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Differential intracellular localization of lysyl oxidase in vitro and in vivo
Author(s) -
Okkelman Irina Alexandrovna,
Pestov Nikolay Borisovich,
Fedotova Anna Sergeevna
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.816.1
Subject(s) - lysyl oxidase , in vitro , extracellular matrix , intracellular , extracellular , microbiology and biotechnology , hela , cell culture , subcellular localization , 3t3 cells , biology , in vivo , cell type , cell , chemistry , biochemistry , transfection , cytoplasm , genetics
Lysyl oxidase is a copper‐dependent amino oxidase that plays an important role in protein cross‐linking. LOX is usually secreted into extracellular space but LOX was also found in the nucleus of many cell types including smooth muscle cells and 3T3 fibroblasts. Using immunocytochemical and immunohistochemical techniques, we compared subcellular localization of LOX in various cells cultured in vitro as well as in different tissues. Endogenous LOX was detected predominantly in nuclear dot‐like structures of cultured cells: NIH 3T3 fibroblasts, Hela, epithelial derived lung cancer cell lines A549 and CALU‐1, and also in primary embryo fibroblasts. In contrast with these results obtained on in vitro cultured cells, such a striking pattern of intracellular distribution was never observed in various histological samples. Interestingly, LOX appears to be abundant in platelets and neutrophils and, in the latter case, LOX staining was also completely extranuclear. In addition, overexpression of recombinant LOX in Hela cells leads to its accumulation outside the nucleus. Therefore, abundant nuclear localization of LOX protein in cultured cells in vitro may be not relevant to its distribution in vivo . Supported by MCB Program of the Russian Academy of Sciences.