scholarly journals The Role of Nonenzymatic Glycation and Carbonyls in Collagen Cross-Linking for the Treatment of Keratoconus

2011 ◽  
Vol 52 (9) ◽  
pp. 6363 ◽  
Author(s):  
Gage Brummer ◽  
Stacy Littlechild ◽  
Scott McCall ◽  
Yuntao Zhang ◽  
Gary W. Conrad
2017 ◽  
Vol 2017 ◽  
pp. 1-13 ◽  
Author(s):  
Marwa Kamel ◽  
Mohamed Wagih ◽  
Gokhan S. Kilic ◽  
Concepcion R. Diaz-Arrastia ◽  
Mohamed A. Baraka ◽  
...  

The role of the extracellular matrix (ECM) in uterine fibroids (UF) has recently been appreciated. Overhydroxylation of lysine residues and the subsequent formation of hydroxylysylpyridinoline (HP) and lysylpyridinoline (LP) cross-links underlie the ECM stiffness and profoundly affect tumor progression. The aim of the current study was to investigate the relationship between ECM of UF, collagen and collagen cross-linking enzymes [lysyl hydroxylases (LH) and lysyl oxidases (LOX)], and the development and progression of UF. Our results indicated that hydroxyl lysine (Hyl) and HP cross-links are significantly higher in UF compared to the normal myometrial tissues accompanied by increased expression of LH (LH2b) and LOX. Also, increased resistance to matrix metalloproteinases (MMP) proteolytic degradation activity was observed. Furthermore, the extent of collagen cross-links was positively correlated with the expression of myofibroblast marker (α-SMA), growth-promoting markers (PCNA; pERK1/2;FAKpY397; Ki-67; and Cyclin D1), and the size of UF. In conclusion, our study defines the role of overhydroxylation of collagen and collagen cross-linking enzymes in modulating UF cell proliferation, differentiation, and resistance to MMP. These effects can establish microenvironment conducive for UF progression and thus represent potential target treatment options of UF.


2008 ◽  
Vol 41 (7) ◽  
pp. 1427-1435 ◽  
Author(s):  
Thomas Siegmund ◽  
Matthew R. Allen ◽  
David B. Burr

2007 ◽  
Vol 7 (5) ◽  
pp. 99S-100S
Author(s):  
Alok Sharan ◽  
Simon Tang ◽  
Martin Quirno ◽  
Deepak Vashishth ◽  
Tom Errico

2015 ◽  
Vol 4 (73) ◽  
pp. 12760-12774
Author(s):  
Atul Gupta ◽  
Superna M ◽  
Bhimasankar D ◽  
Vijayleela M

2004 ◽  
Vol 5 (2) ◽  
pp. 143-153 ◽  
Author(s):  
G. Kesava Reddy

Nonenzymatic glycation of connective tissue matrix proteins is a major contributor to the pathology of diabetes and aging. Previously the author and colleagues have shown that nonenzymatic glycation significantly enhances the matrix stability in the Achilles tendon (Reddy et al., 2002,Arch. Biochem. Biophys., 399, 174–180). The present study was designed to gain further insight into glycation-induced collagen cross-linking and its relationship to matrix stiffness in the rabbit Achilles tendon. The glycation process was initiated by incubating the Achilles tendons (n = 6) in phosphate-buffered saline containing ribose, whereas control tendons (n = 6) were incubated in phosphate-buffered saline without ribose. Eight weeks following glycation, the biomechanical attributes as well as the degree of collagen cross-linking were determined to examine the potential associations between matrix stiffness and molecular properties of collagen. Compared to nonglycated tendons, the glycated tendons showed increased maximum load, stress, strain, Young's modulus of elasticity, and toughness indicating that glycation increases the matrix stiffness in the tendons. Glycation of tendons resulted in a considerable decrease in soluble collagen content and a significant increase in insoluble collagen and pentosidine. Analysis of potential associations between the matrix stiffness and degree of collagen cross-linking showed that both insoluble collagen and pentosidine exhibited a significant positive correlation with the maximum load, stress, and strain, Young's modulus of elasticity, and toughness (rvalues ranging from .61 to .94) in the Achilles tendons. However, the soluble collagen content present in neutral salt buffer, acetate buffer, and acetate buffer containing pepsin showed an inverse relation with the various biomechanical attributes tested (rvalues ranging from .22 to .84) in the Achilles tendons. The results of the study demonstrate that glycation-induced collagen cross-linking is directly associated with the increased matrix stiffness and other mechanical attributes of the tendon.


2008 ◽  
Vol 18 (3) ◽  
pp. 239-247 ◽  
Author(s):  
Kamran Sardari ◽  
Hossein Kazemi ◽  
Mohamad Reza Emami ◽  
Ahmad Reza Movasaghi ◽  
Amir Afkhami Goli

2011 ◽  
Vol 112 (16) ◽  
pp. 2832-2839 ◽  
Author(s):  
Shang-Zhi Pu ◽  
Ya-Nan Wang ◽  
Qiang He ◽  
Xue-Pin Liao ◽  
Wen-Hua Zhang ◽  
...  

2017 ◽  
Vol 5 (1) ◽  
pp. 6
Author(s):  
PV Nanda Kumar Reddy ◽  
BV Kranthi

1982 ◽  
Vol 112 (4) ◽  
pp. 708-716 ◽  
Author(s):  
William Opsahl ◽  
Haig Zeronian ◽  
Mike Ellison ◽  
Davis Lewis ◽  
Robert B. Rucker ◽  
...  

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