A procollagen C-proteinase inhibitor diminishes collagen and lysyl oxidase processing but not collagen cross-linking in osteoblastic cultures

2005 ◽  
Vol 203 (1) ◽  
pp. 111-117 ◽  
Author(s):  
Nicole Pischon ◽  
Hermik Babakhanlou-Chase ◽  
Laurent Darbois ◽  
Wen-Bin Ho ◽  
Mitchell C. Brenner ◽  
...  
Keyword(s):  
Proteinase Inhibitor ◽  
Lysyl Oxidase ◽  
Cross Linking ◽  
Collagen Cross Linking

scholarly journals Impact of Treatment on Myocardial Lysyl Oxidase Expression and Collagen Cross-Linking in Patients With Heart Failure

Hypertension ◽  
2009 ◽  
Vol 53 (2) ◽  
pp. 236-242 ◽  
Author(s):  
Begoña López ◽  
Ramón Querejeta ◽  
Arantxa González ◽  
Javier Beaumont ◽  
Mariano Larman ◽  
...  
Keyword(s):  
Heart Failure ◽  
Lysyl Oxidase ◽  
Cross Linking ◽  
Patients With Heart Failure ◽  
Collagen Cross Linking

Collagen cross-linking: Lysyl oxidase dependent synthesis of pyridinoline in vitro: Confirmation that pyridinoline is derived from collagen

1982 ◽  
Vol 108 (4) ◽  
pp. 1546-1550 ◽  
Author(s):  
Robert C. Siegel ◽  
Joseph C.C. Fu ◽  
Norihiko Uto ◽  
Kentaro Horiuchi ◽  
Daisaburo Fujimoto
Keyword(s):  
Lysyl Oxidase ◽  
Cross Linking ◽  
Collagen Cross Linking

scholarly journals The collagen cross‐linking enzyme lysyl oxidase is associated with the healing of human atherosclerotic lesions

2014 ◽  
Vol 276 (5) ◽  
pp. 525-536 ◽  
Author(s):  
O. A. Ovchinnikova ◽  
L. Folkersen ◽  
J. Persson ◽  
J. H. N. Lindeman ◽  
T. Ueland ◽  
...  
Keyword(s):  
Lysyl Oxidase ◽  
Cross Linking ◽  
Atherosclerotic Lesions ◽  
Collagen Cross Linking

Effects of elevated circulating IGF-1 on the extracellular matrix in "high-growth" C57BL/6J mice

1996 ◽  
Vol 271 (3) ◽  
pp. R696-R703 ◽  
Author(s):  
K. Reiser ◽  
P. Summers ◽  
J. F. Medrano ◽  
R. Rucker ◽  
J. Last ◽  
...  
Keyword(s):  
Gene Expression ◽  
Granulation Tissue ◽  
Posttranslational Modifications ◽  
Lysyl Oxidase ◽  
High Growth ◽  
Cross Linking ◽  
Type I ◽  
Igf Binding Proteins ◽  
Lysyl Hydroxylase ◽  
Collagen Cross Linking

Collagen biosynthesis was analyzed in C57BL/6J mice homozygous for the high-growth locus. Plasma levels of insulin-like growth factor-1 (IGF-1) were significantly elevated in high-growth mice at all ages studied (3 wk-6 mo); IGF-binding proteins were also elevated. Skin biopsies were obtained from mice aged 3, 6, and 9 wk under halothane anesthesia. Mice were killed at 6 mo of age. Collagen, expressed per weight of tissue, was significantly increased in all tissues from high-growth mice, as was collagen cross-linking, expressed as moles of cross-link per mole of collagen. Expression of types I and III collagen, lysyl oxidase, and lysyl hydroxylase was increased in all tissues analyzed. There was a preferential increase in type III expression relative to type I expression. Rate and extent of accumulation of collagen in granulation tissue were measured in polyvinyl alcohol sponges implanted subcutaneously; collagen accumulation was significantly greater in the high-growth mice. These results suggest that 1) elevated circulating IGF-1 may increase collagen deposition both in normal tissue as well as in granulation tissue by increasing collagen gene expression, 2) IGF-1 may increase collagen cross-linking by stimulating expression of lysyl oxidase, and 3) the preferential increase in dihydroxylated cross-links observed in high-growth mice may be due to the stimulation of lysyl hydroxylase expression by IGF-1. In summary, elevated levels of IGF-1 appear to affect collagen both quantitatively and qualitatively, primarily through their effects on gene expression of collagen and of those enzymes responsible for posttranslational modifications of collagen.

