A peptide, parathymosin alpha, containing approximately equal to 105 amino acid residues, has been isolated from rat thymus, and the sequence of the first 30 residues at the NH2 terminus has been determined. In this region, it shows 43% structural identity with thymosin alpha 1 and prothymosin alpha. The common sequences do not include residues 2-9, which accounts for the poor reactivity of parathymosin alpha with an antibody directed against this epitope in thymosin alpha 1. Parathymosin alpha appears to modulate the action of prothymosin alpha in protecting sensitive strains of mice against opportunistic infection with Candida albicans.
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http://dx.doi.org/10.1073/pnas.82.4.1050 | DOI Listing |
Sci Rep
March 2021
Department of Animal Science, National Chung Hsing University, 145 Xingda Road, Taichung, 40227, Taiwan.
The adrenal gland responds to heat stress by epinephrine and glucocorticoid release to alleviate the adverse effects. This study investigated the effect of acute heat stress on the protein profile and histone modification in the adrenal gland of layer-type country chickens. A total of 192 roosters were subject to acute heat stress and thereafter classified into a resistant or susceptible group according to body temperature change.
View Article and Find Full Text PDFLife Sci Alliance
December 2020
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY, USA
This study reports that parathymosin (PTMS) is secreted by hypothalamic stem/progenitor cells (htNSC) to inhibit senescence of recipient cells such as fibroblasts. Upon release, PTMS is rapidly transferred into the nuclei of various cell types, including neuronal GT1-7 cells and different peripheral cells, and it is effectively transferred into neuronal nuclei in various brain regions in vivo. Notably, brain neurons also produce and release PTMS, and because neuronal populations are large, they are important for maintaining PTMS in the cerebrospinal fluid which is further transferable into the blood.
View Article and Find Full Text PDFMol Cell Biochem
June 2020
Division of Endodontics and Restorative Dentistry, Department of Oral Function, Kyushu Dental University, Fukuoka, 803-8580, Japan.
Pro-inflammatory cytokines prevent bone regeneration in vivo and activation of nuclear factor-κB (NF-κB) signaling has been proposed to lead to suppression of bone morphogenetic protein (BMP)-induced osteogenesis via direct binding of p65 to Smad4 in vitro. Application of a small nuclear acidic protein (MTI-II) and its delivered peptide, MPAID (MTI-II peptide anti-inflammatory drug) has been described to elicit therapeutic potential via strong anti-inflammatory action following the physical association of MTI-II and MPAID with p65. However, it is unclear whether MTI-II attenuates tumor necrosis factor (TNF)-α inhibition of BMP-induced osteogenesis.
View Article and Find Full Text PDFEndocrinology
December 2016
Departments of Clinical Proteomics and Molecular Medicine (K.Ok., K.Om., T.S., M.A., N.S., T.K.) and Disease Biomarker Analysis and Molecular Regulation (M.S.K.), St Marianna University Graduate School of Medicine, Kawasaki, Kanagawa 216-8511, Japan; Department of Biological Endodontics (S.H.-T.), Institute of Biomedical and Health Science, Hiroshima University, Hiroshima 734-8553, Japan; and Division of Endodontics and Restorative Dentistry (C.K.), Kyushu Dental University, Kitakyushu, Fukuoka 803-8580, Japan.
Nuclear factor-κB (NF-κB) is the most potent proinflammatory transactivator, and an inhibitor of NF-κB is a good antiinflammatory drug. Glucocorticoids (GCs) are the strongest and the most frequently used antiinflammatory drugs. GC-bound glucocorticoid receptor (GR) inhibits the transcriptional activity of NF-κB and thereby suppresses a broad range of inflammatory processes.
View Article and Find Full Text PDFVitam Horm
October 2017
Center for Proteomics and Systems Biology, Brown Foundation Institute of Molecular Medicine for the Prevention of Human Diseases, The University of Texas Health Science Center at Houston, Houston, TX, United States; Department of Nanomedicine and Biomedical Engineering, The University of Texas Health Science Center at Houston, Houston, TX, United States. Electronic address:
The thymosin proteins are all short, highly charged, intrinsically unstructured proteins under natural conditions. However, structure can be induced in many of the thymosin proteins by providing charge neutralization at low pH or by the addition of Zn(2+) ions, organic reagents such as trifluoroethanol, hexafluoropropanol, or n-dodecyltrimethylammonium bromide, or interactions with their natural binding partner proteins. The differing structures of thymosin alpha and thymosin beta proteins have been studied by circular dichroism, nuclear magnetic resonance, and crystallographic methods in order to better understand the role of these proteins.
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