Calmodulin and rat vitamin D-dependent calcium-binding proteins: Biochemical and immunochemical comparison

Sylvia Christakos; M. Elizabeth; H. Bruns; Aruna S. Mehra; William B. Rhoten; Linda J. Van Eldik

doi:10.1016/0003-9861(84)90360-6

Calmodulin and rat vitamin D-dependent calcium-binding proteins: Biochemical and immunochemical comparison

Sylvia Christakos, M. Elizabeth, H. Bruns, Aruna S. Mehra, William B. Rhoten, Linda J. Van Eldik

Research output: Contribution to journal › Article › peer-review

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Abstract

Purified vitamin D-dependent rat intestinal (M_r 10,000) and rat renal (M_r 28,000) calcium-binding proteins (CaBPs) have been compared to vertebrate calmodulin, and the vitamin D-dependent CaBPs have been found to be distinct from calmodulin by biochemical and immunochemical criteria. Rat renal and rat intestinal CaBPs do not stimulate 3′,5′-cyclic nucleotide phosphodiesterase, do not compete with iodinated calmodulin for binding to phenothiazine-Sepharose conjugates, do not cross-react immunochemically, and do not contain N^ε{lunate}-trimethyllysine. In addition, although calmodulin exhibits a characteristic calcium-dependent mobility shift on polyacrylamide gels in the presence of sodium dodecyl sulfate, a similar mobility shift is not observed for the vitamin D-dependent CaBPs. Immunocytochemically, calmodulin has a widespread localization in the kidney, whereas CaBP is present specifically in the distal tubules of the kidney. These localizations suggest a specialized role for CaBP in the kidney. Thus, although the vitamin D-dependent CaBPs and calmodulin are similar in that they are small, acidic, calcium-binding proteins, these two classes of proteins are biochemically and immunochemically distinct.

Original language	English
Pages (from-to)	38-47
Number of pages	10
Journal	Archives of Biochemistry and Biophysics
Volume	231
Issue number	1
DOIs	https://doi.org/10.1016/0003-9861(84)90360-6
State	Published - May 15 1984

Bibliographical note

Funding Information:
These studies were supported in part by National Science Foundation Grant PCM 8302912 (L.V.E.), National Science Foundation Grant PCM 8103421 (S.C.), and NIH Grants HD12335 (M.E.B.) and NS20270-01 (S.C.). S.C. is a recipient of a Research Career Development Award from the National Institute of Arthritis, Diabetes, Digestive, and Kidney Diseases (AM 01200-01).

Funding

These studies were supported in part by National Science Foundation Grant PCM 8302912 (L.V.E.), National Science Foundation Grant PCM 8103421 (S.C.), and NIH Grants HD12335 (M.E.B.) and NS20270-01 (S.C.). S.C. is a recipient of a Research Career Development Award from the National Institute of Arthritis, Diabetes, Digestive, and Kidney Diseases (AM 01200-01).

Funders	Funder number
National Institute of Arthritis, Diabetes, Digestive, and Kidney Diseases	AM 01200-01
U.S. Department of Energy Chinese Academy of Sciences Guangzhou Municipal Science and Technology Project Oak Ridge National Laboratory Extreme Science and Engineering Discovery Environment National Science Foundation National Energy Research Scientific Computing Center National Natural Science Foundation of China	PCM 8103421, PCM 8302912
U.S. Department of Energy Chinese Academy of Sciences Guangzhou Municipal Science and Technology Project Oak Ridge National Laboratory Extreme Science and Engineering Discovery Environment National Science Foundation National Energy Research Scientific Computing Center National Natural Science Foundation of China
National Institutes of Health (NIH)	NS20270-01
National Institutes of Health (NIH)
Eunice Kennedy Shriver National Institute of Child Health and Human Development	R01HD012335
Eunice Kennedy Shriver National Institute of Child Health and Human Development

