8]  Yan Sun,et al.  Sudan black B reduces autofluorescence in murine renal tissue. , 2011, Archives of pathology & laboratory medicine.

[9]  T. Reinheckel,et al.  CD2AP in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survival. , 2011, The Journal of clinical investigation.

[10]  G. Cooper Therapeutic Potential of Copper Chelation with Triethylenetetramine in Managing Diabetes Mellitus and Alzheimer’s Disease , 2011, Drugs.

[11]  Linghong Huang,et al.  Transglutaminase inhibition ameliorates experimental diabetic nephropathy. , 2009, Kidney international.

[12]  R. Doughty,et al.  A copper(II)-selective chelator ameliorates left-ventricular hypertrophy in type 2 diabetic patients: a randomised placebo-controlled study , 2009, Diabetologia.

[13]  G. Cooper,et al.  A copper(II)-selective chelator ameliorates diabetes-evoked renal fibrosis and albuminuria, and suppresses pathogenic TGF-β activation in the kidneys of rats used as a model of diabetes , 2008, Diabetologia.

[14]  T. Peretz,et al.  Cathepsin L Is Responsible for Processing and Activation of Proheparanase through Multiple Cleavages of a Linker Segment* , 2008, Journal of Biological Chemistry.

[15]  C. Lloyd,et al.  Three-colour fluorescence immunohistochemistry reveals the diversity of cells staining for macrophage markers in murine spleen and liver. , 2008, Journal of immunological methods.

[16]  S. Robins Biochemistry and functional significance of collagen cross-linking. , 2007, Biochemical Society transactions.

[17]  V. Monnier,et al.  Effects of Advanced Glycation End Product Modification on Proximal Tubule Epithelial Cell Processing of Albumin , 2007, American Journal of Nephrology.

[18]  C. Wijmenga,et al.  Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes , 2007, Journal of Medical Genetics.

[19]  A. Rudensky,et al.  Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease. , 2007, The Journal of clinical investigation.

[20]  Francesco Leonetti,et al.  Substrate Profiling of Cysteine Proteases Using a Combinatorial Peptide Library Identifies Functionally Unique Specificities* , 2006, Journal of Biological Chemistry.

[21]  Yong-hui Yu,et al.  Effects of benazepril on renal function and kidney expression of matrix metalloproteinase‐2 and tissue inhibitor of metalloproteinase‐2 in diabetic rats , 2006, Chinese medical journal.

[22]  G. Wolf,et al.  Advanced glycation end products and the kidney. , 2005, American journal of physiology. Renal physiology.

[23]  J. Miyazaki,et al.  Establishment of a diabetic mouse model with progressive diabetic nephropathy. , 2005, The American journal of pathology.

[24]  G. Gamble,et al.  Demonstration of a hyperglycemia-driven pathogenic abnormality of copper homeostasis in diabetes and its reversibility by selective chelation: quantitative comparisons between the biology of copper and eight other nutritionally essential elements in normal and diabetic individuals. , 2005, Diabetes.

[25]  V. Monnier,et al.  Glucosepane Is a Major Protein Cross-link of the Senescent Human Extracellular Matrix , 2005, Journal of Biological Chemistry.

[26]  R. Doughty,et al.  Regeneration of the heart in diabetes by selective copper chelation. , 2004, Diabetes.

[27]  K. Gloe,et al.  Metal complexation by the peptide-bound Maillard reaction products N∈-fructoselysine and N∈-carboxymethyllysine , 2004 .

[28]  Anne Dawnay,et al.  Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry. , 2003, The Biochemical journal.

[29]  G. Jerums,et al.  The breakdown of pre‐existing advanced glycation end products is associated with reduced renal fibrosis in experimental diabetes , 2003, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[30]  J. Eaton,et al.  Interactions of copper with glycated proteins: Possible involvement in the etiology of diabetic neuropathy , 2002, Molecular and Cellular Biochemistry.

[31]  T. Sugiyama,et al.  Urinary Copper Excretion in Type 2 Diabetic Patients with Nephropathy , 2001, Nephron.

[32]  Ashutosh Kumar Singh,et al.  High Glucose Decreases Matrix Metalloproteinase-2 Activity in Rat Mesangial Cells via Transforming Growth Factor-β1 , 2001, Nephron Experimental Nephrology.

