Fibulin 2, a Tyrosine O-Sulfated Protein, Is Up-regulated Following Retinal Detachment

Kanan, Yogita; Brobst, Daniel; Han, Zongchao; Naash, Muna I.; Al‐Ubaidi, Muayyad R.

doi:10.1074/jbc.m114.562157

Cited by 9 publications

(4 citation statements)

References 76 publications

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“…Both FBLN-1 and VSC proteins were also increase in mice undergoing hypoglycemia. Whereas no specific role for Fbln1 has been described so far in the retina, Fibulin2 (Fbln2) has been implicated in retinal detachment observed in diabetic retinopathy, retinopathy of prematurity and other retinal complications [ 24 ]. Fibulin3 (Fbln3) has also been associated with both Malattia Leventinese and Doyne honeycomb retinal dystrophy [ 25 ].…”

Section: Discussionmentioning

confidence: 99%

Biological Characterization of Gene Response to Insulin-Induced Hypoglycemia in Mouse Retina

et al. 2016

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Glucose is the most important metabolic substrate of the retina and maintenance of normoglycemia is an essential challenge for diabetic patients. Chronic, exaggerated, glycemic excursions could lead to cardiovascular diseases, nephropathy, neuropathy and retinopathy. We recently showed that hypoglycemia induced retinal cell death in mouse via caspase 3 activation and glutathione (GSH) decrease. Ex vivo experiments in 661W photoreceptor cells confirmed the low-glucose induction of death via superoxide production and activation of caspase 3, which was concomitant with a decrease of GSH content. We evaluate herein retinal gene expression 4 h and 48 h after insulin-induced hypoglycemia. Microarray analysis demonstrated clusters of genes whose expression was modified by hypoglycemia and we discuss the potential implication of those genes in retinal cell death. In addition, we identify by gene set enrichment analysis, three important pathways, including lysosomal function, GSH metabolism and apoptotic pathways. Then we tested the effect of recurrent hypoglycemia (three successive 4h periods of hypoglycemia spaced by 48 h recovery) on retinal cell death. Interestingly, exposure to multiple hypoglycemic events prevented GSH decrease and retinal cell death, or adapted the retina to external stress by restoring GSH level comparable to control situation. We hypothesize that scavenger GSH is a key compound in this apoptotic process, and maintaining “normal” GSH level, as well as a strict glycemic control, represents a therapeutic challenge in order to avoid side effects of diabetes, especially diabetic retinopathy.

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Section: Discussionmentioning

confidence: 99%

Biological Characterization of Gene Response to Insulin-Induced Hypoglycemia in Mouse Retina

et al. 2016

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“…Before TLE analysis, the sample is spiked with nonradioactive tyrosine sulfate, which is subsequently visualized by ninhydrin. The radioactive tyrosine sulfated is visualized by autoradiographic analysis and its localization with tyrosine sulfate standard identifies the protein as a tyrosine sulfated protein (Hoffhines et al., ; Kanan et al., ,b).…”

Section: Commentarymentioning

confidence: 99%

“…The gold standard for identifying a protein as tyrosine sulfated is by using radioactive methods as developed by Huttner (Huttner, ). This method involves metabolically labeling a protein with radioactive S‐35 in vitro, followed by immunoprecipitation of the protein, barium hydroxide hydrolysis and TLE analysis (Hoffhines et al., ; Kanan et al., ,b).…”

Section: Commentarymentioning

confidence: 99%

“…Therefore, the antibody method may only be helpful in some cases and the inability of the antibody in recognizing a protein as tyrosine sulfated does not mean that the protein is not tyrosine sulfated. Forbes et al, 1994Liu and Lipmann, 1985a, 1985bAntonsson et al, 1991Önnerfjord et al, 2004Kanan et al, 2014aÖnnerfjord et al, 2004Popescu et al, 1999, Trask et al, 2001Paulsson et al, 1985Önnerfjord et al, 2004Jukkola et al, 1986Fessler et al, 1986Kanan et al, 2014bSurmann-Schmitt et al, 2008 Cell adhesion CD44/ CSPG8 Endoglycan/ PODLX2 Glycoprotein Ibα/ GP1B PSGL-1/ CD162 ND Binding L-selectin Binding vWF & Thrombin Binding P & L selectin Sleeman et al, 1998Fieger et al, 2003Dong et al, 1994Marchese et al, 1995Wilkins et al, 1994Sako et al, 1995Pouyani and Seed, 1995 Serine Vishnuvardhan et al, 2000Mutt and Jorpes, 1968Jensen et al, 1982Bundgaard et al, 1995Brand et al, 1984Jensen et al, 1982Torfs et al, 2002 Blood Coagulation Factor V Factor VIII Factor IX Factor X Fibrinogen γ subunit Fibrinogen β subunit Cleavage of thrombin Binding vWF ND ND ND ND Hortin, 1990Pittman et al, 1994Leyte et al, 1991Pittman et al, 1992Michnick et al, 1994Bond et al, 1988Morita and Jackson, 1986Farrell et al, 1991Hirose et al, 1988…”

Section: Commentary Background Informationmentioning

confidence: 99%

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Detection of Tyrosine Sulfation on Proteins

Kanan

Ubaidi

2015

CP Protein Science

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Tyrosine sulfation is a post-translational modification (PTM) where a sulfate group is added to a tyrosine moiety. This PTM is responsible for strengthening interaction between proteins. One of the drawbacks of studying this PTM is the lack of an antibody that can detect all tyrosine-sulfated proteins. In addition, due to the labile nature of the tyrosine sulfate, other techniques such as mass spectrometry cannot be used to study this PTM unless special modification procedures are used. This requires considerable skill and knowledge of mass spectrometry. This unit describes an in vitro technique that can be used to study tyrosine-sulfated proteins by radiolabeling the recombinant protein. The protein is then subject to barium hydroxide hydrolysis and thin-layer electrophoresis (TLE). Co-localization of radioactive tyrosine-sulfate with nonradioactive tyrosine sulfate standard spiked in before TLE analysis identifies a protein as tyrosine-sulfated protein. The advantage of this technique is that, it identifies all tyrosine-sulfated proteins without any bias and is the only technique that identifies the tyrosine sulfate residues in the protein.

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Identification of Tyrosine O Sulfated Proteins in Cow Retina and the 661W Cell Line

Kanan

Al‐Ubaidi

2015

Retinal Degenerative Diseases

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Lack of tyrosine O Sulfation compromises both rod and cone electroretinographic responses emphasizing the importance of this post-translational modification for vision. To identify tyrosine sulfated proteins in retina, cow retinal lysates were subjected to immunoaffinity purification using an anti-sulfotyrosine antibody. The tyrosine sulfated proteins were eluted from the column using a sulfotyrosine pentapeptide and identified using mass spectrometry. Similarly, tyrosine sulfated proteins secreted by the 661W cell line were identified. Proteins identified were vitronectin, fibronectin, fibulin 2, nidogen, collagen V alpha 2, complement component 3 and C4 and fibrinogen beta. All proteins were subjected to analysis by 'Sulfinator' to determine potential sulfated tyrosines.

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Fibulin 2, a Tyrosine O-Sulfated Protein, Is Up-regulated Following Retinal Detachment

Cited by 9 publications

References 76 publications

Biological Characterization of Gene Response to Insulin-Induced Hypoglycemia in Mouse Retina

Biological Characterization of Gene Response to Insulin-Induced Hypoglycemia in Mouse Retina

Detection of Tyrosine Sulfation on Proteins

Identification of Tyrosine O Sulfated Proteins in Cow Retina and the 661W Cell Line

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