Skeletal muscle protein loss due to D-penicillamine results from reduced protein synthesis

Preedy, Victor R.; Wassif, Wassif S.; Baldwin, Dianne; Jones, Jim R.; Falkous, Gavin; Marway, Jaspaul S.; Mantle, David; Scott, David

doi:10.1016/s1357-2725(01)00062-0

Cited by 12 publications

(2 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Both defects might result from alterations of titin elasticity or the assembly of the elastic sarcomere matrix of the cardiomyocytes. Because the Cu 2+ content in muscle tissue is about 1.7 μg/g wet weight43, 44 and eight times higher by dry weight,43 its molar concentration is about 38 μ M (based on a water content of 70% of the wet tissue45), 5% of which is in free states 45. Thus a Cu 2+ avidity in the low micromolar range may manifest itself in muscle tissues.…”

Section: Discussionmentioning

confidence: 99%

Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI‐MS, CD, and NMR

Wang

2003

Biopolymers

View full text Add to dashboard Cite

Titin, a family of giant elastic proteins, constitutes an elastic sarcomere matrix in striated muscle. In the I-band region of the sarcomere, the titin PEVK segment acts as a molecular spring to generate elasticity as well as sites of adhesion with parallel thin filaments. Previously, we reported that PEVK consists of tandem repeats of 28 residue modules and that the "polyproline II-coil" motif is the fundamental conformational motif of the PEVK module. In order to characterize the factors that may affect and alter the PPII-coil conformational motifs, we have initiated a systematic study of the interaction with divalent cations (Cu2+, Ca2+, Zn2+, and Ni2+) and a conformational profile of PEVK peptides (a representative 28-mer peptide PR: PEPPKEVVPEKKAPVAPPKKPEVPPVKV and its subfragments PR1: kvPEPPKEVVPE, PR2: VPEKKAPVAPPK, PR3: KPEVPPVKV). UV-Vis absorption difference spectra and CD spectra showed that Cu2+ bound to PR1 with high affinity (20 microM), while its binding to PR2 and PR3 as well as the binding of other cations to all four peptides were of lower affinity (>100 microM). Conformational studies by CD revealed that Cu2+ binding to PR1 resulted in a polyproline II to turn transition up to a 1:2 PR1/Cu2+ ratio and a coil to turn transition at higher Cu2+ concentration. ESI-MS provided the stoichiometry of PEVK peptide-Cu2+ complexes at both low and high ion strength, confirming the specific high affinity binding of Cu2+ to PR1 and PR. Furthermore, NMR and ESI-MS/MS fragmentation analysis elucidated the binding sites of the PEVK peptide-Cu2+ complexes at (-2)KVPE2, 8VPE10, 13APV15, and 22EVP24. A potential application of Cu2+ binding in peptide sequencing by mass spectrometry was also revealed. We conclude that Cu2+ binds and bends PEVK peptides to a beta-turn-like structure at specific sites. The specific targeting of Cu2+ towards PPII is likely to be of significant value in elucidating the roles of PPII in titin elasticity as well as in interactions of proline-rich proteins.

show abstract

Section: Discussionmentioning

confidence: 99%

Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI‐MS, CD, and NMR

Wang

2003

Biopolymers

View full text Add to dashboard Cite

show abstract

“…Penicillamine (PA) is a strong chelating agent and it can react with the majority of heavy metal ions. Therefore, PA is the drug of choice in the treatment of hepatolenticular degeneration (Wilson’s disease) and is also effective for the treatment of several disorders including rheumatoid arthritis, primary biliary cirrhosis, scleroderma, fibrotic lung diseases, cystinuria, heavy element poisoning and progressive systemic sclerosis 35–37. Electrochemical methods have different advantages and are suitable for determination of PA 38.…”

Section: Introductionmentioning

confidence: 99%

Selective and Simultaneous Voltammetric Determination of Glutathione, Uric Acid and Penicillamine by a Modified Carbon Nanotube Paste Electrode

2013

View full text Add to dashboard Cite

In this paper, the use of a carbon paste electrode (CPE) modified by (E)‐3‐((2‐(2,4‐dinitrophenyl)hydrazono)methyl)benzene‐1,2‐diol (DHB) and carbon nanotubes (CNTs) for the determination of glutathione (GSH), uric acid (UA) and penicillamine (PA) is described. Initially, cyclic voltammetry was used to investigate the redox properties of the modified electrode in phosphate buffer. Next, the electrocatalytic oxidation of GSH via EC′ mechanism at the modified electrode was described. At the optimum pH of 7.0, the oxidation of GSH occurs at a potential that is 530 mV less positive than that of an unmodified carbon paste electrode. The values of the diffusion coefficient (D=2.5×10−6 cm2 s−1) and the catalytic rate constant (k=1.7×103 M−1 s−1) were calculated for GSH, using chronoamperometry. Based on differential pulse voltammetry, the oxidation of GSH exhibited a dynamic range between 0.4 and 700.0 µM and a detection limit (3σ) of 70.0 nM. Also, simultaneous determination of GSH, UA and PA was described at the modified electrode. Finally, this method was used for the determination of these substances in synthetic solutions and blood serum samples.

show abstract

Electrochemical Analysis of D‐Penicillamine Using a Carbon Paste Electrode Modified with Ferrocene Carboxylic Acid

Raoof¹,

Ojani²,

Chekin³

2007

Electroanalysis

View full text Add to dashboard Cite

The electrochemical behavior of d-penicillamine (d-PA) studied at the surface of ferrocene carboxylic acid modified carbon paste electrode (FCAMCPE) in aqueous media using cyclic voltammetry and double step potential chronoamperometry. It has been found that under optimum condition (pH 7.00), the oxidation of d-PA at surface of such an electrode is occurred about 420 mV less positive than that an unmodified carbon paste electrode (CPE). The catalytic oxidation peak current was linearly dependent on the d-PA concentration and a linear calibration curve was obtained in the ranges 7.5 Â 10 À5 M -1.0 Â 10 À3 M and 6.5 Â 10 À6 M À 1.0 Â 10 À4 M of d-PA with cyclic voltammetry (CV) and differential pulse voltammetry (DPV) methods respectively. The detection limits (3s) were determined as 6.04 Â 10 À5 M and 6.15 Â 10 À6 M. This method was also used for the determination of d-PA in pharmaceutical preparation (capsules) by standard addition method.

show abstract

Skeletal muscle protein loss due to D-penicillamine results from reduced protein synthesis

Cited by 12 publications

References 40 publications

Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI‐MS, CD, and NMR

Binding of copper(II) ions to the polyproline II helices of PEVK modules of the giant elastic protein titin as revealed by ESI‐MS, CD, and NMR

Selective and Simultaneous Voltammetric Determination of Glutathione, Uric Acid and Penicillamine by a Modified Carbon Nanotube Paste Electrode

Electrochemical Analysis of D‐Penicillamine Using a Carbon Paste Electrode Modified with Ferrocene Carboxylic Acid

Contact Info

Product

Resources

About