Differential regulation of calbindin-D28k mRNA in the intestine and eggshell gland of the laying hen

1990 ◽  
Vol 4 (2) ◽  
pp. 93-99 ◽  
Author(s):  
A. Bar ◽  
S. Striem ◽  
S. Mayel-Afshar ◽  
D. E. M. Lawson

ABSTRACT The effect of shell calcification and 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3) on calbindin-D28k (previously known as vitamin D-dependent calcium-binding protein) and calbindin mRNA was investigated in the intestine and eggshell gland (ESG) of juvenile female chicks, laying hens and non-laying female birds with active gonads. Increasing amounts of 1,25-(OH)2D3 were fed to laying hens and juvenile birds treated with oestradiol to develop the ESG. The intestinal concentration of calbindin was increased 30-fold by 1,25-(OH)2D3 in chicks treated with oestradiol and fed a vitamin D-deficient diet. In these same animals, 1,25-(OH)2D3 had no effect on the formation of calbindin mRNA or calbindin in the ESG even though fully viable 1,25-(OH)2D3 receptors are present in this tissue. In laying birds fed adequate amounts of vitamin D3, intestinal, but not ESG, calbindin was increased by the addition of 1,25-(OH)2D3 to the diet. At the onset of egg production the concentrations of calbindin and calbindin mRNA were increased in the intestine and ESG. This increase occurred within the period of calcification of the first egg, through a process unaffected by vitamin D. Calcification of the first egg increased the concentration of calbindin in the ESG by eight- to tenfold, although the concentration of calbindin mRNA was increased by only two- to threefold. These results suggest that the induction of calbindin synthesis by 1,25-(OH)2D3 or by the egg calcification process is associated with an increase in the concentration of calbindin mRNA in the ESG and intestine. They also suggest that the vitamin D-dependent physiological changes in the ESG occurring during the calcification process do not include an increase in calbindin synthesis, that calbindin is induced and/or regulated by a mechanism requiring additional factors besides 1,25-(OH)2D3, and that post-transcriptional regulation of calbindin synthesis in these tissues may be possible.

2000 ◽  
Vol 164 (1) ◽  
pp. 67-76 ◽  
Author(s):  
K Hamilton ◽  
M Tein ◽  
J Glazier ◽  
EB Mawer ◽  
JL Berry ◽  
...  

Offspring of rats with diabetes mellitus are at risk of reduced calcium and bone mineral content. Altered expression of the maternal calcium binding proteins, calbindin-D(9K) and calbindin-D(28K), which are involved in renal and placental calcium transport, may underlie these problems.We have investigated the effect of diabetes on circulating concentrations of regulatory hormones with respect to calbindin-D mRNA concentrations. Three rat groups were studied; control (CP), streptozotocin-induced diabetic (DP), and insulin-treated diabetic (DPI) pregnant rats. Calbindin-D(9K) and calbindin-D(28K) mRNA abundance in placenta and maternal kidney were measured at days 7, 15, 18 and 21 of gestation, together with serum or plasma concentrations of 1,25 dihydroxyvitamin D(3) (1, 25(OH)(2)D(3)), parathyroid hormone (PTH), PTH-related protein (PTHrP), calcitonin, oestradiol and IGF-I. An increase in placental calbindin-D(9K) mRNA abundance between days 18 and 21 in CP and DPI rats was severely blunted in the DP rats. In contrast, renal calbindin-D(28K) mRNA abundance was greater at days 7, 15 and 18 in DP compared with CP rats, as was calbindin-D(9K) at day 18. Calcitonin concentrations showed no differences between the groups, and both PTH and IGF-I were reduced over the first half of gestation, unlike the calbindins. In contrast, the concentrations of PTHrP and 1,25(OH)(2)D(3) were reduced at term in the DP group compared with the other two groups. Plasma oestradiol concentrations were lower in DP than in CP rats at days 7, 15 and 18, and most striking was the absence in DP rats of the peak of oestradiol seen at day 18 in CP rats. Despite the similarity between changes in placental calbindin mRNA and 1,25(OH)(2)D(3), previous work has shown placental calbindin-D(9K) regulation to be vitamin-D-independent. These studies produce suggestive evidence, therefore, that PTHrP and oestradiol may be involved in the altered calbindin-D expression by kidney and placenta in rat diabetic pregnancy.


2020 ◽  
Author(s):  
Qian Xin ◽  
Jingpeng Zhao ◽  
Hongchao Jiao ◽  
Haifang Li ◽  
Xiaojuan Wang ◽  
...  

