Supramolecular assembly of basement membranes

Timpl, Rupert; Brown, Judith C.

doi:10.1002/bies.950180208

Cited by 627 publications

(492 citation statements)

References 76 publications

(29 reference statements)

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“…14,15 In addition, collagen type IV has been shown to be present in the intima of fatty streaks and in advanced lesions. 16 Collagen type IV interaction to endothelial cells is important for maintaining endothelial cell function.…”

Section: Discussionmentioning

confidence: 99%

Increased aldehyde-modification of collagen type IV in symptomatic plaques – A possible cause of endothelial dysfunction

et al. 2015

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Increased aldehyde-modification of collagen type IV in symptomatic plaques -A possible cause of endothelial dysfunction.Dunér, Pontus; Goncalves, Isabel; Grufman, Helena; Edsfeldt, Andreas; To, Fong; Nitulescu, Mihaela; Nilsson, Jan; Bengtsson, Eva Link to publication Citation for published version (APA): Dunér, P., Goncalves, I., Grufman, H., Edsfeldt, A., To, F., Nitulescu, M., ... Bengtsson, E. (2015). Increased aldehyde-modification of collagen type IV in symptomatic plaques -A possible cause of endothelial dysfunction. Atherosclerosis, 240(1), 26-32. DOI: 10.101626-32. DOI: 10. /j.atherosclerosis.2015 General rights Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights.• Users may download and print one copy of any publication from the public portal for the purpose of private study or research.• You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal Abstract ObjectiveSubendothelial LDL-adhesion and its subsequent oxidation are considered as key events in the development of atherosclerotic lesions. During oxidation of LDL, reactive aldehydes such as malondialdehyde (MDA) are formed, which modify apolipoproteinB100. However, the possibility that these reactive aldehydes could leak out of the LDL-particle and modify surrounding extracellular matrix proteins has been largely unexplored. We have investigated if aldehyde-modification of collagen type IV, one of the major basement membrane components, in plaques is associated with cardiovascular events. MethodsThe amount of MDA-modified collagen type IV and native collagen type IV were determined in homogenates from 155 carotid artery lesions, removed by endarterectomy from patients with or without previous cerebrovascular events. ResultsPlaque MDA-collagen type IV, but not native collagen type IV, correlated with oxidized LDL (r=0.31, P<0.001) and lipoprotein-associated phospholipase A2 (r=0.44, P<0.001).MDA-collagen type IV was increased in lesions from symptomatic patients compared to lesions from asymptomatic patients. Autoantibodies against MDA-collagen type IV in plasma correlated with the amount of MDA-collagen type IV in lesions. MDA-modification of collagen type IV decreased endothelial cell attachment. In addition, culture of endothelial cells with MDA-modified collagen type IV increased vascular cell adhesion molecule expression and reduced the anti-coagulant proteins thrombomodulin and endothelial protein C receptor. In the lesions native collagen type IV, but not MDA-collagen type IV, was positively associated with thrombomodulin. Conclusion 3The present observations imply that aldehyde-modification of collagen type IV, associated with LDL oxidation, in atherosclerotic plaques may cause endothelial d...

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Section: Discussionmentioning

confidence: 99%

Increased aldehyde-modification of collagen type IV in symptomatic plaques – A possible cause of endothelial dysfunction

et al. 2015

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“…Functionally, the ILM is more appropriately considered as an adhesive sheet that facilitates the connection of the vitreous body (VB) with the retina. Identical to other BMs, [1][2][3] the ILM consists of about ten high-molecular weight extracellular matrix (ECM) proteins that include members of the laminin family, nidogen1 and 2, collagen IV and three heparan sulphate proteoglycans, agrin, perlecan and collagen XVIII. 4,5 The ILM is invisible by conventional light microscopy but can be readily visualized by immunocytochemistry using antibodies to any of the BM components ( Figure 1a).…”

Section: Ilmmentioning

confidence: 99%

Origin and turnover of ECM proteins from the inner limiting membrane and vitreous body

