Interaction of the retinol/cellular retinol-binding protein complex with isolated nuclei and nuclear components.

Liau, Gene; Ong, David E.; Chytil, Frank

doi:10.1083/jcb.91.1.63

Cited by 122 publications

(39 citation statements)

References 30 publications

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“…Since the finding by Strickland (4)(5)(6), while the other is the nucleus, where retinoic acid (or retinol) carried by cellular binding proteins (7,8) binds to chromatin (29,30) and leads to alteration in gene expression (31). A possible relationship to protein kinases has also been suggested by recent findings of cooperative actions of adenosine 3',5'-cyclic monophosphate (32) or phorbol esters (33) with retinoids in embryonal teratocarcinoma cells.…”

Section: Discussionmentioning

confidence: 91%

Induction of murine teratocarcinoma cell differentiation by suppression of poly(ADP-ribose) synthesis.

Ōhashi¹,

Ueda²,

Hayaishi³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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Poly(ADP-ribose) synthesizing activity in mouse teratocarcinoma EC-Al cells decreased markedly during differentiation induced by retinoic acid; the activities assayed in permeabilized cells decreased to 25% and 10% of the activity of control (uninduced cells) 2 and 3 days, respectively, after the addition of 0.1 ,uM retinoic acid to the culture medium. This change preceded changes in morphology and DNA synthesis, which became prominent after 4 days. The decrease in poly(ADP-ribose) synthesizing activity appeared to be caused by a diminution of the synthetase protein and not by a decrease in its catalytic activity, because the full activity disclosed by DNase I treatment decreased in parallel, albeit at about 20 times higher levels. When 8 mM 3-aminobenzamide or 10 mM nicotinamide, specific inhibitors of poly(ADP-ribose) synthetase, was added to the culture medium, the cells underwent differentiation after 7-9 days. An analogue, 3-aminobenzoic acid, which is not inhibitory to the synthetase, induced differentiation much less efficiently than did 3-aminobenzamide, and the effect of 3-aminobenzoic acid appeared to be ascribable to its potent cytotoxicity. Immunohistochemical analysis using anti-poly(ADP-ribose) antibody confirmed the marked reduction in poly(ADP-ribose) synthesizing activity in nuclei of the cells treated with retinoic acid or 3-aminobenzamide but not with 3-aminobenzoic acid. These results suggest that a decrease in poly(ADP-ribose) synthesis triggers differentiation of teratocarcinoma cells.Retinoic acid and related compounds (retinoids) have been shown to induce differentiation of several lines of murine teratocarcinoma cells into endoderm epitheloid cells or fibroblast-like cells (1, 2). The molecular mechanism of this induction of differentiation is not yet fully understood (3); De Luca (4), Wolf et al. (5), and Jetten and De Luca (6) reported observations suggesting a role of retinyl phosphate mannose in early cell surface changes, while Chytil and Ong (7) and Jetten and Jetten (8) proposed an alteration in transcription mediated by specific binding proteins. We became interested in these cells in view of our and others' finding that poly(ADP-ribose) is closely related to cell differentiation (9, 10). Poly(ADP-ribose) is a macromolecule synthesized from NAD in eukaryotic cells by a chromatin-bound enzyme, poly(ADP-ribose) synthetase (11). This synthesis proceeds in covalent attachment, at one terminus of the polymer, to various protein acceptors such as histones, nonhistone chromosomal proteins, and the synthetase itself (11). Accumulating evidence suggests that this polymer is involved in DNA repair (12-14), cell transformation (15, 16), and cell differentiation (9,10). Previously, we demonstrated that the poly(ADP-ribose) synthesizing activity serves as a marker of differentiation of human granulocytes (17, 18), leukemic lymphocytes (19), and epidermal cells (20

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Section: Discussionmentioning

confidence: 91%

Induction of murine teratocarcinoma cell differentiation by suppression of poly(ADP-ribose) synthesis.