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/0003-9861(84)90360-6

Cite this

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title = "Calmodulin and rat vitamin D-dependent calcium-binding proteins: Biochemical and immunochemical comparison",

abstract = "Purified vitamin D-dependent rat intestinal (Mr 10,000) and rat renal (Mr 28,000) calcium-binding proteins (CaBPs) have been compared to vertebrate calmodulin, and the vitamin D-dependent CaBPs have been found to be distinct from calmodulin by biochemical and immunochemical criteria. Rat renal and rat intestinal CaBPs do not stimulate 3′,5′-cyclic nucleotide phosphodiesterase, do not compete with iodinated calmodulin for binding to phenothiazine-Sepharose conjugates, do not cross-react immunochemically, and do not contain Nε\{lunate\}-trimethyllysine. In addition, although calmodulin exhibits a characteristic calcium-dependent mobility shift on polyacrylamide gels in the presence of sodium dodecyl sulfate, a similar mobility shift is not observed for the vitamin D-dependent CaBPs. Immunocytochemically, calmodulin has a widespread localization in the kidney, whereas CaBP is present specifically in the distal tubules of the kidney. These localizations suggest a specialized role for CaBP in the kidney. Thus, although the vitamin D-dependent CaBPs and calmodulin are similar in that they are small, acidic, calcium-binding proteins, these two classes of proteins are biochemically and immunochemically distinct.",

author = "Sylvia Christakos and M. Elizabeth and H. Bruns and Mehra, \{Aruna S.\} and Rhoten, \{William B.\} and \{Van Eldik\}, \{Linda J.\}",

note = "Funding Information: These studies were supported in part by National Science Foundation Grant PCM 8302912 (L.V.E.), National Science Foundation Grant PCM 8103421 (S.C.), and NIH Grants HD12335 (M.E.B.) and NS20270-01 (S.C.). S.C. is a recipient of a Research Career Development Award from the National Institute of Arthritis, Diabetes, Digestive, and Kidney Diseases (AM 01200-01).",

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AU - Rhoten, William B.

AU - Van Eldik, Linda J.

N1 - Funding Information: These studies were supported in part by National Science Foundation Grant PCM 8302912 (L.V.E.), National Science Foundation Grant PCM 8103421 (S.C.), and NIH Grants HD12335 (M.E.B.) and NS20270-01 (S.C.). S.C. is a recipient of a Research Career Development Award from the National Institute of Arthritis, Diabetes, Digestive, and Kidney Diseases (AM 01200-01).

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N2 - Purified vitamin D-dependent rat intestinal (Mr 10,000) and rat renal (Mr 28,000) calcium-binding proteins (CaBPs) have been compared to vertebrate calmodulin, and the vitamin D-dependent CaBPs have been found to be distinct from calmodulin by biochemical and immunochemical criteria. Rat renal and rat intestinal CaBPs do not stimulate 3′,5′-cyclic nucleotide phosphodiesterase, do not compete with iodinated calmodulin for binding to phenothiazine-Sepharose conjugates, do not cross-react immunochemically, and do not contain Nε{lunate}-trimethyllysine. In addition, although calmodulin exhibits a characteristic calcium-dependent mobility shift on polyacrylamide gels in the presence of sodium dodecyl sulfate, a similar mobility shift is not observed for the vitamin D-dependent CaBPs. Immunocytochemically, calmodulin has a widespread localization in the kidney, whereas CaBP is present specifically in the distal tubules of the kidney. These localizations suggest a specialized role for CaBP in the kidney. Thus, although the vitamin D-dependent CaBPs and calmodulin are similar in that they are small, acidic, calcium-binding proteins, these two classes of proteins are biochemically and immunochemically distinct.

AB - Purified vitamin D-dependent rat intestinal (Mr 10,000) and rat renal (Mr 28,000) calcium-binding proteins (CaBPs) have been compared to vertebrate calmodulin, and the vitamin D-dependent CaBPs have been found to be distinct from calmodulin by biochemical and immunochemical criteria. Rat renal and rat intestinal CaBPs do not stimulate 3′,5′-cyclic nucleotide phosphodiesterase, do not compete with iodinated calmodulin for binding to phenothiazine-Sepharose conjugates, do not cross-react immunochemically, and do not contain Nε{lunate}-trimethyllysine. In addition, although calmodulin exhibits a characteristic calcium-dependent mobility shift on polyacrylamide gels in the presence of sodium dodecyl sulfate, a similar mobility shift is not observed for the vitamin D-dependent CaBPs. Immunocytochemically, calmodulin has a widespread localization in the kidney, whereas CaBP is present specifically in the distal tubules of the kidney. These localizations suggest a specialized role for CaBP in the kidney. Thus, although the vitamin D-dependent CaBPs and calmodulin are similar in that they are small, acidic, calcium-binding proteins, these two classes of proteins are biochemically and immunochemically distinct.

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Calmodulin and rat vitamin D-dependent calcium-binding proteins: Biochemical and immunochemical comparison

Abstract

Bibliographical note

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