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The Management of Treatment-Resistant Depression
Published in Dr. Ather Muneer, Mood Disorders, 2018
Dysregulation of the HPA axis and failure of negative feedback loops has been noted in TRD. The findings in this regard are: Loss of diurnal variation of cortisol.Excessive blood cortisol levels in the evening.Flattening of the cortisol curve with persistent hypercortisolemia.Insensitivity of the glucocorticoid receptor (GR).Increased activity of the GR chaperone protein, FKBP5.
Hyperthermic Intraperitoneal Chemotherapy (HIPEC) for Peritoneal Malignancies
Published in II-Jin Kim, Cancer Genetics and Genomics for Personalized Medicine, 2017
G.E. Bates, P. Kim, C.M. DeRosa, L. Petrukhin, Y. Bressler, R.N. Taub
It was under hyperthermic conditions that heat shock proteins (HSPs) were discovered; their expression results from exposure to high temperatures in the cellular environment (Aispe, 2004). These proteins, which also respond to other cellular stressors (such as nutrition deprivation), prevent denaturation of intracellular proteins. Commonly referred to as molecular chaperone proteins, HSPs may augment tumorigenesis by allowing neoplastic cells to survive hostile environments. First discovered as a physical and chemical stressor, these highly conserved proteins are upregulated during times of cellular stress and promote various chaperoning properties which serve either a protective function or as a stimulus to the immune system (Goetz, 2003; Aispe, 2004).
Mycobacterium tuberculosis – The Organism
Published in Peter D O Davies, Stephen B Gordon, Geraint Davies, Clinical Tuberculosis, 2014
Mycobacterial antigens are divisible into those shared by all species and to some extent by related genera, those restricted to slowly growing species, those only present in rapidly growing species and shared with nocardiae and those unique to each species [64]. Antigens shared by all species include the so-called chaperone proteins, or chaperonins, especially a class known as heat-shock proteins (HSPs). These have a high amino-acid sequence homology with HSPs in mammalian cells and thus, by cross-reactivity, may induce various autoimmune phenomena seen in mycobacterial disease [65].
Passive heat stress induces mitochondrial adaptations in skeletal muscle
Published in International Journal of Hyperthermia, 2023
Erik D. Marchant, W. Bradley Nelson, Robert D. Hyldahl, Jayson R. Gifford, Chad R. Hancock
The molecular mechanisms by which heat stress causes improvements in mitochondrial content and function is an active area of research. Heat shock proteins (HSPs) are a family of molecular chaperones (chaperone proteins assist in protein folding and are critically important for normal protein function) which are highly conserved across tissues and organisms [70,71]. Heat shock proteins appear to be central to mitochondrial adaptations that occur following heat stress, with HSP72 being especially important. HSP72 protein expression has been shown to be consistently upregulated in skeletal muscle following heat exposure in cell culture [20], animals [22,24,72,73], and humans [23,67,68], and is associated with increases in mitochondrial content and function [20,22,23,74]. Furthermore, the transgenic overexpression of HSP72 in mouse skeletal muscle results in mitochondrial biogenesis [75,76].
Mutations of DNAJC7 are rare in Chinese amyotrophic lateral sclerosis patients
Published in Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, 2021
Xiaohan Sun, Ximeng Zhao, Qing Liu, Kang Zhang, Shuangwu Liu, Zhili Wang, Xunzhe Yang, Liang Shang, Liying Cui, Xue Zhang
DNAJC7 is a highly conserved gene, which encodes a member of DNAJ heat shock protein 40 family of protein. This protein is characterized by two N-terminal tetratricopeptide repeat domains and a C-terminal DNAJ domain. It acts as a co-chaperone, which binds the chaperone proteins heat shock protein 70 and 90 in an ATP-dependent manner and facilitates protein maintenance and quality control, such as folding of newly synthesized polypeptides and clearance of degraded proteins (8). Recently, a large ALS exome case–control study revealed that DNAJC7 was a novel gene for ALS (5). In their study, they identified 6 distinct protein-truncating variants and 4 rare missense damaging variants. No loss-of-function variants were identified in our study. This distinct genetic architecture between Caucasians and Chinese populations could be explained by different ethnic background (2), and should be considered in clinical application.
Proteomic study of skeletal muscle in obesity and type 2 diabetes: progress and potential
Published in Expert Review of Proteomics, 2018
In a study from 2010, Hwang et al. investigated the proteome in skeletal muscle biopsies from patients with T2D and lean and obese non-diabetic individuals. Muscle lysate proteins were separated using one-dimensional gel electrophoresis (1-DE), with protein assignment using HPLC-electrospray ionization (ESI)-MS/MS and label-free quantification based on the normalized spectral abundance factor (NSAF) method [62]. In total, 1218 proteins were assigned in at least one of the 24 participants. Of these, 92 proteins were increased or decreased by 2-fold in at least one of the two insulin-resistant groups (obesity or T2D) versus lean controls, and 15 of these proteins were significantly (p < 0.05) changed. The study demonstrated an increased abundance of chaperone proteins (HSP90 and T complex 1 isoforms) and proteins involved in proteasomal degradation (Cullin 5 and proteasomal subunits). This is consistent with the findings from in our initial proteomic characterization of the skeletal muscle proteome in individuals with T2D [58]. Importantly, Hwang et al. [62] also identified a decreased abundance of several mitochondrial proteins (UQCRCQ, COX6C, and CHCHD3), which is consistent with several previous studies that have reported abnormalities in mitochondrial oxidative metabolism, also termed mitochondrial dysfunction, in skeletal muscle in obesity and T2D [13–15,62,82–86].