Halfter

Dong

et al. 2008

Eye

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The inner limiting membrane (ILM) and the vitreous body (VB) are two major extracellular matrix (ECM) structures that are essential for early eye development. The ILM is considered to be the basement membrane of the retinal neuroepithelium, yet in situ hybridization and chick/quail transplant experiments in organcultured eyes showed that all components critical for ILM assembly, such as laminin or collagen IV, are not synthesized by the retina. Rather, ILM proteins, with the exception of agrin, originate from the lens or (and) ciliary body and are shed into the vitreous. The VB serves as a reservoir providing high concentrations of ILM proteins for the instant assembly of new ILM during rapid embryonic eye growth. The function of the retina in ILM assembly is to provide the cellular receptor proteins for the binding of the ILM proteins from the vitreous. The VB is a gelatinous ECM structure that fills the vitreous cavity of the eye. Its major structural proteins, collagen II and fibrillin, originate primarily from the ciliary body. Reverse transcription-PCR and western blotting show that the rate of synthesis of structural, monomeric ILM and VB proteins, such as laminin, collagen IV and II is very high during embryogenesis and very low in the adult. The downregulation of ILM and VB protein synthesis occurs during early postnatal life, and both ILM and VB are from then on maintained throughout life with minimum turnover. Our data explain why ILM and VB do not regenerate after vitrectomy and ILM peeling.

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“…For example, endostatin, 7 a 20-kDa C-terminal fragment of type XVIII collagen that is a component of vascular and epithelial BMs, inhibits endothelial cell migration 8 and angiogenesis. Type IV collagen is also known as an important structural component of the BM 9 and comprises six genetically distinct products of the COL4A1-COL4A6 genes-α1-α6 chains of type IV collagen, or α1(IV) to α6(IV) chains. 10 In type IV collagen, arresten 11 and canstatin, 12 which are parts of the C-terminal globular noncollagenous (NC1) domains of α1(IV) and α2(IV) chains, respectively, inhibit endothelial cell migration.…”

mentioning

confidence: 99%

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

Urushiyama

Terasaki

Nagasaka

et al. 2015

Laboratory Investigation

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Early fibrotic lesions are thought to be the initial findings of fibrogenesis in idiopathic interstitial pneumonias, but little is known about their properties. Type IV collagen comprises six gene products, α1-α6, and although it is known as a major basement membrane component, its abnormal deposition is seen in fibrotic lesions of certain organs. We studied the expression of type I and III collagen and all α chains of type IV collagen in lung specimens from patients with usual interstitial pneumonia (UIP) or organizing pneumonia (OP) via immunohistochemistry. With cultured lung fibroblasts, we analyzed the expression and function of all α chains of type IV collagen via immunohistochemistry, western blotting, realtime quantitative PCR, and a Boyden chamber migration assay after the knockdown of α1 and α2 chains. Although we observed type I and III collagens in early fibrotic lesions of both UIP and OP, we found type IV collagen, especially α1 and α2 chains, in early fibrotic lesions of UIP but not OP. Fibroblasts enhanced the expression of α1 and α2 chains of type IV collagen after transforming growth factor-β1 stimulation. Small interfering RNA against α1 and α2 chains increased fibroblast migration, with upregulated phosphorylation of focal adhesion kinase (FAK), and adding medium containing fibroblast-produced α1 and α2 chains reduced the increased levels of fibroblast migration and phosphorylation of FAK. Fibroblasts in OP were positive for phosphorylated FAK but fibroblasts in UIP were not. These results suggest that fibroblasts in UIP with type IV collagen deposition, especially α1 and α2 chains, have less ability to migrate from early fibrotic lesions than fibroblasts in OP without type IV collagen deposition. Thus, type IV collagen deposition in early fibrotic lesions of UIP may be implicated in refractory pathophysiology including migration of lesion fibroblasts via a FAK pathway.

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Supramolecular assembly of basement membranes

Cited by 627 publications

References 76 publications

Increased aldehyde-modification of collagen type IV in symptomatic plaques – A possible cause of endothelial dysfunction

Increased aldehyde-modification of collagen type IV in symptomatic plaques – A possible cause of endothelial dysfunction

Origin and turnover of ECM proteins from the inner limiting membrane and vitreous body

Role of α1 and α2 chains of type IV collagen in early fibrotic lesions of idiopathic interstitial pneumonias and migration of lung fibroblasts

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