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Cellular retinoic acid binding protein is associated with mitochondria
Author(s) -
Ruff Susan J,
Ong David E
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02366-8
Subject(s) - cytoplasm , mitochondrion , retinoic acid , organelle , immunofluorescence , biology , staining , cell fractionation , binding protein , biochemistry , microbiology and biotechnology , antibody , enzyme , gene , genetics , immunology
We report that immunohistochemical staining for cellular retinoic acid‐binding protein (CRABP) was restricted to the cytoplasm of cortical cells in bovine adrenal. In contrast, staining for the similar protein, cellular retinol‐binding protein (CRBP), was found throughout these cells. After transfections of CRABP and CRBP into cultured cells, immunofluorescence analyses again revealed cytoplasmic restriction only for CRABP, with a pronounced punctate appearance. Use of organelle‐specific fluorochromes indicated that CRABP immunofluorescence overlaid exactly with the pattern of the mitochondrial‐specific fluorochrome. Confirmation of this association came with subcellular fractionation of the adrenal cortex. CRABP, but not CRBP, co‐sedimented with the mitochondria, a novel finding for a member of this superfamily of cellular lipid‐binding proteins.