Proteomic profiling of the HSPB chaperonome: Mass spectrometric identification of small heat shock proteins in stressed skeletal muscles

Abstract

e continuing maintenance of protein homeostasis and the protection of proteomic integrity is essential for the survival of complex cellular systems under stressful conditions. Proteostasis is maintained by a complex system of protective pathways that involve several classes of molecular chaperones, now referred to as the chaperonome. e elaborate interplay of these components averts detrimental protein aggregation and supports proteins in resuming their functional fold. In skeletal muscle tissues, molecular chaperones protect contractile functions throughout bre adaptations to changed physiological demands and prevent tissue damage during acute phases of protein misfolding or prolonged periods of harmful protein accumulation. is results in considerable changes in the expression pro le of individual members of the large family of heat shock proteins. Systematic proteomic surveys of skeletal muscle tissues have revealed that the concentration of small heat shock proteins is especially a ected following strenuous exercise, in various neuromuscular disorders and during the natural aging process. Of the 10 identi ed members of the small heat shock protein HSPB family, HSPB1 (Hsp25), HSPB2 (MKBP), HSPB3 (Hsp27), HSPB4 (αA-crystallin), HSPB5 (αB-crystallin), HSPB6 (Hsp20), HSPB7 (cardiovascular cvHsp) and HSPB8 (Hsp22) are clearly present in skeletal muscle tissues. is review outlines the proteomic identi cation of small heat shock proteins and their muscle-speci c expression and induction patterns in health and disease. Since HSPB molecules are of relatively low molecular mass, belong to the markedly soluble type of proteins and represent critical pro-survival proteins that are intrinsically involved in the prevention of stress-induced bre damage, they present ideal muscle-associated biomarker candidates for the establishment of superior diagnostic and therapy-monitoring approaches to assess stress-related skeletal muscle degeneration.

Significant genomic introgression from grey junglefowl (Gallus sonneratii) to domestic chickens (Gallus gallus domesticus)

“…Additionally, we also identified two members of the small heat shock protein family, including CRYAB and HSPB2 , which have been introgressed in many domestic chickens. They play crucial roles in cellular defense mechanisms when organisms are exposed to high-temperature environments [ 42 ] and may be involved in the high-altitude adaptation of animals [ 43 , 44 ]. These two genes are located within the significantly introgressed region on chromosome 24, downstream of BCO2 , spanning from 0.07 Mb to 0.08 Mb.…”