@article{WangKarnatiMadhusudhan2022,
  author    = {Wang, Hongjie and Karnati, Srikanth and Madhusudhan, Thati},
  title     = {Regulation of the homeostatic unfolded protein response in diabetic nephropathy},
  series = {Pharmaceuticals},
  volume    = {15},
  journal   = {Pharmaceuticals},
  number    = {4},
  issn      = {1424-8247},
  doi       = {10.3390/ph15040401},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-267143},
  year      = {2022},
  abstract  = {A growing body of scientific evidence indicates that protein homeostasis, also designated as proteostasis, is causatively linked to chronic diabetic nephropathy (DN). Experimental studies have demonstrated that the insulin signaling in podocytes maintain the homeostatic unfolded protein response (UPR). Insulin signaling via the insulin receptor non-canonically activates the spliced X-box binding protein-1 (sXBP1), a highly conserved endoplasmic reticulum (ER) transcription factor, which regulates the expression of genes that control proteostasis. Defective insulin signaling in mouse models of diabetes or the genetic disruption of the insulin signaling pathway in podocytes propagates hyperglycemia induced maladaptive UPR and DN. Insulin resistance in podocytes specifically promotes activating transcription factor 6 (ATF6) dependent pathogenic UPR. Akin to insulin, recent studies have identified that the cytoprotective effect of anticoagulant serine protease-activated protein C (aPC) in DN is mediated by sXBP1. In mouse models of DN, treatment with chemical chaperones that improve protein folding provides an additional benefit on top of currently used ACE inhibitors. Understanding the molecular mechanisms that transmute renal cell specific adaptive responses and that deteriorate renal function in diabetes will enable researchers to develop new therapeutic regimens for DN. Within this review, we focus on the current understanding of homeostatic mechanisms by which UPR is regulated in DN.},
  language  = {en}
}
@article{MuenchHsinFerberetal.2016,
  author    = {M{\"u}nch, Miriam and Hsin, Chih-Hsuan and Ferber, Elena and Berger, Susanne and M{\"u}ller, Martin J.},
  title     = {Reactive electrophilic oxylipins trigger a heat stress-like response through HSFA1 transcription factors},
  series = {Journal of Experimental Botany},
  volume    = {67},
  journal   = {Journal of Experimental Botany},
  number    = {21},
  doi       = {10.1093/jxb/erw376},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-186766},
  pages     = {6139-6148},
  year      = {2016},
  abstract  = {Electrophilic oxylipins trigger a heat-shock-like response in the absence of heat through the canonical heat-shock transcription factor A1, thereby helping to cope with stresses associated with protein damage.Abiotic and biotic stresses are often characterized by an induction of reactive electrophile species (RES) such as the jasmonate 12-oxo-phytodienoic acid (OPDA) or the structurally related phytoprostanes. Previously, RES oxylipins have been shown massively to induce heat-shock-response (HSR) genes including HSP101 chaperones. Moreover, jasmonates have been reported to play a role in basal thermotolerance. We show that representative HSR marker genes are strongly induced by RES oxylipins through the four master regulator transcription factors HSFA1a, b, d, and e essential for short-term adaptation to heat stress in Arabidopsis. When compared with Arabidopsis seedlings treated at the optimal acclimation temperature of 37 A degrees C, the exogenous application of RES oxylipins at 20 A degrees C induced a much weaker induction of HSP101 at both the gene and protein expression levels which, however, was not sufficient to confer short-term acquired thermotolerance. Moreover, jasmonate-deficient mutant lines displayed a wild-type-like HSR and were not compromised in acquiring thermotolerance. Hence, the OPDA- and RES oxylipin-induced HSR is not sufficient to protect seedlings from severe heat stress but may help plants to cope better with stresses associated with protein unfolding by inducing a battery of chaperones in the absence of heat.},
  language  = {en}
}