[33]  L. Beilin,et al.  Advanced glycation end-products: a review , 2001, Diabetologia.

[34]  J. Bijlsma,et al.  Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products* , 2000, The Journal of Biological Chemistry.

[35]  D. Yue,et al.  High glucose concentration inhibits the expression of membrane type metalloproteinase by mesangial cells: possible role in mesangium accumulation , 2000, Diabetologia.

[36]  M. Obrenovich,et al.  Protein aging by carboxymethylation of lysines generates sites for divalent metal and redox active copper binding: relevance to diseases of glycoxidative stress. , 1999, Biochemical and biophysical research communications.

[37]  A. Mitchell,et al.  Copper, lysyl oxidase, and extracellular matrix protein cross-linking. , 1998, The American journal of clinical nutrition.

[38]  L. Creemers,et al.  Gelatinase A (MMP-2) and cysteine proteinases are essential for the degradation of collagen in soft connective tissue. , 1998, Matrix biology : journal of the International Society for Matrix Biology.

[39]  L. Creemers,et al.  Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling , 1996, The Histochemical Journal.

[40]  James P. Quigley,et al.  Matrix Metalloproteinase-2 Is an Interstitial Collagenase , 1995, The Journal of Biological Chemistry.

[41]  J. Bucher,et al.  Subchronic toxicity of cupric sulfate administered in drinking water and feed to rats and mice. , 1993, Fundamental and applied toxicology : official journal of the Society of Toxicology.

[42]  J. Walcott,et al.  STZ-Induced Diabetes Results in Decreased Activity of Glomerular Cathepsin and Metalloprotease in Rats , 1993, Diabetes.

[43]  C. Olbricht,et al.  Renal hypertrophy in streptozotocin diabetic rats: role of proteolytic lysosomal enzymes. , 1992, Kidney international.

[44]  R. Nordquist,et al.  The role of nonenzymatic glycosylation, transition metals, and free radicals in the formation of collagen aggregates. , 1991, Archives of biochemistry and biophysics.

[45]  H. Kühn,et al.  Mode of action of triethylenetetramine dihydrochloride on copper metabolism in Wilson's disease , 1991, Acta neurologica Scandinavica.

[46]  C. Hasslacher,et al.  Degradation of glomerular basement membrane in diabetes , 1987, Research in experimental medicine. Zeitschrift fur die gesamte experimentelle Medizin einschliesslich experimenteller Chirurgie.

[47]  S P Wolff,et al.  Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes. , 1987, The Biochemical journal.

[48]  R. Kohn,et al.  Effects of age and diabetes mellitus on the solubility and nonenzymatic glucosylation of human skin collagen. , 1981, The Journal of clinical investigation.

[49]  J. Uitto,et al.  Increased Collagen Cross-Linkages in Experimental Diabetes: Reversal by β-Aminopropionitrile and D-Penicillamine , 1980, Diabetes.

[50]  I. Bergman,et al.  Two Improved and Simplified Methods for the Spectrophotometric Determination of Hydroxyproline. , 1963 .

[51]  C. Isidoro,et al.  Cathepsins: Getting in Shape for Lysosomal Proteolysis , 2013 .

[52]  M. Juliano,et al.  Lysosomal enzymes are decreased in the kidney of diabetic rats. , 2013, Biochimica et biophysica acta.

[53]  I. Cuthill,et al.  Reporting : The ARRIVE Guidelines for Reporting Animal Research , 2010 .

[54]  J. Baynes,et al.  Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. , 1999, Diabetes.

[55]  A. Bailey,et al.  An efficient method for the isolation of intramuscular collagen. , 1995, Meat science.

[56]  J. Quigley,et al.  Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. , 1995, The Journal of biological chemistry.

[57]  E. Shaw,et al.  The identification of active forms of cysteine proteinases in Kirsten-virus-transformed mouse fibroblasts by use of a specific radiolabelled inhibitor. , 1989, The Biochemical journal.

[58]  V. Neuhoff,et al.  Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G‐250 and R‐250 , 1988, Electrophoresis.

[59]  G. Laurent,et al.  Dynamic state of collagen: pathways of collagen degradation in vivo and their possible role in regulation of collagen mass. , 1987, The American journal of physiology.

[60]  E. J. Miller,et al.  Preparation and characterization of the different types of collagen. , 1982, Methods in enzymology.