Transcortin: A Corticosteroid-binding Protein of Plasma. VII. Half-Life in Normal and Estrogen-treated Subjects *

Sandberg, Avery A.; Woodruff, Marvin W.; Rosenthal, Hannah E.; Nienhouse, S.; Slaunwhite, W. Roy

doi:10.1172/jci104931

Cited by 61 publications

(11 citation statements)

References 16 publications

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“…Furthermore, a half-life T1 /2 value of about 5 days for CBG has been measured in sheep (Ballard et al, 1982), rats and humans (Sandberg et al, 1964). Our results in newborn guinea-pigs confirm these postnatal changes in CBG .…”

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confidence: 79%

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The regulation of glucocorticosteroid secretion during the perinatal period

Dalle¹,

Pradier²,

Delost³

1985

Reprod. Nutr. Dévelop.

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Summary. The regulation of adrenal activity during the perinatal period raises different experimental problems ; studies are often limited and their conclusions vary with the species studied. During the perinatal period, the profile of the ratio of adrenal weight to body weight reaches a minimum earlier the more mature is the species ; this minimum occurs before birth in sheep, at birth in guinea-pigs and 10 days after birth in mice.In mature species, fetal plasma cortisol is higher than that of the mother ; it rises sharply near term. In other species, maternal plasma cortisol remains higher than that of the fetus which also rises during the days before birth. In all species, the fetal adrenal is activated concomitantly with a sharp increase of the action of corticosteroid binding globulin on fetal plasma. The (Jost, 1954(Jost, , 1957(Jost, , 1966 (Wintour et al., 1975). In these species, the induction of parturition by the fetal adrenal gland has been extensively described and reviewed (Liggins et al., 1973). 4) Guinea-pigs : these laboratory animals present a relatively long gestation period with fetuses large enough to permit fetal surgical procedures and vessel catheterization. Moreover, the guinea-pig placenta appears to be very active and broadly resembles that of women (Duval, 1889 ;Myers et al., 1936 ;Kaufmann and Davidoff, 1977 (Gay, 1976 (Comline and Silver, 1961), pigs (Dvorak, 1972), goats (Currie and Thornburn, 1977) and calves (Boshier et al., 1980 ;Richet et al., 1984) Thornburn, 1977 ; pigs : F6vre, 1975 (Khaldoun, 1977) and macaques (Robinson and Bridson, 1978).The profile of CBG in neonatal plasma parallels this decrease. Furthermore, a half-life T1 /2 value of about 5 days for CBG has been measured in sheep (Ballard et al., 1982), rats and humans (Sandberg et al., 1964 (Koch, 1969) or in neonatal rabbits (Sereni et al., 1966). In newborn guinea-pigs, the glucocuronide conjugating system is defective (Brown and Zuelzer, 1958), and Dalle et a/. (1985) have demonstrated that, in this species, cortisol metabolism depends on its degradation in the liver and on its distribution volume. This volume develops during the neonatal period (Dalle et al., 1985), paralleling body growth after 10 days postpartum, but more slowly before this stage. Fetal steroid metabolism cannot be investigated without keeping in mind maternal influence on fetal plasma corticosteroid levels. Furthermore, the role of placental enzymes in steroid metabolism has been well documented in several species, especially in humans (Diczfalusy, 1962(Diczfalusy, , 1969Murphy, 1981) (Osinski, 1960 ;Villee et al., 1961 ; Goldkrand et al., 19761. We demonstrated a similar process in guinea-pigs (Dalle and Delost, 1976) showing that the cortisone/cortisol ratio in newborn plasma might be used as an index of adrenal maturity.The origin of fetal corticosteroids was investigated and their metabolism measured by infusing radioactive cortisol to pregnant guinea-pigs or to their fetuses.At the end of gestation, 90 % of the fetal cortisol...

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confidence: 79%

“…Furthermore, a half-life T1 /2 value of about 5 days for CBG has been measured in sheep (Ballard et al, 1982), rats and humans (Sandberg et al, 1964 (Koch, 1969) or in neonatal rabbits (Sereni et al, 1966). In newborn guinea-pigs, the glucocuronide conjugating system is defective (Brown and Zuelzer, 1958), and Dalle et a/.…”

mentioning

confidence: 99%

The regulation of glucocorticosteroid secretion during the perinatal period

Dalle¹,

Pradier²,

Delost³

1985

Reprod. Nutr. Dévelop.

