Anti–γ-Enolase Autoimmune Retinopathy Manifesting in Early Childhood

Ko, Audrey C.; Hernández, Javier; Brinton, Jason Philip; Faidley, Elizabeth A.; Mugge, S. A.; Mets, Marilyn B.; Kardon, Randy H.; Folk, James C.; Mullins, Robert F.; Stone, Edwin M.

doi:10.1001/archophthalmol.2010.295

Cited by 9 publications

(6 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Membrane strips that were only probed with secondary antibody served as negative controls; membrane strips that were probed with a serum sample that had previously demonstrated antienolase antibody activity served as a positive control. 13 The number of bands on Western blot was counted in a masked fashion for each patient sample. Bands corresponding to the reduced IgG heavy-chain band were not included in analysis; visualized bands were omitted if the band signal intensity was less than 1.5 times that of the background for that sample as quantified using Adobe Photoshop (version 10.0; Adobe Systems Inc, San Jose, California).…”

Section: Serum Collection and Screeningmentioning

confidence: 99%

“…In addition, autoimmune retinopathy may mimic inherited retinal disease in some cases, as we noted recently in a patient with anti-␥-enolase activity. 13 The role of circulating antibodies reactive to retinal proteins in the pathogenesis of other retinal diseases is still unclear and was discussed in a recent letter and a response to that letter in this journal. [17][18][19] Previous studies looking at healthy populations have reported varying levels of antiretinal antibody activity.…”

Section: Commentmentioning

confidence: 99%

“…Serum samples of patients with retinal degenerations without molecular confirmation were not in- cluded in this study in order to exclude possible phenocopies of inherited eye disease. 13 Second, despite thorough ophthalmologic examination and review of medical charts, individuals within the control group may still have inflammatory disease that is not yet clinically evident. Third, it is possible that some of the bands on this or any similar Western blot are representative of autoantibodies crossreacting with retinal protein epitopes rather than autoantibodies specifically raised against retinal proteins.…”

Section: Commentmentioning

confidence: 99%

“…However there is good evidence that antibodies to enolase and especially to recoverin cause retinal degeneration. 7,11,13,20 Further studies are needed to determine the identity of pathogenic autoantibodies as well as the significance of reactivity against aqueous-and detergent-soluble retinal proteins. Patients with additional typesofposterioruveitisshouldbetested,andserumsamples should also be assessed during different stages of disease to correlate autoantibody activity with appearance of retinal inflammation.…”

Section: Commentmentioning

confidence: 99%

See 3 more Smart Citations

Seroreactivity Against Aqueous-Soluble and Detergent-Soluble Retinal Proteins in Posterior Uveitis

Brinton²,

Mahajan³

et al. 2011

Arch Ophthalmol

Self Cite

View full text Add to dashboard Cite

To characterize the seroreactivity against retinal proteins in patients with posterior uveitis, retinal disease of noninflammatory origin, and healthy controls. Methods: Patients with posterior uveitis (n =47), molecularly confirmed photoreceptor degenerations (n=11), and healthy controls (n=33) received dilated fundus examinations at the University of Iowa. Aqueous-soluble and detergent-soluble fractions of human retina were separated by gel electrophoresis and transferred to polyvinylidene fluoride membranes. Membranes were probed with patient serum samples to detect IgG, IgA, and IgM human antibodies that react with retinal antigens. The number of bands detected by Western blot was counted, and their molecular weights were determined. Results: Antibodies recognizing retinal proteins were found in healthy controls, in patients with posterior uveitis, and in patients with molecularly confirmed heri

show abstract

Section: Serum Collection and Screeningmentioning

confidence: 99%

Section: Commentmentioning

confidence: 99%

Section: Commentmentioning

confidence: 99%

Section: Commentmentioning

confidence: 99%

See 2 more Smart Citations

Seroreactivity Against Aqueous-Soluble and Detergent-Soluble Retinal Proteins in Posterior Uveitis

Brinton²,

Mahajan³

et al. 2011

Arch Ophthalmol

Self Cite

View full text Add to dashboard Cite

show abstract

“…Further, increased oxidation of alpha-enolase also occurs in other models of AD [57, 67]. Several pathologies are linked to enolase-dependent pathways [68, 69]. …”

Section: Resultsmentioning

confidence: 99%

Proteomic identification of specifically carbonylated brain proteins in APPNLh/APPNLh×PS-1P264L/PS-1P264L human double mutant knock-in mice model of Alzheimer disease as a function of age

Sultana¹,

Robinson²,

Domenico³

et al. 2011

Journal of Proteomics

View full text Add to dashboard Cite

Alzheimer disease (AD) is the most common type of dementia and is characterized pathologically by the presence of neurofibrillary tangles (NFTs), senile plaques (SPs), and loss of synapses. The main component of SP is amyloid-beta peptide (Aβ), a 39 to 43 amino acid peptide, generated by the proteolytic cleavage of amyloid precursor protein (APP) by the action of beta- and gamma-secretases. The presenilins (PS) are components of the γ-secretase, which contains the protease active center. Mutations in PS enhance the production of the Aβ42 peptide. To date, more than 160 mutations in PS1 have been identified. Many PS mutations increase the production of the β-secretase-mediated C-terminal (CT) 99 amino acid-long fragment (CT99), which is subsequently cleaved by γ-secretase to yield Aβ peptides. Aβ has been proposed to induce oxidative stress and neurotoxicity. Previous studies from our laboratory and others showed an age-dependent increase in oxidative stress markers, loss of lipid asymmetry, and Aβ production and amyloid deposition in the brain of APP/PS1 mice. In the present study, we used APPNLh/APPNLh x PS-1P246L/PS-1P246L human double mutant knock-in APP/PS-1 mice to identify specific targets of brain protein carbonylation in an age-dependent manner. We found a number of proteins that are oxidatively modified in APP/PS1 mice compared to age-matched controls. The relevance of the identified proteins to the progression and pathogenesis of AD is discussed.

show abstract