Disease relevance of TDGF5

• We compared digital retinal images and 35 mm colour transparencies taken with the Canon CR5 retinal camera for the detection and grading of diabetic retinopathy in a clinical setting, in a randomized, blinded study of diabetic patients with a spectrum of severity of diabetic retinopathy [1].

High impact information on TDGF5

• The first TER structures have been reported, for regions of the catalytically essential pseudoknot and CR4/CR5 domains of human TER, and provide a structural basis for interpretation of mutational and biochemical data [2].
• On the basis of intracellular acidifications in the presence of 30 microM cariporide, we selected a fibroblast cell line termed CR5, expressing a mutated Na(+)/H(+) exchanger NHE-1 with a low affinity for cariporide (87 +/- 11.6 microM) and extracellular sodium (248 +/- 63.7 mM) [3].
• The presence of more than one binding site on RAP for CR domains from LRP, together with the previous demonstration by others that RAP can bind to CR5-CR6 with comparably low affinities suggest an explanation for the dual roles of RAP as a folding chaperone and a tight competitive inhibitor of ligand binding [4].
• METHODS: We analysed 758 fundal images of 385 patients with diabetes attending the clinic obtained using a Canon CR5 with an EOS10 digital camera through a dilated pupil [5].

Biological context of TDGF5

• The introduction of the Canon CR5 45NM non-mydriatic retinal camera with the Frost Medical Software RIS-Lite digital imaging system provides a new screening tool for diabetic retinopathy with potential for remote diagnosis and telemedicine [6].

Anatomical context of TDGF5

• Using intracellular acidifications in the presence of 3 mM external sodium on the CR5 fibroblasts, we isolated two revertants which exhibited a complete recovery for sodium affinity but were still resistant to cariporide [3].

References