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“…We have carefully demonstrated that the half-lives of intact and elastase cleaved human CBG in the rabbit are identical and hence not significantly different but much shorter than the 5 days reported in humans [15]. In rabbits it is longer than the half-life (6.8 h) reported for native human CBG in hamsters [16] but shorter than the circulating biological half-life of 13 h reported for 2 forms of rabbit CBG [17].…”

Section: Discussionmentioning

confidence: 60%

The half-lives of intact and elastase cleaved human corticosteroid-binding globulin (CBG) are identical in the rabbit

Lewis

Saunders

Dyer

et al. 2015

The Journal of Steroid Biochemistry and Molecular Biology

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“…Corresponding values for the half-time of I131-TBPA in the plasma were 2.67 ± 0.53 days, values in close agreement with those reported by Oppenheimer and colleagues for the terminal slope of I131-TBPA disappearance (12). Thus, TBPA appears to be among the most rapidly turning over of the plasma proteins thus far studied (26,(31)(32)(33)(34).…”

Section: Discussionmentioning

confidence: 99%

Preparation of I-131-labeled human serum prealbumin and its metabolism in normal and sick patients.

Socolow¹,

Woeber²,

Purdy³

et al. 1965

J. Clin. Invest.

118

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Despite some early doubts concerning its presence in plasma and its physiological function (1-4), the thyroxine-binding prealbumin of human serum (TBPA) is now known to play a significant role in the transport of thyroxine (T4) (5-8). Normally, as assessed by in vitro techniques, TBPA appears to bind at least 25 to 35%o of T4 in serum (5,6). In the serum of many patients with severe acute or chronic illness, however, the proportion of endogenous T4 in serum bound by TBPA and the T4-binding capacity of TBPA decline (8,9). The recent availability of substantial quantities of a highly purified preparation of TBPA has made possible an investigation of the in vivo metabolism of this protein in normal patients and in patients with a variety of disorders that lead to decreased binding of T4 by TBPA in serum. In addition, the cause of this decrease in T4 binding in the serum of such "sick" patients has been evaluated. A portion of the findings has been presented in abstract form (10). While these studies were in progress, Oppenheimer, Surks, Bernstein, and Smith reported similar studies in abstract form (11,12). MethodsHighly purified TBPA was prepared from plasma Fraction IV-6 (method 6) of Cohn and colleagues (13).* Submitted for publication April 9, 1965; accepted June 16, 1965. This The method of purification of the protein and details of its characterization will be described in detail elsewhere (14). Additional characterization of the specific batch of protein employed in the present studies was carried out. Solutions of TBPA (2.0 g per 100 ml), enriched with I'-labeled T4,1 were subjected to electrophoresis in acrylamide gel in a Tris-maleate buffer system,2 pH 9.2. Gel concentrations of 5.0, 7.0, and 8.0 g per 100 ml were employed, and, in some instances, two dimensional gel electrophoretic studies were conducted (15). After electrophoresis, gels were radioautographed and then stained with amido black 10 B.Iodination of TBPA. To minimize the possibility of denaturing the TBPA during the iodination process, a technique was developed for iodinating protein by a microdiffusion process. The technique, an adaptation of that described by Banerjee and Ekins (16), was first employed in tests with human serum albumin (HSA) or with purified TBPA for relatively low specific activity labeling. When the method had been standardized, it was employed for higher specific activity labeling of the TBPA used in the present studies. This was performed as follows. All glassware and buffer media employed were autoclaved before use. A 2.0 g per 100 ml solution of TBPA was prepared in 0.01 M phosphate buffer, pH 7.5, and 200 Al was pipetted into the center well of a single side-armed Warburg flask of 5.0 ml capacity. NaI' (10 to 15 mc, free of carrier iodide and reducing agent),8 together with 60 Ag of unlabeled NaI, was introduced into the main compartment of the vessel in approximately 1 ml of phosphate buffer. Five hundred Al of fresh 3% H202 4 was added to the side arm, and the vessel was closed with a greased ground-glass stopp...

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Transcortin: A Corticosteroid-binding Protein of Plasma. VII. Half-Life in Normal and Estrogen-treated Subjects *

Cited by 61 publications

References 16 publications

The regulation of glucocorticosteroid secretion during the perinatal period

The regulation of glucocorticosteroid secretion during the perinatal period

The half-lives of intact and elastase cleaved human corticosteroid-binding globulin (CBG) are identical in the rabbit

Preparation of I-131-labeled human serum prealbumin and its metabolism in normal and sick patients.

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