Abstract Background: The absorption and transportation of calcium and phosphorus is mainly relied on their corresponding transporters. Eggshell is mainly formed during dark time in one egg cycle. The aim of this study was to determine the effect of different light regime on eggshell quality and the expression of the relevant calcium and phosphorus transporters in laying hens. Seventy two 56-week-old laying hens were randomly divided into two groups and subjected to the following treatments: 16 h light: 8 h dark (control) and 9 h light: 15 h dark (LDP). The expression of phosphorus transporters type IIb Na/Pi co-transporter NaPi-IIa (NPt2a) and NaPi-IIb (NPt2b), calcium transporter calbindin-D28k (CaBP-D28k), and plasma membrane Ca ATPase 1b (PMCA1b) were measured in small intestine, kidney, and eggshell gland. Results: The results showed that the feed intake (P < 0.001) and egg weight (P = 0.05) was decreased by LDP treatment, while laying rate, egg production, and feed efficiency were not significantly influenced (P > 0.05). Compared to control, eggshell hardness was increased (P < 0.05) by LDP treatment whereas eggshell thickness and eggshell percentage were not significant changed. Eggshell calcium (Ca) and phosphorus (P) contents were elevated in LDP-hens, compared to control birds. Compared to control birds, serum Ca (P < 0.01) and P levels (P = 0.079) at dark time were increased in LDP-hens while and alkaline phosphatase (ALP) activity was lowered (P < 0.05). The protein expression levels of CaBP-D28k and PMCA1b were not influenced in duodenum but were decreased at light time in jejunum of LDP hens. In kidney, the expression of CaBP-D28k, PMCA1b and NPt2a were not changed by LDP treatment. In eggshell gland, however, the expression of CaBP-D28k and osteopontin (OPN) were relative higher in LDP hens compared to control birds, whereas the PMCA1b expression was not altered. Conclusions: The result indicates that the increased circulating Ca and P concentrations in dark time are favorable for the deposition of calcium and phosphorus in eggshell. The result offers an alternative strategy for the laying hen with a worse eggshell problem.


1996 ◽  
Vol 270 (4) ◽  
pp. F677-F681 ◽  
Author(s):  
L. Liu ◽  
A. Khastgir ◽  
J. M. McCauley ◽  
S. T. Dunn ◽  
J. H. Morrissey ◽  
...  

The spatial relationship between vitamin D receptor (VDR) and calbindin D28k [calcium binding protein D28k (CaBP-D28k)] gene expression within the murine kidney was studied by localizing their mRNAs in discrete nephron structures using reverse transcription-polymerase chain reaction (RT-PCR). Primers for beta-actin mRNA were used as a control for the presence of tissue during RT-PCR for CaBP-D28k mRNA. mRNA for CaBP-D28k was found only in distal convoluted tubules (DCTs), connecting tubules (CNTs), and cortical collecting ducts (CCDs). In contrast, VDR mRNA was detected in glomeruli, S2 proximal convoluted tubules, cortical thick ascending limbs of Henle's loop, DCTs, CNTs, and initial CCDs. The presence of both VDR and CaBP-D28k mRNA in DCTs, CNTs, and CCDs is consistent with the hypothesis that cacitriol acts via the VDR to stimulate CaBP-D28k synthesis. Conversely, the presence of VDR mRNA in other parts of the nephron suggests that calcitriol has genomically mediated actions within the kidney in addition to stimulation of CaBP-D28k synthesis.


DNA ◽  
1988 ◽  
Vol 7 (9) ◽  
pp. 585-593 ◽  
Author(s):  
TERESA L. WOOD ◽  
YUTAKA KOBAYASHI ◽  
GRETCHEN FRANTZ ◽  
SAMUEL VARGHESE ◽  
SYLVIA CHRISTAKOS ◽  
...  

1977 ◽  
Vol 55 (3) ◽  
pp. 595-600 ◽  
Author(s):  
J. E. Harrison ◽  
A. J. W. Hitchman ◽  
G. B. Gordon ◽  
S. A. Hasany

The effect of vitamin D activity on the major renal Ca-binding protein has been compared with that on the intestinal Ca-binding protein. Using a method based on Ca-binding capacity, these proteins were measured in vitamin D deficient rats after vitamin D treatment for varying periods up to 5 days. Since P deficiency has been shown to stimulate synthesis of the active metabolite 1,25-dihydroxycholecalciferol, a similar experiment was done on rats fed a P-deficient diet for periods up to 21 days. The renal Ca-binding protein was unchanged by vitamin D treatment to vitamin D deficient rats and was only slightly increased (50%) by phosphate deficiency. By comparison, the intestinal protein was increased twofold by vitamin D treatment and fivefold by phosphate deficiency. Results indicate that vitamin D activity has no direct effect on the major renal Ca-binding protein.


1979 ◽  
Vol 57 (3) ◽  
pp. 257-263 ◽  
Author(s):  
Jennifer J. Pointon ◽  
M. J. O. Francis ◽  
R. Smith

1. Weanling rabbits were made rachitic either by a vitamin D-deficient diet or by parenteral administration of ethane 1-hydroxy-1,1-diphosphonate (EHDP) in amounts sufficient in other species to block the formation of 1,25-dihydroxycholecalciferol [1,25-(OH)2D,]. 2. The uptake of calcium into the isolated sarcoplasmic reticulum from mixed striated quadriceps muscle, and the amount of troponin C (the calcium-binding component of the troponin complex) in relation to other proteins from the same muscle, were measured. 3. In muscle from animals made rachitic by a dietary deficiency of vitamin D, the rate of uptake of calcium by the sarcoplasmic reticulum and the troponin C concentration were both significantly less (P < 0·02) than in control littermates. In EHDP-treated animals no significant differences from controls were found. 4. These results show that dietary deficiency of vitamin D in such animals can affect muscle physiology. Since no changes are found in animals made rachitic with EHDP, who presumably have a selective deficiency of 1,25-(OH)2D3, it is possible that the effect of vitamin D on muscle is mediated through metabolites other than 1,25-(OH)2D3 such as 25-hydroxycholecalciferol.


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