Cellular Retinol- and Retinoic Acid-Binding Proteins

Chytil, Frank; Ong, David E.

doi:10.1007/978-1-4613-9937-7_2

Cited by 62 publications

(48 citation statements)

References 52 publications

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“…These t 1 ; 2s are shorter than those transported bound to plasma albumin), in the intestine, brain , and kidney of the fe tal rabbit , in limb buds of the mouse, and in embryonic chick skin (Chytil and Ong , 1983;Rainier et al, 1983;K warta et al , 1985;Sani and Hill , 1974). In the mouse limb bud , all-lill.M-RA has a 315-fold greater affinit y with cRABP than 13-cis-retinoic acid (13-ffi-RA) (Kwarta et al, 1985).…”

Section: Pharmacokineticsmentioning

confidence: 98%

“…chick skin (Chytil and Ong, 1983;Rainier et al, 1983;Kwarta et al, 1985). In the mouse limb bud, all-lli!lli.-RA has a 315-fold greater affinity for cRABP than 13-ili-RA (Kwarta et al, 1985).…”

Section: List Of Figuresmentioning

confidence: 99%

“…Chytil and Ong (1979) have put forth the hypothesis that retinoids are bound in the cytosol by either cellular retinol-binding protein (cRBP)(if an alcohol) or cRABP (if an acid) and are subsequently transported into the nucleus where they can modify gene expression.…”

Section: List Of Figuresmentioning

confidence: 99%

“…A free carboxyl group at Cl5 is required for binding of retinoids to cellular retinoic acid-binding protein (cRABP) (Chytil and Ong, 1983). Cellular retinoic acid-binding protein (cRABP) has been identified in all fetal rat tissues, in the intestine, brain, and kidney of the fetal rabbit, and in limb buds of the mouse (Chytil and Ong, 1983;Rainier et al, 1983;K warta et al, 1985). In mouse limb buds, all-!mru.-RA has a 315-fold greater affinity for cRABP than 13-lli-RA (Kwarta et al , 1985).…”

Section: Kochhar and Coworkers {1985) Induced Teratogenesis In Icr MImentioning

confidence: 99%

“…Sporn and Roberts (1983) and Omori and Chytil (1982) suggested that retinoids are modifiers of gene express ion . Chytil and Ong ( 1979) suggested that retinoids are bound in the cytosol by either cellular retinol-binding protein (cRBP) (if an alcohol) or cellular retinoic acid-binding protein (cRABP) (if an acid) and transported into the nucleus where they can modify gene expression. An alternative to the steroid-like mechanism for retinoids has been proposed by Sporn and Roberts (1983).…”

Section: Structure-toxicity Relationships and Postulated Mechanisms Omentioning

confidence: 99%

See 4 more Smart Citations

Structure-activity relationships of retinoids in developmental toxicology

Howard

Willhite

Dawson

et al. 1988

Toxicology and Applied Pharmacology

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Section: Pharmacokineticsmentioning

confidence: 98%

Section: List Of Figuresmentioning

confidence: 99%

Section: List Of Figuresmentioning

confidence: 99%

Section: Kochhar and Coworkers {1985) Induced Teratogenesis In Icr MImentioning

confidence: 99%

Section: Structure-toxicity Relationships and Postulated Mechanisms Omentioning

confidence: 99%

See 3 more Smart Citations

Structure-activity relationships of retinoids in developmental toxicology

Howard

Willhite

Dawson

et al. 1988

Toxicology and Applied Pharmacology

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Regulation of Differentiation of Tracheal Epithelial Cells by Retinoids

Jetten

Smits

1985

Novartis Foundation Symposia

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Effect of Gestational Age Upon Prealbumin and Retinol Binding Protein in Preterm and Term Infants

Sasanow,

Spitzer,

Pereira

et al. 1986

J. pediatr. gastroenterol. nutr.

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SummaryThe relationships between maternal and umbilical cord levels of prealbumin and retinol binding protein (RBP) were studied in 68 mothers and in their appropriate‐for‐gestational‐age neonates delivered between 25 and 42 weeks gestation. Arterial and venous concentrations of prealbumin and RBP in cord sera were also studied in a subsample of eight infants. In cord sera, prealbumin and RBP levels increased with gestational age (prealbumin, r = 0.47; RBP, r = 0.40, p < 0.01), and were significantly different in neonates born at term compared to those born prematurely (mean ± SD, prealbumin 12.0 ± 3.9 mg/dl vs. 8.8 ± 2.3 mg/dl, p < 0.001; RBP, 2.3 ± 0.8 vs. 1.8 ± 0.5 mg/dl, p < 0.005). No significant differences between arterial and venous concentrations of prealbumin and RBP were observed in cord blood. In maternal blood, serum prealbumin and RBP concentrations did not increase with length of gestation (25–42 weeks). Maternal prealbumin was not correlated significantly with infants' cord serum levels; the correlation coefficient for RBP was 0.29, p < 0.05. Maternal prealbumin and RBP serum levels were approximately twice the values seen in neonates born both at term and prematurely. Although the difference between premature and full‐term cord levels of prealbumin and RBP may reflect an increase in hepatic protein synthesis that occurs with maturation of the fetus and/or a change in placental function after 37 weeks gestation, neither of these factors sufficiently explains the variance in neonatal prealbumin and RBP levels.

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Cellular Retinol- and Retinoic Acid-Binding Proteins

Cited by 62 publications

References 52 publications

Structure-activity relationships of retinoids in developmental toxicology

Structure-activity relationships of retinoids in developmental toxicology

Regulation of Differentiation of Tracheal Epithelial Cells by Retinoids

Effect of Gestational Age Upon Prealbumin and Retinol Binding Protein in Preterm and Term Infants

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