Three-dimensional Supramolecular Organization of the Extracellular Matrix in Human and Rabbit Corneal Stroma, as Revealed by Ultrarapid-freezing and Deep-etching Methods

Hirsch, M.; Prenant, G.; Renard, G

doi:10.1006/exer.2000.0935

Cited by 39 publications

(22 citation statements)

References 48 publications

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“…Type XII and XIV are two structurally similar collagens of this family that occur in the cornea [56]. They have a collagenous fibril-associated filament attached to non-collagenous, finger-like projections that, by protruding from the surface of corneal collagen fibrils, could interact with proteins [57]. They were found to not be uniformly present in the stroma, but are more concentrated near cells, in the interfacial regions and between lamellae [58,59].…”

Section: Discussionmentioning

confidence: 99%

Microscopic characterization of collagen modifications induced by low‐temperature diode‐laser welding of corneal tissue

Matteini

Rossi

Menabuoni³

et al. 2007

Lasers Surg Med

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The preservation of substantially intact, undenatured collagen fibrils in laser-welded corneal wounds supported the thermodynamic studies that we carried out recently, which indicated temperatures below 66 degrees C at the weld site under laser irradiation. This observation enabled us to hypothesize that the mechanism, proposed in the literature, of unwinding of collagen triple helixes followed by fibrils "interdigitation" is not likely to occur in the welding process that we set up for the corneal suturing.

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Section: Discussionmentioning

confidence: 99%

Microscopic characterization of collagen modifications induced by low‐temperature diode‐laser welding of corneal tissue

Matteini

Rossi

Menabuoni³

et al. 2007

Lasers Surg Med

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“…Neovessels appearing in the knockout animals were shorter, sparser, and minimally arborized compared with those seen in wild-type controls, and histological studies showed that endothelial cells in the annexin II-deficient corneas were frequently isolated or formed lumenless, cordlike structures. Because the injured corneal stroma is rich in both fibrin (46,47) and multiple isoforms of collagen (types I, VI, and XII) (48,49), impaired breakdown of one or more of these proteins would likely hinder endothelial cell migration and retard the neovascular response.…”

Section: Discussionmentioning

confidence: 99%

Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo

Qi¹,

Jacovina²,

Deora³

et al. 2004

J. Clin. Invest.

120

145

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A central tenet of fibrinolysis is that tissue plasminogen activator–dependent (t-PA– dependent) conversion of plasminogen to active plasmin requires the presence of the cofactor/substrate fibrin. However, previous in vitro studies have suggested that the endothelial cell surface protein annexin II can stimulate t-PA–mediated plasminogen activation in the complete absence of fibrin. Here, homozygous annexin II–null mice displayed deposition of fibrin in the microvasculature and incomplete clearance of injury-induced arterial thrombi. While these animals demonstrated normal lysis of a fibrin-containing plasma clot, t-PA–dependent plasmin generation at the endothelial cell surface was markedly deficient. Directed migration of annexin II–null endothelial cells through fibrin and collagen lattices in vitro was also reduced, and an annexin II peptide mimicking sequences necessary for t-PA binding blocked endothelial cell invasion of Matrigel implants in wild-type mice. In addition, annexin II–deficient mice displayed markedly diminished neovascularization of fibroblast growth factor–stimulated cornea and of oxygen-primed neonatal retina. Capillary sprouting from annexin II–deficient aortic ring explants was markedly reduced in association with severe impairment of activation of metalloproteinase-9 and -13. These data establish annexin II as a regulator of cell surface plasmin generation and reveal that impaired endothelial cell fibrinolytic activity constitutes a barrier to effective neoangiogenesis

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“…There may be other intermediate levels of organisation between molecule and fibril in the cornea (Ottani et al 2002). Freeze-fracture and -etching (Marchini et al 1986;Hirsch et al 2001) has revealed fibril sub-structures greater than 4 nm wide, tilted with respect to the fibril axis by 16-17° (Fig. 2).…”

Section: Collagen Fibrilsmentioning

confidence: 99%

Corneal collagen—its role in maintaining corneal shape and transparency

2009

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Corneal collagen has a number of properties that allow it to fulfil its role as the main structural component within the tissue. Fibrils are narrow, uniform in diameter and precisely organised. These properties are vital to maintain transparency and to provide the biomechanical prerequisites necessary to sustain shape and provide strength. This review describes the structure and arrangement of corneal collagen from the nanoscopic to the macroscopic level, and how this relates to the maintenance of the form and transparency of the cornea.

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Three-dimensional Supramolecular Organization of the Extracellular Matrix in Human and Rabbit Corneal Stroma, as Revealed by Ultrarapid-freezing and Deep-etching Methods

Cited by 39 publications

References 48 publications

Microscopic characterization of collagen modifications induced by low‐temperature diode‐laser welding of corneal tissue

Microscopic characterization of collagen modifications induced by low‐temperature diode‐laser welding of corneal tissue

Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo

Corneal collagen—its role in maintaining corneal shape and transparency

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