Ōhashi¹,

Ueda²,

Hayaishi³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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“…Another hypothesis for retinoid action suggested that retinoids might act in a manner analogous to steroid hormones (Chytil and Ong, 1979;Liau et al, 1981). Indeed, several cytosolic binding proteins have been identified: two for retinol and one for retinoic acid (Chytil and Ong, 1983).…”

Section: Possible Mechanisms For Retinoid Action: Indirect Versus Directmentioning

confidence: 99%

Regulation of human mesothelial cell differentiation: opposing roles of retinoids and epidermal growth factor in the expression of intermediate filament proteins.

Kim

Stellmach

Javors

et al. 1987

The Journal of Cell Biology

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“…The lack of nuclear staining was not unexpected. Although CRBP delivers retinol to specific binding sites within the liver nucleus, it does not itself remain bound (16). Radioimmunoassay of subcellular fractions has confirmed that CRBP exists predominantly in the cytoplasm (17).…”

mentioning

confidence: 99%

Localization of cellular retinol-binding protein in several rat tissues.

Porter¹,

Fraker²,

Chytil³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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The distribution of cellular retinol-binding protein (CRBP) in rat liver, ileum, and epididymis was examined by the peroxidase-antiperoxidase immunolocalization technique. Positive cytoplasmic staining was seen in the liver when antiserum prepared against purified CRBP was used but not when antiserum absorbed with purified CRBP was used. Ileal mucosa, a tissue that contains no detectable CRBP, showed no positive staining. The epididymis showed strong positive staining in the caput but not in the cauda. Staining was present in principal and basal cells but not in peritubular or interstitial cells. Radioimmunoassay revealed that the CRBP within the caput epididymidis was localized in the initial segment and proximal region, areas known to be involved in the synthesis and secretion of factors necessary for sperm maturation. The results demonstrate that the expression of CRBP may vary within the same cell type, as well as between different cell types within the same tissue.Vitamin A is known to be essential for the support and differentiation of most epithelial tissues (1). Although the mechanism of retinol (vitamin A alcohol) action is unknown, an increasing body of evidence suggests that its effects are mediated in part by cellular retinol-binding protein (CRBP) (2, 3). CRBP is present in all retinol-sensitive tissues of the body but at widely varying levels (4). In addition, the levels of CRBP within a tissue can change during perinatal development (5) and also with the induction of neoplasia (6)(7)(8). This variation might be due to differing cellular levels of CRBP, differing populations of cells that contain CRBP, or both.Previous attempts to examine this question have been by fractionation of the various cell types, followed by measurement of CRBP content through the ability to bind retinol (9). This cannot be done for all tissues and is particularly ineffective for cell types of limited abundance. To overcome this, we have identified CRBP in intact tissue sections, using an immunohistochemical technique. We report here the immunolocalization of CRBP in several rat tissues known to contain high levels of CRBP. In addition, immunolocalization in one organ showed an unexpected cellular distribution of CRBP, which was verified both by retinol binding and by radioimmunoassay.MATERIALS AND METHODS Preparation of CRBP. CRBP was purified from rat liver as described (10).Production and Detection of Antibodies. Specific antibodies to CRBP were raised in male New Zealand rabbits by methods described earlier (4).Radioimmunoassay of CRBP. Tissues were prepared and CRBP levels measured as described (4). Liver, ileum, and epididymis were obtained from normal, chow-fed rats (Harlan Industries, Indianapolis, IN). The epididymis was dissected into its various regions, each of which was then assayed separately. Protein content was determined by the method of Lowry et al. (11).Immunolocalization of CRBP. The peroxidase-antiperoxidase (PAP) technique of Sternberger was used (12). Rats were killed by decapitation, and t...

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Interaction of the retinol/cellular retinol-binding protein complex with isolated nuclei and nuclear components.

Cited by 122 publications

References 30 publications

Induction of murine teratocarcinoma cell differentiation by suppression of poly(ADP-ribose) synthesis.

Induction of murine teratocarcinoma cell differentiation by suppression of poly(ADP-ribose) synthesis.

Regulation of human mesothelial cell differentiation: opposing roles of retinoids and epidermal growth factor in the expression of intermediate filament proteins.

Localization of cellular retinol-binding protein in several rat tissues.

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