Characterization of a specific, high affinity binding macromolecule for 1 alpha, 25-dihydroxyvitamin D3 in cultured chick kidney cells

Simpson, R.U.; Franceschi, R.T.; DeLuca, H.F.

doi:10.1016/s0021-9258(19)70442-6

Cited by 50Vitamin D Research StudiesParathyroid Disorders and TreatmentsProtein Interaction Studies and Fluorescence Analysis

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Characterization of a specific, high affinity binding macromolecule for 1 alpha, 25-dihydroxyvitamin D3 in cultured chick kidney cells

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Simpson, R.U., Franceschi, R.T., DeLuca, H.F.·1980·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(19)70442-6

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Abstract

Cytosol prepared from vitamin D3-deficient kidney cells in culture contains a 3.7 S protein that specifically binds 1,25-dihydroxyvitamin D3 with high affinity and low capacity. Whole kidney homogenate cytosol preparations are shown to possess two 1,25-dihydroxyvitamin D3 binding macromolecules. One of the binding proteins sediments at 3.5 to 3.7 S while the second sediments at 6.0 S. The 6.0 S component has a greater affinity for 25-dihydroxyvitamin D3 than for 1,25-dihydroxyvitamin D3. Cultured cell cytosol was found to have little 6.0 S 25-hydroxyvitamin D3 binding protein. Scatchard analysis of the cultured cell cytosol reveals an equilibrium binding constant (KD) of 5.6 x 10 (-11) with 57 fmol of sites/mg of protein. The receptor-like protein has a Mr = 72,000 and as with other steroid receptors it aggregates in the presence of low potassium concentrations. Analog competition for receptor binding reveals the following potency order: 1,25-dihydroxyvitamin D3 > 25-hydroxyvitamin D3 > 1 alpha-hydroxyvitamin D3 > 24(R),25-dihydroxyvitamin D3; the receptor had no detectable affinity for vitamin D3. The kidney cells respond to 1,25-dihydroxyvitamin D3 by diminishing 25-hydroxyvitamin D3 1 alpha-hydroxylation and increasing 24R-hydroxylation. Cultured cells provide a preparation of cytosol which has allowed extensive characterization of the renal 1,25-dihydroxyvitamin D3 receptor and should facilitate investigations into the role this receptor plays in renal control of vitamin D3 metabolism.

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The active form of vitamin D binds to a highly specific nuclear receptor in muscle tissue and leads to protein synthesis and growth of muscle tissue.
“the active form of vitamin D binds to a highly specific nuclear receptor in the muscle tissue [64,68] and leads to protein synthesis and growth of muscle tissue [64].”
From Novel Insights on Intake of Fish and Prevention of Sarcopenia: All Reasons for an Adequate Consumption (2020) · cites this paper as [68]

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Background
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Simpson, R. U., & DeLuca, H. F. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.10.5822 · Cited by 115
A specific 1,25-dihydroxyvitamin D3 binding macromolecule in chicken bone.
Mellon, W. S., & Deluca, H. F. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85636-3 · Cited by 43

Authors: Simpson, R. U., Franceschi, R. T., & DeLuca, H. F.
Affiliations: University of Wisconsin–Madison (US)
ORCID: Simpson, R.U.
Franceschi, R.T.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1980-11
Volume: 255
Issue: 21
Pages: 10160-10166
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(19)70442-6
OpenAlex: W1509999489
Cited by: 50
References: 32
Citations by year: 2020: 1 · 2018: 2 · 2017: 1
FWCI: 6.62
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 14582 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Vitamin D Research Studies
Health Sciences › Medicine › Nephrology › Parathyroid Disorders and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords: 1,25-dihydroxyvitamin D3, vitamin D receptor, 25-hydroxyvitamin D3, 1α-hydroxyvitamin D3, chick kidney cells, receptor binding affinity
MeSH terms: Animals, Binding, Competitive, Cells, Cultured, Chickens, Cytosol, Kidney, Kinetics, Molecular Weight, Receptors, Steroid, Vitamin D Deficiency, Receptors, Calcitriol

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Characterization of a specific, high affinity binding macromolecule for 1 alpha, 25-dihydroxyvitamin D3 in cultured chick kidney cells

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