Topic:Ubiquitin
Ubiquitin is a small regulatory protein found in almost all tissues of horses, where it plays a role in protein degradation and cellular homeostasis. It tags damaged or misfolded proteins for degradation by the proteasome, a process essential for maintaining cellular function and responding to stress. Ubiquitin is involved in various cellular processes, including cell cycle regulation, DNA repair, and response to oxidative stress. Its function and regulation are critical in understanding equine cellular physiology and pathology. This page compiles peer-reviewed research studies and scholarly articles that explore the role, mechanisms, and implications of ubiquitin in equine biology.
Effects of Horse Meat Hydrolysate on Oxidative Stress, Proinflammatory Cytokines, and the Ubiquitin-Proteasomal System of C2C12 Cells. Sarcopenia, the age-related muscle atrophy, is a serious concern as it is associated with frailty, reduced physical functions, and increased mortality risk. Protein supplementation is essential for preserving muscle mass, and horse meat can be an excellent source of proteins. Since sarcopenia occurs under conditions of oxidative stress, this study aimed to investigate the potential anti-muscle atrophy effect of horse meat hydrolysate using C2C12 cells. A horse meat hydrolysate less than 3 kDa (A4<3kDa) significantly increased the viability of C2C12 myoblasts against HO-induced cytotoxicity....
Ion Channel and Ubiquitin Differential Expression during Erythromycin-Induced Anhidrosis in Foals. Macrolide drugs are the treatment of choice for infections, despite severe side-effects temporary anhidrosis as a. To better understand the molecular biology leading to macrolide induced anhidrosis, we performed skin biopsies and Quantitative Intradermal Terbutaline Sweat Tests (QITSTs) in six healthy pony-cross foals for three different timepoints during erythromycin administration-pre-treatment (baseline), during anhidrosis and post-recovery. RNA sequencing of biopsies followed by differential gene expression analysis compared both pre and post normal sweating timepoints to the erythromycin...
Morphological data indicate a stress response at the oral border of strangulated small intestine in horses. Strangulation colic often leads to surgery. We aimed to document the molecular response in the non-resected intestine in these horses using quantitative Western blot analysis, and immunohistochemistry. The expression of hypoxia-inducible factor 1-alpha (HIF1α) was investigated together with two molecular pathways initiated after protein destruction: proteasome degradation via ubiquitin chain formation and protein restoration via molecular chaperones such as inducible heat shock protein 70 (HSP70). In addition, the expression of c-fos and c-jun could indicate an early proinflammatory response....
Development of polyglucosan inclusions in skeletal muscle. Muscle samples from 24 horses with polysaccharide storage myopathy were stained with periodic acid-Schiff (PAS) stain and were immunostained for ubiquitin. Abnormalities detected with PAS stain were coarse granular cytoplasmic aggregates of amylase sensitive glycogen, subsarcolemmal aggregates of glycogen, central amylase sensitive bodies, and a variety of subsarcolemmal to intracytoplasmic amylase resistant polyglucosan inclusions. All amylase resistant inclusions were positive for ubiquitin. Ubiquitin was also detected in many amylase sensitive inclusions. Based on morphologic findings and p...
Budding of equine infectious anemia virus is insensitive to proteasome inhibitors. The only retrovirus protein required for the budding of virus-like particles is the Gag protein; however, recent studies of Rous sarcoma virus (RSV) and human immunodeficiency virus have suggested that modification of Gag with ubiquitin (Ub) is also required. As a consequence, the release of these viruses is reduced in the presence of proteasome inhibitors, which indirectly reduce the levels of free Ub within the cell. Here we show that the budding of equine infectious anemia virus (EIAV) from infected equine cells is largely unaffected by these drugs, although use of one inhibitor (MG-132) re...