Lysyl Oxidase Activity in the Ocular Tissues and the Role of LOX in Proliferative Diabetic Retinopathy and Rhegmatogenous Retinal Detachment

Coral, Karunakaran; Angayarkanni, Narayanasamy; Madhavan, Jagadeesan; Bharathselvi, Muthuvel; Ramakrishnan, Sivaramakrishnan; Nandi, Krishnendu; Rishi, Pukhraj; Kasinathan, Nachiappan; Krishnakumar, Subramanian

doi:10.1167/iovs.07-1550

Cited by 44 publications

(29 citation statements)

References 36 publications

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“…35 An extensive study of LOX enzyme's expression and activity in ocular tissues was recently undertaken and revealed interesting insights into the pathogenesis of some retinal abnormalities. 36 Extensive examination of human expressed sequences located in the NCBI Unigene database (http://www.ncbi.nlm. nih.gov/unigene/) identified multiple expressed sequence tags (ESTs) matching to the LOX gene sequence in a variety of tissues including connective tissue and various parts of the eye including retinal pigment epithelium and fetal eye.…”

Section: Discussionmentioning

confidence: 99%

Variation in the Lysyl Oxidase (LOX) Gene Is Associated with Keratoconus in Family-Based and Case-Control Studies

Bykhovskaya

Epifantseva

et al. 2012

Invest. Ophthalmol. Vis. Sci.

112

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Section: Discussionmentioning

confidence: 99%

Variation in the Lysyl Oxidase (LOX) Gene Is Associated with Keratoconus in Family-Based and Case-Control Studies

Bykhovskaya

Epifantseva

et al. 2012

Invest. Ophthalmol. Vis. Sci.

112

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“…Aliquots of 10 µg protein extract were analyzed immediately for the assay with or without LOX-specific inhibitor β-propionitrile (BAPN; Sigma-Aldrich). The sample solution was added to the final reaction mixture (50 mM sodium borate [pH 8.2], 1.2 M urea, 50 µM N-acetyl -3,7-dihydroxyphenoxazine (Amplex Red; Molecular Probes-Invitrogen), 0.1 U/ml horseradish peroxidase (HRP; Sigma-Aldrich), and 10 mM 1,5-diaminopentane substrate (Cadaverine dihydrochloride; Sigma-Aldrich) in the presence or absence of 500 µM BAPN (Alfa-Aesar, Ward hill, MA), as previously described (32,33). LOX acts on Cadaverine (pseudosubstrate) and produces H 2 O 2 , and the HRP-catalyzed oxidation of N -acetyl-3,7-dihydroxyphenoxazine by H 2 O 2 produces fluorescent resorufin.…”

Section: Methodsmentioning

confidence: 99%

Disparate response of articular- and auricular-derived chondrocytes to oxygen tension

Kean

Mera

Whitney

et al. 2016

Connective Tissue Research

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Purpose/Aim To determine the effect of reduced (5%) oxygen tension on chondrogenesis of auricular-derived chondrocytes. Currently, many cell and tissue culture experiments are performed at 20% oxygen with 5% carbon dioxide. Few cells in the body are subjected to this supra-physiological oxygen tension. Chondrocytes and their mesenchymal progenitors are widely reported to have greater chondrogenic expression when cultured at low, more physiological, oxygen tension (1–7%). Although generally accepted, there is still some controversy, and different culture methods, species, and outcome metrics cloud the field. These results are, however, articular chondrocyte biased and have not been reported for auricular-derived chondrocytes. Materials and Methods Auricular and articular chondrocytes were isolated from skeletally mature New Zealand White rabbits, expanded in culture and differentiated in high density cultures with serum free chondrogenic media. Cartilage tissue derived from aggregate cultures or from the tissue engineered sheets were assessed for biomechanical, glycosaminoglycan, collagen, collagen cross-links, and lysyl oxidase activity and expression. Results Our studies show increased proliferation rates for both auricular and articular chondrocytes at low (5%) O2 versus standard (20%) O2. In our scaffold free chondrogenic cultures, low O2 was found to increase articular chondrocyte accumulation of glycosaminoglycan, but not cross-linked type II collagen, or total collagen. Conversely, auricular chondrocytes accumulated less glycosaminoglycan, cross-linked type II collagen and total collagen under low oxygen tension. Conclusions This study highlights the dramatic difference in response to low O2 of chondrocytes isolated from different anatomical sites. Low O2 is beneficial for articular-derived chondrogenesis but detrimental for auricular-derived chondrogenesis.

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“…Aorta tissue was isolated immediately and homogenized in 4 M urea in 0.02 M borate buffer (pH 8.0) at 4°C and centrifuged at 15,000 g for 30 min at 4°C, as previously reported (2). The supernatants were analyzed immediately for LOX assay with and without ␤-APN (13).…”

Section: Methodsmentioning

confidence: 99%

The role of lysyl oxidase family members in the stabilization of abdominal aortic aneurysms

Remus

O’Donnell

Rafferty

et al. 2012

American Journal of Physiology-Heart and Circulatory Physiology

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Abdominal aortic aneurysms (AAAs) are a major cause of morbidity and mortality in the United States today. We employed a model for AAA development using apolipoprotein E knock out mice fed a high-fat diet and treated with ANG II and β-aminopropionitrile (β-APN) for 4 wk. ANG II induces hypertension and atherosclerotic disease, whereas β-APN inhibits the activity of the lysyl oxidase/ lysyl oxidase-like protein (LOX/LOXL) family members. LOX/LOXL family members crosslink collagen and elastin in the extracellular matrix and therefore contribute to the integrity and stabilization of a healthy vessel wall. In this model, cotreatment with ANG II and β-APN caused a 90% AAA incidence and increased atherosclerotic lesion formation from less than 5% to greater than 25% after 4 wk. In more atheroprotected mouse strains (C57BL/6 and BalbC), cotreatment with ANG II and β-APN caused 50% and 40% AAA incidence, respectively. These data demonstrate the importance of LOX/LOXL to the stability of the vessel wall. Therapeutic strategies to overexpress LOX/LOXL enzymes or to support the crosslinking of soluble matrix proteins in a polymeric scaffold are a promising opportunity to achieve stabilization of AAAs.

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Lysyl Oxidase Activity in the Ocular Tissues and the Role of LOX in Proliferative Diabetic Retinopathy and Rhegmatogenous Retinal Detachment

Abstract: LOX activity showed a statistically significant decrease in the vitreous of PDR and RRD relative to control specimens. This effect can contribute to the inadequate collagen cross-linking that causes the ECM changes that occur in these diseases.

Cited by 44 publications

References 36 publications

Variation in the Lysyl Oxidase (LOX) Gene Is Associated with Keratoconus in Family-Based and Case-Control Studies

Variation in the Lysyl Oxidase (LOX) Gene Is Associated with Keratoconus in Family-Based and Case-Control Studies

Disparate response of articular- and auricular-derived chondrocytes to oxygen tension

The role of lysyl oxidase family members in the stabilization of abdominal aortic aneurysms

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