A new role for Nogo as a regulator of vascular remodeling

Acevedo, Lisette M.; Yu, Jun; Erdjument‐Bromage, Hediye; Miao, Robert Q.; Kim, Ji Eun; Fulton, David; Tempst, Paul; Strittmatter, Stephen M.; Sessa, William C.

doi:10.1038/nm1020

Cited by 223 publications

(305 citation statements)

References 22 publications

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“…In addition, using mice deficient in Nogo-A or NgR, some reports have shown axonal regeneration and marked behavioral improvement following SCI Kim et al, 2003Kim et al, , 2004, whereas other studies did not detect any differences when compared to their wild-type littermates (Zheng et al, 2003(Zheng et al, , 2005. Other recent reports have suggested a more complex role for Nogo other than associated with inhibition of axonal outgrowth (Jokic et al, 2005;He et al, 2004;Karnezis et al, 2004;Acevado et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Selective temporal and regional alterations of Nogo-A and small proline-rich repeat protein 1A (SPRR1A) but not Nogo-66 receptor (NgR) occur following traumatic brain injury in the rat

Marklund

Fulp

Shimizu

et al. 2006

Experimental Neurology

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Axons show a poor regenerative capacity following traumatic central nervous system (CNS) injury, partly due to the expression of inhibitors of axonal outgrowth, of which Nogo-A is considered the most important. We evaluated the acute expression of Nogo-A, the Nogo-66 receptor (NgR) and the novel small proline-rich repeat protein 1A (SPRR1A, previously undetected in brain), following experimental lateral fluid percussion (FP) brain injury in rats. Immunofluorescence with antibodies against Nogo-A, NgR and SPRR1A was combined with antibodies against the neuronal markers NeuN and microtubule-associated protein (MAP)-2 and the oligodendrocyte marker RIP, while Western blot analysis was performed for Nogo-A and NgR. Brain injury produced a significant increase in Nogo-A expression in injured cortex, ipsilateral external capsule and reticular thalamus from days 1-7 post-injury (P < 0.05) compared to controls. Increased expression of Nogo-A was observed in both RIP-and NeuN positive (+) cells in the ipsilateral cortex, in NeuN (+) cells in the CA3 region of the hippocampus and reticular thalamus and in RIP (+) cells in white matter tracts. Alterations in NgR expression were not observed following traumatic brain injury (TBI). Brain injury increased the extent of SPRR1A expression in the ipsilateral cortex and the CA3 at all post-injury time-points in NeuN (+) cells. The marked increases in Nogo-A and SPRR1A in several important brain regions suggest that although inhibitors of axonal growth may be upregulated, the injured brain is also capable of expressing proteins promoting axonal outgrowth following TBI. KeywordsNogo-A; Nogo-66 receptor; Small proline-rich repeat protein 1A (SPRR1A); Traumatic brain injury; Oligodendrocytes

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Section: Introductionmentioning

confidence: 99%

Selective temporal and regional alterations of Nogo-A and small proline-rich repeat protein 1A (SPRR1A) but not Nogo-66 receptor (NgR) occur following traumatic brain injury in the rat

Marklund

Fulp

Shimizu

et al. 2006

Experimental Neurology

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“…These aspects have been discussed previously 85 and reviewed recently in the context of graft pathophysiology 86 and here we bring the literature up to date with recent original papers in this area. It has recently been demonstrated that NogoB is a novel regulator of the vascular system 87 and that NogoB overexpression using the Ad5 approach significantly reduced neointima formation in pig venous grafts. 88 An interesting recently published study 89 focused on the concept that overexpression of cyclooxygenase-1 might attenuate vein graft disease.…”

Section: Studies Using Gene Therapy For Vein Graftsmentioning

confidence: 99%

Vein graft failure: current clinical practice and potential for gene therapeutics

et al. 2012

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Autologous saphenous vein is commonly used as a conduit to bypass atherosclerotic lesions in coronary and femoral arteries. Despite the wide use of arterial conduits, which are less susceptible to complications and failure, as alternative conduits, the saphenous vein will continue to be used in coronary artery bypass grafting until acceptable alternative approaches are evaluated. Hence, preservation of vein graft patency is essential for the long-term success. Gene therapy is attractive in this setting as an ex-vivo technology to genetically manipulate the conduit before grafting. The use of safe and efficient vectors for delivery is a necessity as well as a strategy to improve patency in the long term. Here, we review the current clinical practice, the pathogenesis of bypass graft failure and adenovirus-mediated gene therapy strategies designed to improve late vein graft failure by modulation of smooth muscle cells in the vein wall.

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“…The N terminus of Nogo has been recognized recently to have another NgR-independent action via an extreme N-terminal domain present in Nogo-B. This domain has a selective role in remodeling the vasculature after injury (Acevedo et al, 2004). Thus, Nogo appears to have multiple functional domains and receptors (supplemental Fig.…”

Section: Ngr-independent Action Of Amino-nogomentioning

confidence: 99%

Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist

Liu²,

Budel³

et al. 2005

J. Neurosci.

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Nogo is a myelin-derived protein that limits axonal regeneration after CNS injury. A short hydrophilic Nogo-66 loop between two hydrophobic domains of Nogo binds to a Nogo-66 receptor (NgR) to inhibit axonal outgrowth. Inhibition of axon outgrowth and cell spreading by a second Nogo domain, termed Amino-Nogo-A, is thought to be mediated by a distinct receptor complex. Here, we define a novel Nogo-A-specific domain in Amino-Nogo that binds to NgR with nanomolar affinity. This second domain of 24 amino acids does not alter cell spreading or axonal outgrowth. Fusion of the two NgR-binding Nogo-A domains creates a ligand with substantially enhanced affinity for NgR and converts a NgR antagonist peptide to an agonist. Thus, NgR activation by Nogo-A involves multiple sites of interaction between Nogo-A and NgR.

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A new role for Nogo as a regulator of vascular remodeling

Cited by 223 publications

References 22 publications

Selective temporal and regional alterations of Nogo-A and small proline-rich repeat protein 1A (SPRR1A) but not Nogo-66 receptor (NgR) occur following traumatic brain injury in the rat

Selective temporal and regional alterations of Nogo-A and small proline-rich repeat protein 1A (SPRR1A) but not Nogo-66 receptor (NgR) occur following traumatic brain injury in the rat

Vein graft failure: current clinical practice and potential for gene therapeutics

Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist

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