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Parasite Induced Genetically Driven Autoimmune Chagas Heart Disease in the Chicken Model

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Published on: July 29, 2012

Calpain specificity and expression in chicken tissues.

Hsiao Lin Lee¹, Veronique Santé-Lhoutellier, Sophie Vigouroux

¹Laboratoire de Génie Chimique et Biochimique, Unité Biochimie - CUST - Université Blaise Pascal, 63174 Aubière, France.

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology

|November 14, 2006

Summary

Chicken and turkey calpains were compared to mammals. Chicken tissues revealed two calpains: mu-calpain and mu/m-calpain, with distinct calcium sensitivities and tissue distributions, suggesting unique roles in poultry.

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Area of Science:

Biochemistry
Molecular Biology
Comparative Genomics

Background:

Calpains are ubiquitous intracellular cysteine proteases crucial for various cellular processes.
Understanding calpain diversity and function across species, including avian models like chicken (Gallus gallus) and turkey (Meleagris gallopavo), is important for comparative biology.
Previous studies have identified multiple calpain isoforms in mammals, but their characterization in birds remains less explored.

Purpose of the Study:

To compare ubiquitous calpains in chicken, turkey, and mammals.
To investigate the tissue distribution of calpains in chicken.
To characterize the biochemical properties, specifically calcium sensitivity and electrophoretic mobility, of chicken calpains.

Main Methods:

Casein zymography was employed to determine calpain activity without prior sample purification, minimizing autolysis and denaturation.
Comparative analysis of calpain isoforms was performed between chicken, turkey, and mammalian species.
Tissue distribution of identified calpain isozymes in chicken was analyzed.

Main Results:

Two ubiquitous calpains were identified in chicken: a mu-calpain and a mu/m-calpain.
Chicken mu-calpain exhibited higher calcium sensitivity and lower electrophoretic mobility compared to its mammalian counterpart.
Chicken mu/m-calpain displayed intermediate calcium sensitivity and predominated in most tissues, unlike the varied distribution of mu-calpain, which was low in some tissues.

Conclusions:

Chicken possesses distinct ubiquitous calpain isoforms with unique biochemical properties and tissue expression patterns compared to mammals.
The prevalence of mu/m-calpain across chicken tissues suggests a potentially distinct or expanded functional role in avian physiology compared to its mammalian orthologs.
These findings contribute to the understanding of calpain evolution and functional diversification in vertebrates.