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Non-specific peroxidase activity and catalase-inhibitory behavior of fibrillar aggregates after interaction with heme: relevance to the etiology of amyloid-related neurodegenerative disorders using the experimental-based evidences

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Abstract

The exact mechanism of cell death in neurodegenerative diseases remains obscure, but the aberrant assembly of proteins into fibrillar aggregates is accused to be the primary cause of pathogenesis. Furthermore, the structural determinants of protein fibrils that are responsible for cell dysfunction are not yet clear. In the present study, using α-crystallin-/α-chymotrypsin-based experimental systems, we reported non-specific peroxidase behavior of “heme–amyloid fibril” complex using DNA, serotonin and DOPA as potential substrates. Also, amyloid-mediated inhibition of catalase activity was documented. More importantly, we suggested that uncontrollable peroxidase activity may be involved in neurodegenerative cell toxicity via several independent (mechanistic) routes. According to the results and literature, it is reasonable to assume that oxidative stress plays at least partially a causative rather than merely bystander role in the neurofibrillary pathology in AD/PD in vivo. Since the consequence of heme–amyloid interaction has yet to be identified, additional in vitro/in vivo data on it may help us to manage amyloid aggregation processes and postpone/attenuate the onset/extent of irreversible part of neurodegenerative pathogenesis.

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Abbreviations

CR:

Congo red

GdnHCl:

Guanidine hydrochloride

ThT:

Thioflavin T

BSA:

Bovine serum albumin

TMB:

3,3′,5,5′-Tetramethylbenzidine

DMSO:

Dimethyl sulphoxide

TFE:

2,2,2-Trifluoroethanol

AD:

Alzheimer’s disease

PD:

Parkinson’s disease

PCDs:

Protein conformational diseases

ROS:

Reactive oxygen species

DOPA:

3,4-Dihydroxyphenylalanine

Aβ:

Amyloid beta

MBTH:

3-Methyl-2-benzothiazolinone hydrazone

PMSF:

Phenylmethylsulfonyl fluoride

HO-1:

Heme oxygenase-1

LB:

Lewy body

8-oxo-dG:

7,8-Dihydro-8-oxo-2′-deoxyguanosine

HEC:

Human erythrocyte catalase

4-HO-8-oxo-dG:

4,8-Dihydro-4-hydroxy-8-oxo-2′-deoxyguanosine

HRP:

Horseradish peroxidase

PCR:

Polymerase chain reaction

SDS:

Sodium dodecyl sulfate

CNS:

Central nervous system

TEM:

Transmission electron microscopy

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Acknowledgments

The authors thank the Research Council of Kermanshah University of Medical Sciences for financial support of this investigation. The sponsor, however, had any direct involvement with this work. Also, we are deeply indebted to Dr. M. Ghadermarzi (Medical University of Kordestan) for a generous gift of the catalase, Mr. Hadi Mozafari, Mr. Reza Yarani (Medical Biology Research Center, Kermanshah, Iran) and Dr. M. Amani for their invaluable assistances in preparation of the DNA sample and final revision of the manuscript.

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Authors and Affiliations

  1. Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran

    Reza Khodarahmi, Zahra Hossein-pour, Kamran Mansouri, Ali Mostafaie, Khirollah Yari & Seyyed Abolghasem Ghadami

  2. Department of Pharmacognosy and Biotechnology, Faculty of Pharmaceutical Sciences, Kermanshah University of Medical Sciences, Kermanshah, Iran

    Reza Khodarahmi

  3. Department of Biology, Faculty of Sciences, Razi University, Kermanshah, Iran

    Sirous Ghobadi & Seyyed Abolghasem Ghadami

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  1. Reza Khodarahmi
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  2. Zahra Hossein-pour
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  7. Seyyed Abolghasem Ghadami
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Correspondence to Reza Khodarahmi.

Additional information

This work was performed in partial fulfillment of the requirements for MSc of Z. Hossein-pour, in Kermanshah University of Medical Sciences and Razi University, Kermanshah, Iran.

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Khodarahmi, R., Hossein-pour, Z., Ghobadi, S. et al. Non-specific peroxidase activity and catalase-inhibitory behavior of fibrillar aggregates after interaction with heme: relevance to the etiology of amyloid-related neurodegenerative disorders using the experimental-based evidences. J IRAN CHEM SOC 9, 939–950 (2012). https://doi.org/10.1007/s13738-012-0111-6

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