Lysyl Oxidase Expression and Collagen Cross-Linking during Chronic Adriamycin Nephropathy

Nephron ◽  
1997 ◽  
Vol 76 (2) ◽  
pp. 192-200 ◽  
Author(s):  
Armando Di Donato ◽  
Gian Marco Ghiggeri ◽  
Marco Di Duca ◽  
Elena Jivotenko ◽  
Roberto Acinni ◽  
...  
Keyword(s):  
Lysyl Oxidase ◽  
Cross Linking ◽  
Adriamycin Nephropathy ◽  
Collagen Cross Linking

Loss of fibulin-4 results in abnormal collagen fibril assembly in bone, caused by impaired lysyl oxidase processing and collagen cross-linking

2016 ◽  
Vol 50 ◽  
pp. 53-66 ◽  
Author(s):  
Takako Sasaki ◽  
Reinout Stoop ◽  
Takao Sakai ◽  
Andreas Hess ◽  
Rainer Deutzmann ◽  
...  
Keyword(s):  
Collagen Fibril ◽  
Lysyl Oxidase ◽  
Cross Linking ◽  
Collagen Cross Linking

scholarly journals N-acetyl-seryl-aspartyl-lysyl-proline reduces cardiac collagen cross-linking and inflammation in angiotensin II-induced hypertensive rats

2013 ◽  
Vol 126 (1) ◽  
pp. 85-94 ◽  
Author(s):  
Germán E. González ◽  
Nour-Eddine Rhaleb ◽  
Pablo Nakagawa ◽  
Tang-Dong Liao ◽  
Yunhe Liu ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Transforming Growth Factor ◽  
Nuclear Translocation ◽  
Lysyl Oxidase ◽  
Left Ventricular ◽  
Cross Linking ◽  
Lymphocyte Infiltration ◽  
Total Collagen ◽  
Induced Hypertension ◽  
Collagen Cross Linking

We have reported previously that Ac-SDKP (N-acetyl-seryl-aspartyl-lysyl-proline) reduces fibrosis and inflammation (in macrophages and mast cells). However, it is not known whether Ac-SDKP decreases collagen cross-linking and lymphocyte infiltration; lymphocytes modulate both collagen cross-linking and ECM (extracellular matrix) formation in hypertension. Thus we hypothesized that (i) in AngII (angiotensin II)-induced hypertension, Ac-SDKP prevents increases in cross-linked and total collagen by down-regulating LOX (lysyl oxidase), the enzyme responsible for cross-linking, and (ii) these effects are associated with decreased pro-fibrotic cytokine TGFβ (transforming growth factor β) and the pro-inflammatory transcription factor NF-κB (nuclear factor κB) and CD4+/CD8+ lymphocyte infiltration. We induced hypertension in rats by infusing AngII either alone or combined with Ac-SDKP for 3 weeks. Whereas Ac-SDKP failed to lower BP (blood pressure) or LV (left ventricular) hypertrophy, it did prevent AngII-induced increases in (i) cross-linked and total collagen, (ii) LOX mRNA expression and LOXL1 (LOX-like 1) protein, (iii) TGFβ expression, (iv) nuclear translocation of NF-κB, (v) CD4+/CD8+ lymphocyte infiltration, and (vi) CD68+ macrophages infiltration. In addition, we found a positive correlation between CD4+ infiltration and LOXL1 expression. In conclusion, the effect of Ac-SDKP on collagen cross-linking and total collagen may be due to reduced TGFβ1, LOXL1, and lymphocyte and macrophage infiltration, and its effect on inflammation could be due to lower NF-κB.

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