High capacity, low affinity Ca2+ binding of chromogranin A: Relationship between the pH-induced conformational change and Ca2+ binding property

Seung Hyun Yoo; Joseph P. Albanesi

High capacity, low affinity Ca²⁺ binding of chromogranin A: Relationship between the pH-induced conformational change and Ca²⁺ binding property

Research output: Contribution to journal › Article

Abstract

Chromogranin A, the major intravesicular protein of adrenal chromaffin granules, bound Ca²⁺ in a pH-dependent manner. Both the maximal binding and affinity of chromogranin A for Ca²⁺ were dependent on pH. Chromogranin A bound 670 nmol of Ca²⁺/mg (32 mol/ mol) and 1150 nmol of Ca²⁺/mg (55 mol/mol) at pH 7.5 and 5.5, respectively, with dissociation constants (Kd) of 2.7 and 4 mM. This pH dependence probably reflects different conformations of the protein at the two pH values. Conformational differences of chromogranin A at two different pH values were demonstrated by limited tryptic digestion patterns confirming previous results obtained by circular dichroism spectroscopy (Yoo, S. H., and Albanesi, J. P. (1990) J. Biol. Chem. 265, 14414-14421). Sedimentation equilibrium studies revealed the native molecular mass of chromogranin A to be 100 kDa at pH 7.5 ad 192 kDa at pH 5.5, indicating dimeric and tetrameric states of the protein at the two pH levels. We postulate that the pH- and Ca²⁺-induced conformational changes of chromogranin A may have a role both in the regulation of Ca²⁺ release of chromaffin granules and in the early stages of secretory vesicle biogenesis.

Original language	English (US)
Pages (from-to)	7740-7745
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	266
Issue number	12
State	Published - Apr 25 1991

Fingerprint

Chromogranin A

Chromaffin Granules

Circular dichroism spectroscopy

Proteins

Molecular mass

Sedimentation

Conformations

Protein Conformation

Secretory Vesicles

Circular Dichroism

Digestion

Spectrum Analysis

ASJC Scopus subject areas

Biochemistry

Cite this

Yoo, S. H., & Albanesi, J. P. (1991). High capacity, low affinity Ca²⁺ binding of chromogranin A: Relationship between the pH-induced conformational change and Ca²⁺ binding property. Journal of Biological Chemistry, 266(12), 7740-7745.

High capacity, low affinity Ca²⁺ binding of chromogranin A : Relationship between the pH-induced conformational change and Ca²⁺ binding property. / Yoo, Seung Hyun; Albanesi, Joseph P.

In: Journal of Biological Chemistry, Vol. 266, No. 12, 25.04.1991, p. 7740-7745.

Research output: Contribution to journal › Article

Yoo, SH & Albanesi, JP 1991, 'High capacity, low affinity Ca²⁺ binding of chromogranin A: Relationship between the pH-induced conformational change and Ca²⁺ binding property', Journal of Biological Chemistry, vol. 266, no. 12, pp. 7740-7745.

Yoo SH, Albanesi JP. High capacity, low affinity Ca²⁺ binding of chromogranin A: Relationship between the pH-induced conformational change and Ca²⁺ binding property. Journal of Biological Chemistry. 1991 Apr 25;266(12):7740-7745.

Yoo, Seung Hyun ; Albanesi, Joseph P. / High capacity, low affinity Ca²⁺ binding of chromogranin A : Relationship between the pH-induced conformational change and Ca²⁺ binding property. In: Journal of Biological Chemistry. 1991 ; Vol. 266, No. 12. pp. 7740-7745.

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abstract = "Chromogranin A, the major intravesicular protein of adrenal chromaffin granules, bound Ca2+ in a pH-dependent manner. Both the maximal binding and affinity of chromogranin A for Ca2+ were dependent on pH. Chromogranin A bound 670 nmol of Ca2+/mg (32 mol/ mol) and 1150 nmol of Ca2+/mg (55 mol/mol) at pH 7.5 and 5.5, respectively, with dissociation constants (Kd) of 2.7 and 4 mM. This pH dependence probably reflects different conformations of the protein at the two pH values. Conformational differences of chromogranin A at two different pH values were demonstrated by limited tryptic digestion patterns confirming previous results obtained by circular dichroism spectroscopy (Yoo, S. H., and Albanesi, J. P. (1990) J. Biol. Chem. 265, 14414-14421). Sedimentation equilibrium studies revealed the native molecular mass of chromogranin A to be 100 kDa at pH 7.5 ad 192 kDa at pH 5.5, indicating dimeric and tetrameric states of the protein at the two pH levels. We postulate that the pH- and Ca2+-induced conformational changes of chromogranin A may have a role both in the regulation of Ca2+ release of chromaffin granules and in the early stages of secretory vesicle biogenesis.",

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