ArticlePloS one2014
Complement factor H, vitronectin, and opticin are tyrosine-sulfated proteins of the retinal pigment epithelium.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Bone sialoprotein: a multifunctional regulator of bone remodelling and tumour progression.Bone research · 2026Review
- Potential Involvement of Sulfotransferase in the Mechanism of Lamotrigine-induced Skin Rash.Chemical research in toxicology · 2023Article
- Small leucine rich proteoglycans: Biology, function and their therapeutic potential in the ocular surface.The ocular surface · 2023Review
- Engineering of SH2 Domains for the Recognition of Protein Tyrosine O-Sulfation Sites.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Engineering of a Small Protein Scaffold To Recognize Sulfotyrosine with High Specificity.ACS chemical biology · 2021Article
- High Myopia and the Complement System: Factor H in Myopic Maculopathy.Journal of clinical medicine · 2021Article
- Silicon Nanowire Field-Effect Transistor as Biosensing Platforms for Post-Translational Modification.Biosensors · 2020Article
- The origins and developments of sulfation-prone tyrosine-rich and acidic N- and C-terminal extensions of class ll and lll small leucine-rich repeat proteins shed light on connective tissue evolution in vertebrates.BMC evolutionary biology · 2020Article
- From Translation to Protein Degradation as Mechanisms for Regulating Biological Functions: A Review on the SLRP Family in Skeletal Tissues.Biomolecules · 2020Review
- Structure-based design of nucleoside-derived analogues as sulfotransferase inhibitors.RSC advances · 2019Article
- Differential cleavage of lysyl oxidase by the metalloproteinases BMP1 and ADAMTS2/14 regulates collagen binding through a tyrosine sulfate domain.The Journal of biological chemistry · 2019Article
- ACUTE CENTRAL SEROUS CHORIORETINOPATHY: Factors Influencing Episode Duration.Retina (Philadelphia, Pa.) · 2017Observational
- Plasma metabolomic study in Chinese patients with wet age-related macular degeneration.BMC ophthalmology · 2017Article
- Role of tyrosine-sulfated proteins in retinal structure and function.Experimental eye research · 2015Review
- Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.Matrix biology : journal of the International Society for Matrix Biology · 2015Review
- Tyrosine sulfation as a protein post-translational modification.Molecules (Basel, Switzerland) · 2015Review
- Uncommon posttranslational modifications in proteomics: ADP-ribosylation, tyrosine nitration, and tyrosine sulfation.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lack of tyrosine sulfation of ocular proteins results in disorganized photoreceptor structure and drastically reduced visual function, demonstrating the importance of this post-translational modification to vision. To understand the role that tyrosine sulfation plays in the function of ocular proteins, we identified some tyrosine-sulfated proteins in the retinal pigment epithelium using two independent methods, immuno-affinity column purification with an anti-sulfotyrosine specific antibody and computer-based sequence analysis of retinal pigment epithelium secretome by means of the prediction program Sulfinator. Radioactive labeling followed by thin layer electrophoresis revealed that three proteins, vitronectin, opticin, and complement factor H (CFH), were post-translationally modified by tyrosine sulfation. The identification of vitronectin and CFH as tyrosine-sulfated proteins is significant, since both are deposited in drusen in the eyes of patients with age-related macular degeneration (AMD). Furthermore, mutations in CFH have been determined to be a major risk factor in the development of AMD. Future studies that seek to understand the role of CFH in the development of AMD should take into account the role that tyrosine sulfation plays in the interaction of this protein with its partners, and examine whether modulating sulfation provides a potential therapeutic target.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.