The intermediate-affinity CTLs may increase and decrease choline uptake under different conditions. Further investigations into the function of SLC44A5 as a choline transporter are required. The majority of cellular choline is phosphorylated by choline kinase to phosphocholine, which is essential for the formation of membrane phosphatidylcholine in the Kennedy pathway. Our metabolic studies indicated that SLC44A5 did not transport phosphocholine. Thus SLC44A5 transports choline before entering the Kennedy pathway, suggesting that SLC44A5 might keep the appropriate level of cellular choline. During pregnancy, fetal plasma choline levels are kept higher than maternal plasma, implicating the importance of choline for the developing fetus. Dietary rumen-protected choline improved reproductive performance of Holstein dairy cows. However, supplementing too much choline would increase the birth weight of calves and cause dystocia. Thus SLC44A5 might transport excess choline and keep the appropriate size of fetus. In conclusion, we found that birth weight in cattle was associated with SLC44A5. SLC44A5 is a choline transporter and the birth weight of cows with the G polymorphism in the 59 UTR of SLC44A5 is smaller than that of cows with the A polymorphism. This G polymorphism increases the expression level of SLC44A5. Our work identified that SLC44A5 is a critical mediator of birth weight and that SLC44A5 might be a useful target for preventing dystocia. Several histopathological changes in the RAD001 retinal pigment epithelial cell and in its underlying basement membrane, are distinctly characteristic of aging and may contribute to sight-threatening age-related macular degeneration. For instance, aging of RPE is associated with a progressive accumulation of autofluorescent pigments consisting of photo-sensitive bisretinoid compounds. In Bruch’s membrane, there is a build-up of esterified cholesterol-rich apolipoprotein Bcontaining lipoprotein that originates from RPE cells. Bruch’s membrane also undergoes thickening, diffusional rates across this layer are diminished, the integrity of the elastic lamina of Bruch’s membrane is compromised and collagens in this layer become cross-linked and less soluble. Histologically visible dome-shaped extracellular deposits that can be detected as yellow-white lesions in a retinal fundus image, are also common in older individuals. Drusen size and area within the macula are factors considered in the clinical characterization of age-related macular degeneration. Besides containing neutral lipid, drusen house a number of proteins which function within the complement system. This feature is of interest since genetic studies demonstrate that sequence variants in some complement related proteins confer increased risk or protection against age-related macular degeneration. As part of the pathological process, resident proteins within drusen accumulate non-enzymatic modifications in the form of advanced glycation end-products. AGE-modified proteins have been detected in drusen by immunocytochemistry, by Raman confocal microscopy and by chromatography. AGE formation is pronounced in diabetes and several disorders of aging such as atherosclerosis. In diabetes, AGE modification is a product of autooxidation and decomposition of carbohydrates and is considered to be a major pathogenic link between hyperglycemia and the onset and progression of disease. Conversely, the origin of AGEs such as carboxymethyllysine and carboxyethyllysine in ocular drusen is not known. Here we have demonstrated that methylglyoxal and glyoxal, two agents known to form AGEs, are released upon photodegradation of A2E.