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Transport of Calcium

Ilka Nemere, Anthony W. Norman

10.1002/cphy.cp060413

Source: Supplement 19: Handbook of Physiology, The Gastrointestinal System, Intestinal Absorption and Secretion

Originally published: 1991

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Historical Background
1.1 Calcium Absorption
1.2 Vitamin D
1.3 Evolution in Methodology
2 Factors That Influence Calcium Absorption
2.1 Intestinal Segment and Diet
2.2 Age
2.3 Hormonal Influences
3 Calbindin D
3.1 Characteristics of Calcium‐Binding Proteins
3.2 Classes of “Tight” Calcium‐Binding Proteins
3.3 Structure of Calbindins
3.4 Calbindin D9K
3.5 Calbindin D28K
3.6 Tissue and Subcellular Distribution of Calbindins
3.7 Calbindin D Molecular Biology
3.8 Biological Functions of Calbindins D
4 Mechanisms
4.1 Brush‐Border Membranes
4.2 Basal Lateral Membranes
4.3 Intracellular Organelles
Figure 1. Figure 1.

Photobiological production of the secosteroid vitamin D.
Figure 2. Figure 2.

Metabolism of vitamin D to the hormonally active secosteroid 1,25(OH)2D3.
Figure 3. Figure 3.

Dose‐response curve of bPTH(1–34) (bovine parathyroid hormone peptide containing the first 34 NH2‐terminal amino acids) action on calcium transport in vascularly perfused duodena of normal chicks. T/B, ratio of treated venous effluent to basal venous effluent.
Figure 4. Figure 4.

Calcium‐binding domains (“EF‐hand”). EF‐hand domains consist of only 30 amino acids, 10 of which are in an α‐helix, 10 of which are in loops surrounding and liganding to the calcium ion, followed by an additional 10 amino acids in a second length of α‐helix. EF‐hand domains are shown with the calcium coordinated by carboxyl atoms from residues 10, 12, 14, 18, and 21 and the peptide oxygen atom from residue 16. Residues 2, 5, 6, 9, 17, 22, 25, 26, and 29 are usually an amino acid residue with a hydrophobic side chain and are presumed to “face” the inside of the molecule.

[From Kretsinger 134.]
Figure 5. Figure 5.

A: amino acid sequence of calbindin D9K. Data shown are for rat intestinal protein. Also bovine intestinal calbindin D9K has been sequenced 240, as has rat placental calbindin D9K 147. B: primary amino acid sequence of chick intestinal calbindin D28K. [A, data from Desplan et al. 59; B, data from nucleotide sequence of cDNA by Hunziker 110.]
Figure 6. Figure 6.

A: steroid hormone receptor model of action of 1,25(OH)2D3 for induction of calbindins. B: correlations between 1,25(OH)2D3 nuclear uptake (top panel), receptor occupancy (middle panel), and calbindin D28K mRNA (bottom panel) in chick intestine after 1,25(OH)2D3 administration to vitamin D–deficient chicks. Vitamin D–deficient chicks were dosed intramuscularly with 6.5 nmol of 1,25(OH)2D3, total RNA was isolated, and calcium‐binding protein (CaBP) mRNA was measured by dot blot hybridization to a specific probe. Results are expressed as percent relative to the 12‐h peak. C: time course of the appearance of calbindin D28K in chick intestine after 1,25(OH)2D3 administration to vitamin D–deficient chicks. Vitamin D–deficient chicks were dosed intramuscularly with 6.5 nmol of 1,25(OH)2D3 and calbindin D28K levels were measured by enzyme‐linked immunosorbent assay (ELISA). [B and C adapted from Theofan et al. 254.]
Figure 7. Figure 7.

Biochemical identification of microsomes (A) and lysosomes (B) containing 45Ca, after calcium absorption in vivo. ER, endoplasmic reticulum; GA, Golgi membranes; BLM, basal lateral membranes.
Figure 8. Figure 8.

Schematic representation of subcellular phenomena that contribute to calcium transport.


Figure 1.

Photobiological production of the secosteroid vitamin D.



Figure 2.

Metabolism of vitamin D to the hormonally active secosteroid 1,25(OH)2D3.



Figure 3.

Dose‐response curve of bPTH(1–34) (bovine parathyroid hormone peptide containing the first 34 NH2‐terminal amino acids) action on calcium transport in vascularly perfused duodena of normal chicks. T/B, ratio of treated venous effluent to basal venous effluent.



Figure 4.

Calcium‐binding domains (“EF‐hand”). EF‐hand domains consist of only 30 amino acids, 10 of which are in an α‐helix, 10 of which are in loops surrounding and liganding to the calcium ion, followed by an additional 10 amino acids in a second length of α‐helix. EF‐hand domains are shown with the calcium coordinated by carboxyl atoms from residues 10, 12, 14, 18, and 21 and the peptide oxygen atom from residue 16. Residues 2, 5, 6, 9, 17, 22, 25, 26, and 29 are usually an amino acid residue with a hydrophobic side chain and are presumed to “face” the inside of the molecule.

[From Kretsinger 134.]


Figure 5.

A: amino acid sequence of calbindin D9K. Data shown are for rat intestinal protein. Also bovine intestinal calbindin D9K has been sequenced 240, as has rat placental calbindin D9K 147. B: primary amino acid sequence of chick intestinal calbindin D28K. [A, data from Desplan et al. 59; B, data from nucleotide sequence of cDNA by Hunziker 110.]



Figure 6.

A: steroid hormone receptor model of action of 1,25(OH)2D3 for induction of calbindins. B: correlations between 1,25(OH)2D3 nuclear uptake (top panel), receptor occupancy (middle panel), and calbindin D28K mRNA (bottom panel) in chick intestine after 1,25(OH)2D3 administration to vitamin D–deficient chicks. Vitamin D–deficient chicks were dosed intramuscularly with 6.5 nmol of 1,25(OH)2D3, total RNA was isolated, and calcium‐binding protein (CaBP) mRNA was measured by dot blot hybridization to a specific probe. Results are expressed as percent relative to the 12‐h peak. C: time course of the appearance of calbindin D28K in chick intestine after 1,25(OH)2D3 administration to vitamin D–deficient chicks. Vitamin D–deficient chicks were dosed intramuscularly with 6.5 nmol of 1,25(OH)2D3 and calbindin D28K levels were measured by enzyme‐linked immunosorbent assay (ELISA). [B and C adapted from Theofan et al. 254.]



Figure 7.

Biochemical identification of microsomes (A) and lysosomes (B) containing 45Ca, after calcium absorption in vivo. ER, endoplasmic reticulum; GA, Golgi membranes; BLM, basal lateral membranes.



Figure 8.

Schematic representation of subcellular phenomena that contribute to calcium transport.

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Article Title: Transport of Calcium
 

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Ilka Nemere, Anthony W. Norman. Transport of Calcium. Compr Physiol 2011, Supplement 19: Handbook of Physiology, The Gastrointestinal System, Intestinal Absorption and Secretion: 337-360. First published in print 1991. doi: 10.1002/cphy.cp060413