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Osteocrin ameliorates adriamycin nephropathy via p38 mitogen-activated protein kinase inhibition.
Sci Rep
November 2021
Department of Nephrology, Graduate School of Medicine, Kyoto University, 54 Shogoin Kawahara-cho, Sakyo-ku, Kyoto, Kyoto, 6068507, Japan.
Natriuretic peptides exert multiple effects by binding to natriuretic peptide receptors (NPRs). Osteocrin (OSTN) binds with high affinity to NPR-C, a clearance receptor for natriuretic peptides, and inhibits degradation of natriuretic peptides and consequently enhances guanylyl cyclase-A (GC-A/NPR1) signaling. However, the roles of OSTN in the kidney have not been well clarified.
View Article and Find Full Text PDFPosttranslational modifications as therapeutic targets for intestinal disorders.
Pharmacol Res
March 2021
College of Pharmacy, Pusan National University, Busan, 46241, Republic of Korea. Electronic address:
A variety of biological processes are regulated by posttranslational modifications. Posttranslational modifications including phosphorylation, ubiquitination, glycosylation, and proteolytic cleavage, control diverse physiological functions in the gastrointestinal tract. Therefore, a better understanding of their implications in intestinal diseases, including inflammatory bowel disease, irritable bowel syndrome, celiac disease, and colorectal cancer would provide a basis for the identification of novel biomarkers as well as attractive therapeutic targets.
View Article and Find Full Text PDFNatriuretic peptide receptor guanylyl cyclase-A pathway counteracts glomerular injury evoked by aldosterone through p38 mitogen-activated protein kinase inhibition.
Sci Rep
April 2017
Department of Nephrology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Guanylyl cyclase-A (GC-A) signaling, a natriuretic peptide receptor, exerts renoprotective effects by stimulating natriuresis and reducing blood pressure. Previously we demonstrated massive albuminuria with hypertension in uninephrectomized, aldosterone-infused, and high salt-fed (ALDO) systemic GC-A KO mice with enhanced phosphorylation of p38 mitogen-activated protein kinase (MAPK) in podocytes. In the present study, we examined the interaction between p38 MAPK and GC-A signaling.
View Article and Find Full Text PDFAcquired Exchange Protein Directly Activated by Cyclic Adenosine Monophosphate Activity Induced by p38 Mitogen-activated Protein Kinase in Primary Afferent Neurons Contributes to Sustaining Postincisional Nociception.
Anesthesiology
January 2017
From the Department of Anesthesiology (M.M., T.S., F.A.), Research Unit for the Neurobiology of Pain, Department of Anesthesiology (M.M., F.A.), and Department of Biostatistics, Graduate School of Medical Science (I.Y.), Kyoto Prefectural University of Medicine, Kyoto, Japan; United Graduate School of Drug Discovery and Medical Information Sciences, and Department of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University, Gifu, Japan (K.O.-H.).
Background: The molecular mechanisms responsible for sustained pain after tissue injury are largely unknown. The aim of this study was to clarify the role of exchange protein directly activated by cyclic adenosine monophosphate (EPAC) in sustained postincisional nociception, using tissue injury-induced nociceptor priming, and involvement of p38 mitogen-activated protein kinase (p38MAPK) in EPAC-mediated nociceptor priming.
Methods: Plantar incisions were made in the hind paws of Sprague-Dawley rats (n = 144).
Activation of p38 mitogen-activated protein kinase in the dorsal root ganglion contributes to pain hypersensitivity after plantar incision.
Neuroscience
March 2013
Department of Anesthesiology, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Background: The phosphorylation of p38 mitogen-activated protein kinase (MAPK) in the dorsal root ganglion (DRG) promotes primary afferent sensitization. The role of p38MAPK signaling in the DRG in the pathogenesis of plantar incision hyperalgesia has not been investigated.
Results: Levels of phosphorylated p38MAPK (p-p38MAPK) obviously increased in the DRG after plantar incision.
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