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Biomolecules 2018, 8(3), 79; https://doi.org/10.3390/biom8030079

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme

Laboratory of Biochemistry, Department of Pathology, University of Pisa, via Roma 55, 56126 Pisa, Italy
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Received: 19 July 2018 / Revised: 13 August 2018 / Accepted: 20 August 2018 / Published: 23 August 2018
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Abstract

Multiple muscle-specific isoforms of the Zn2+ metalloenzyme AMP deaminase (AMPD) have been identified based on their biochemical and genetic differences. Our previous observations suggested that the metal binding protein histidine-proline-rich glycoprotein (HPRG) participates in the assembly and maintenance of skeletal muscle AMP deaminase (AMPD1) by acting as a zinc chaperone. The evidence of a role of millimolar-strength phosphate in stabilizing the AMPD-HPRG complex of both AMPD1 and cardiac AMP deaminase (AMPD3) is suggestive of a physiological mutual dependence between the two subunit components with regard to the stability of the two isoforms of striated muscle AMPD. The observed influence of the HPRG content on the catalytic behavior of the two enzymes further strengthens this hypothesis. Based on the preferential localization of HPRG at the sarcomeric I-band and on the presence of a Zn2+ binding motif in the N-terminal regions of fast TnT and of the AMPD1 catalytic subunit, we advance the hypothesis that the Zn binding properties of HPRG could promote the association of AMPD1 to the thin filament. View Full-Text
Keywords: AMP deaminase (AMPD); histidine-proline-rich glycoprotein (HPRG); striated muscle; Troponin T (TnT) AMP deaminase (AMPD); histidine-proline-rich glycoprotein (HPRG); striated muscle; Troponin T (TnT)
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Ronca, F.; Raggi, A. Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme. Biomolecules 2018, 8, 79.

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