Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine

D. R. Marshak; D. M. Watterson; L. J. Van Eldik

doi:10.1073/pnas.78.11.6793

Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine

D. R. Marshak, D. M. Watterson, L. J. Van Eldik

Pharmacology

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

100 Scopus citations

Abstract

We have purified the brain-specific S100b by affinity-based adsorption chromatography on phenothiazine-Sepharose conjugates and studied the interaction of this and other calcium-modulated proteins with the immobilized antipsychotic drug. Bovine brain calmodulin, rabbit skeletal muscle troponin C, and bovine brain S100b bind to phenothiazine-Sepharose in a calcium-dependent manner. These three proteins competitively inhibit the calcium-dependent binding of ¹²⁵I-labeled chicken gizzard calmodulin to the immobilized drug. However, carp parvalbumin and chicken intestinal vitamin D-dependent calcium binding protein do not inhibit the phenothiazine-calmodulin interaction. These results suggest that the known amino acid sequence homology among calmodulin, troponin C, and S100b may be reflected in a similar functional domain present in these proteins but absent in parvalbumin and vitamin D-dependent protein.

Original language	English (US)
Pages (from-to)	6793-6797
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	78
Issue number	11 II
DOIs	https://doi.org/10.1073/pnas.78.11.6793
State	Published - 1981

ASJC Scopus subject areas

General

Access to Document

10.1073/pnas.78.11.6793

Cite this

@article{a32e6c0c494142689715bbd28a90e681,

title = "Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine",

abstract = "We have purified the brain-specific S100b by affinity-based adsorption chromatography on phenothiazine-Sepharose conjugates and studied the interaction of this and other calcium-modulated proteins with the immobilized antipsychotic drug. Bovine brain calmodulin, rabbit skeletal muscle troponin C, and bovine brain S100b bind to phenothiazine-Sepharose in a calcium-dependent manner. These three proteins competitively inhibit the calcium-dependent binding of 125I-labeled chicken gizzard calmodulin to the immobilized drug. However, carp parvalbumin and chicken intestinal vitamin D-dependent calcium binding protein do not inhibit the phenothiazine-calmodulin interaction. These results suggest that the known amino acid sequence homology among calmodulin, troponin C, and S100b may be reflected in a similar functional domain present in these proteins but absent in parvalbumin and vitamin D-dependent protein.",

author = "Marshak, {D. R.} and Watterson, {D. M.} and {Van Eldik}, {L. J.}",

year = "1981",

doi = "10.1073/pnas.78.11.6793",

language = "English (US)",

volume = "78",

pages = "6793--6797",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "11 II",

}

TY - JOUR

T1 - Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine

AU - Marshak, D. R.

AU - Watterson, D. M.

AU - Van Eldik, L. J.

PY - 1981

Y1 - 1981

N2 - We have purified the brain-specific S100b by affinity-based adsorption chromatography on phenothiazine-Sepharose conjugates and studied the interaction of this and other calcium-modulated proteins with the immobilized antipsychotic drug. Bovine brain calmodulin, rabbit skeletal muscle troponin C, and bovine brain S100b bind to phenothiazine-Sepharose in a calcium-dependent manner. These three proteins competitively inhibit the calcium-dependent binding of 125I-labeled chicken gizzard calmodulin to the immobilized drug. However, carp parvalbumin and chicken intestinal vitamin D-dependent calcium binding protein do not inhibit the phenothiazine-calmodulin interaction. These results suggest that the known amino acid sequence homology among calmodulin, troponin C, and S100b may be reflected in a similar functional domain present in these proteins but absent in parvalbumin and vitamin D-dependent protein.

AB - We have purified the brain-specific S100b by affinity-based adsorption chromatography on phenothiazine-Sepharose conjugates and studied the interaction of this and other calcium-modulated proteins with the immobilized antipsychotic drug. Bovine brain calmodulin, rabbit skeletal muscle troponin C, and bovine brain S100b bind to phenothiazine-Sepharose in a calcium-dependent manner. These three proteins competitively inhibit the calcium-dependent binding of 125I-labeled chicken gizzard calmodulin to the immobilized drug. However, carp parvalbumin and chicken intestinal vitamin D-dependent calcium binding protein do not inhibit the phenothiazine-calmodulin interaction. These results suggest that the known amino acid sequence homology among calmodulin, troponin C, and S100b may be reflected in a similar functional domain present in these proteins but absent in parvalbumin and vitamin D-dependent protein.

UR - http://www.scopus.com/inward/record.url?scp=0242607702&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0242607702&partnerID=8YFLogxK

U2 - 10.1073/pnas.78.11.6793

DO - 10.1073/pnas.78.11.6793

M3 - Article

C2 - 6947252

AN - SCOPUS:0242607702

SN - 0027-8424

VL - 78

SP - 6793

EP - 6797

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 11 II

ER -

Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this