scholarly journals Sex-dependent inhibition by retinoic acid of thyroid-hormone action on rabbit reticulocyte Ca2+-ATPase activity

1991 ◽  
Vol 273 (2) ◽  
pp. 489-492
Author(s):  
F B Davis ◽  
T J Smith ◽  
P J Davis ◽  
W D Lawrence ◽  
A J Ryan ◽  
...  

The interaction was examined in vitro of retinoic acid and thyroid hormone with rabbit reticulocyte Ca2(+)-ATPase. L-Thyroxine (T4) (0.1 nM) stimulated female-source Ca2(+)-ATPase activity (+21%; P less than 0.03) and inhibited male-source enzyme (-20%; P less than 0.05). Addition of retinoic acid (10 nM-1 microM) did not influence T4-inhibitable male-source Ca2(+)-ATPase, but caused a 52% loss of T4 effect on the female-source enzyme. Incubation of female-source membranes with testosterone caused the enzyme response to T4 and retinoic acid to become that of male-source membranes, and the male-source enzyme response was converted into the ‘female’ pattern by exposure to 17 beta-oestradiol. We postulate that a membrane-associated sex-steroid-dependent factor imparts a gender-specific interaction of thyroid hormone and retinoic acid on Ca2(+)-ATPase, and that ultimately the factor is shed during erythrocyte maturation.

2020 ◽  
Vol 21 (23) ◽  
pp. 8945
Author(s):  
Mercedes Fernández ◽  
Micaela Pannella ◽  
Vito Antonio Baldassarro ◽  
Alessandra Flagelli ◽  
Giuseppe Alastra ◽  
...  

While the role of thyroid hormones (THs) during fetal and postnatal life is well-established, their role at preimplantation and during blastocyst development remains unclear. In this study, we used an embryonic stem cell line isolated from rat (RESC) to study the effects of THs and retinoic acid (RA) on early embryonic development during the pre-implantation stage. The results showed that THs play an important role in the differentiation/maturation processes of cells obtained from embryoid bodies (EB), with thyroid hormone nuclear receptors (TR) (TRα and TRβ), metabolic enzymes (deiodinases 1, 2, 3) and membrane transporters (Monocarboxylate transporters -MCT- 8 and 10) being expressed throughout in vitro differentiation until the Embryoid body (EB) stage. Moreover, thyroid hormone receptor antagonist TR (1-850) impaired RA-induced neuroectodermal lineage specification. This effect was significantly higher when cells were treated with retinoic acid (RA) to induce neuroectodermal lineage, studied through the gene and protein expression of nestin, an undifferentiated progenitor marker from the neuroectoderm lineage, as established by nestin mRNA and protein regulation. These results demonstrate the contribution of the two nuclear receptors, TR and RA, to the process of neuroectoderm maturation of the in vitro model embryonic stem cells obtained from rat.


Thyroid ◽  
2009 ◽  
Vol 19 (6) ◽  
pp. 639-644 ◽  
Author(s):  
Lars C. Moeller ◽  
Craig Wardrip ◽  
Marek Niekrasz ◽  
Samuel Refetoff ◽  
Roy E. Weiss

Endocrinology ◽  
1982 ◽  
Vol 110 (1) ◽  
pp. 297-298 ◽  
Author(s):  
FAITH B. DAVIS ◽  
JOSEPH H. KITE ◽  
PAUL J. DAVIS ◽  
SUSAN D. BLAS

1999 ◽  
Vol 277 (4) ◽  
pp. H1338-H1349 ◽  
Author(s):  
Mara Ferrandi ◽  
Sergio Salardi ◽  
Grazia Tripodi ◽  
Paolo Barassi ◽  
Rodolfo Rivera ◽  
...  

Adducin point mutations are associated with genetic hypertension in Milan hypertensive strain (MHS) rats and in humans. In transfected cells, adducin affects actin cytoskeleton organization and increases the Na+-K+-pump rate. The present study has investigated whether rat and human adducin polymorphisms differently modulate rat renal Na+-K+-ATPase in vitro. We report the following. 1) Both rat and human adducins stimulate Na+-K+-ATPase activity, with apparent affinity in tens of nanomolar concentrations. 2) MHS and Milan normotensive strain (MNS) adducins raise the apparent ATP affinity for Na+-K+-ATPase. 3) The mechanism of action of adducin appears to involve a selective acceleration of the rate of the conformational change E2 (K) → E1 (Na) or E2(K) ⋅ ATP → E1Na ⋅ ATP. 4) Apparent affinities for mutant rat and human adducins are significantly higher than those for wild types. 5) Recombinant human α- and β-adducins stimulate Na+-K+-ATPase activity, as do the COOH-terminal tails, and the mutant proteins display higher affinities than the wild types. 6) The cytoskeletal protein ankyrin, which is known to bind to Na+-K+-ATPase, also stimulates enzyme activity, whereas BSA is without effect; the effects of adducin and ankyrin when acting together are not additive. 7) Pig kidney medulla microsomes appear to contain endogenous adducin; in contrast with purified pig kidney Na+-K+-ATPase, which does not contain adducin, added adducin stimulates the Na+-K+-ATPase activity of microsomes only about one-half as much as that of purified Na+-K+-ATPase. Our findings strongly imply the existence of a direct and specific interaction between adducin and Na+-K+-ATPase in vitro and also suggest the possibility of such an interaction in intact renal membranes.


Cell Calcium ◽  
1983 ◽  
Vol 4 (2) ◽  
pp. 71-81 ◽  
Author(s):  
Faith B Davis ◽  
Elliott Middleton ◽  
Paul J Davis ◽  
Susan D Blas

2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
Joshua D. Safer

Although thyroid hormone is one of the most potent stimulators of growth and metabolic rate, the potential to use thyroid hormone to treat cutaneous pathology has never been subject to rigorous investigation. A number of investigators have demonstrated intriguing therapeutic potential for topical thyroid hormone. Topical T3has accelerated wound healing and hair growth in rodents. Topical T4has been used to treat xerosis in humans. It is clear that the use of thyroid hormone to treat cutaneous pathology may be of large consequence and merits further study. This is a review of the literature regarding thyroid hormone action on skin along with skin manifestations of thyroid disease. The paper is intended to provide a context for recent findings of direct thyroid hormone action on cutaneous cellsin vitroandin vivowhich may portend the use of thyroid hormone to promote wound healing.


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