Ferritin light chain

Fibrinogen beta chain Ferritin light chain... 

The down-regulated proteins in HCC tissues have been identified. Park et al. identified aldehyde dehydrogenase 2 (25) and ferritin light chain (32). Kim et al. identified HSP 27, cathepsin D, and others (26). Lim et al. identified cytochrome B5, liver car-boxyesterase, and others (27). Li et al. identified SOD 1, aldolase B, and others (28). Fujii et al. identified galectin-1 (29). Kim et al. identified argininosuccinate synthase, carbamoyl-phosphate s mthase, and others (31). Table 1 shows the summary of the proteins whose expression was different between HCC cancer tissues and non-cancerous tissues. 

Table 3 shows the proteins up-regulated or down-regulated in panereatie eaneer tissues. Shen et al. reported that, in panereatie eaneer tissues, expressions of Mn-SOD, S100A8, annexin A4, eathepsin D, 14-3-3 zeta, tropomyosin 2, aetin, ferritin light chain, alpha-enolase, galectin-1, and cyclophilin A increased, and that those of peroxiredoxin... 

Park KS, Kim H, Kim NG et al. Proteomic analysis and molecular characterization of tissue ferritin light chain in hepatocellular carcinoma. Hepatology 2002 35 1459-1466. 

Fig 12. Schematic diagram of the ferroxidase center of human rHF (a), and the equivalent region of horse light-chain ferritin (b) showing the ferroxidase site replaced by a salt bridge. 

Unknowns are the light and heavy chains of ferritin, the iron-storage protein found in animals, plants, and microbes. 

Ferritin is a hollow shell containing 24 subunits that are a mixture of heavy (H) and light (L) chains, arranged in octahedral symmetry. The hollow core has a diameter of 8 nm and can hold as many as 4 500 iron atoms in the approximate form of the mineral ferrihydrite (5Fe203 9H2O). Iron(II) enters the protein through any of six pores located on the threefold symmetry axes of the octahedron. Oxidation to Fe(III) takes place at catalytic sites on the H chains. Sites on the inside of L chains appear to nucleate crystallization of ferrihydrite. 

Ferritin is an iron-storage protein, which keeps iron in a safe form within a protein shell. The protein shell of mammalian ferritin is composed of 24 subunits of heavy (H)and light (L) amino acid chains. The external diameter of the protein shell is about 12 nm, and the diameter of the internal cavity is about 7 nm. Inside this cavity up to 4500 ions of iron may be located. Most of the ferritin molecules are not full, but contain varying amounts of iron [IT]. 

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