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ABSTRACT : To investigate the expression of pigment epithelium-derived factor (PEDF) and αB-crystallin in human lens epithelial cells (LEC) and explore their relationships with diabetes.: Lens anterior capsules attached with LEC were collected from cataract surgeries in patients with or without diabetes, and grouped as following: non-diabetes mellitus (NDM) group, no diabetic retinopathy (NDR) group, non-proliferative diabetic retinopathy (NPDR) group and proliferative diabetic retinopathy (PDR) group. The expression of PEDF and αB-crystallin in all groups were determined by Western blot and immunofluorescence assay.: PEDF and αB-crystallin protein were both detected in LEC. PEDF was mainly distributed in the cytoplasm, whereas αB-crystallin was present in both cytoplasm and nucleus. The levels of PEDF protein and αB-crystallin protein in LEC were significantly increased with the appearance and aggravation of diabetic retinopathy (DR) (p<0.01).: The expression of PEDF and αB-crystallin protein are both positively correlated with the progression of DR, which may contribute to the regulation of iris neovascularization.
This article was published in the following journal.
Name: Current eye research
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One of the subunits of alpha-crystallins. Unlike ALPHA-CRYSTALLIN B CHAIN the expression of ALPHA-CRYSTALLIN A CHAIN is limited primarily to the lens (LENS, CRYSTALLINE).
One of the alpha crystallin subunits. In addition to being expressed in the lens (LENS, CRYSTALLINE), alpha-crystallin B chain has been found in a variety of tissues such as HEART; BRAIN; MUSCLE; and KIDNEY. Accumulation of the protein in the brain is associated with NEURODEGENERATIVE DISEASES such as CREUTZFELDT-JAKOB SYNDROME and ALEXANDER DISEASE.
A subclass of crystallins that provides the majority of refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Alpha-crystallins also act as molecular chaperones that bind to denatured proteins, keep them in solution and thereby maintain the translucency of the lens. The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits.
A class of crystallins that provides refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Beta-crystallins are similar in structure to GAMMA-CRYSTALLINS in that they both contain Greek key motifs. Beta-crystallins exist as oligomers formed from acidic (BETA-CRYSTALLIN A CHAIN) and basic (BETA-CRYSTALLIN B CHAIN) subunits.
A type of crystallin that has been found in the lens (LENS, CRYSTALLINE) of certain species of VERTEBRATES. They are inactivated form of PHOSPHOPYRUVATE HYDRATASE.
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