Best matches for glycation in bone marrow:
Hematopoietic stem/progenitor involvement in retinal microvascular repair during diabetes: Implications for bone marrow rejuvenation.
Bhatwadekar AD et al. Vision Res.
(2017)
Identification of megakaryocytes as a target of advanced glycation end products in diabetic complications in bone marrow.
Wang B et al. Acta Diabetol.
(2018)
Bone Marrow Fat Changes After Gastric Bypass Surgery Are Associated With Loss of Bone Mass.
Kim TY et al. J Bone Miner Res.
(2017)
1.
Davis HM, Valdez S, Gomez L, Malicky P, White FA, Subler MA, Windle JJ, Bidwell JP, Bruzzaniti A, Plotkin LI.
J Cell Biochem. 2019 May 20. doi: 10.1002/jcb.28932. [Epub ahead of print]
2.
Stamatopoulos A, Stamatopoulos T, Gamie Z, Kenanidis E, Ribeiro RDC, Rankin KS, Gerrand C, Dalgarno K, Tsiridis E.
J Bone Oncol. 2019 Mar 19;16:100231. doi: 10.1016/j.jbo.2019.100231. eCollection 2019 Jun. Review.
3.
Alamri BN, Bahabri A, Aldereihim AA, Alabduljabbar M, Alsubaie MM, Alnaqeb D, Almogbel E, Metias NS, Alotaibi OA, Al-Rubeaan K.
Eur Rev Med Pharmacol Sci. 2019 Mar;23(5):2139-2150. doi: 10.26355/eurrev_201903_17259.
4.
Tamada
K, Nakajima S, Ogawa N, Inada M, Shibasaki H, Sato A, Takasawa R,
Yoshimori A, Suzuki Y, Watanabe N, Oyama T, Abe H, Inoue S, Abe T,
Yokomizo T, Tanuma S.
Biochem Biophys Res Commun. 2019 Apr 9;511(3):665-670. doi: 10.1016/j.bbrc.2019.01.136. Epub 2019 Feb 27.
- PMID:
- 30826057
5.
Jin H, Zhang Z, Wang C, Tang Q, Wang J, Bai X, Wang Q, Nisar M, Tian N, Wang Q, Mao C, Zhang X, Wang X.
Exp Mol Med. 2018 Nov 21;50(11):154. doi: 10.1038/s12276-018-0177-z.
6.
Xiu G, Xiong W, Yin Y, Chen X, Liu P, Sun J, Ling B.
Zhonghua Wei Zhong Bing Ji Jiu Yi Xue. 2018 Sep;30(9):830-835. doi: 10.3760/cma.j.issn.2095-4352.2018.09.003. Chinese.
7.
Wang Y, Ma WQ, Zhu Y, Han XQ, Liu N.
Front Endocrinol (Lausanne). 2018 Sep 21;9:524. doi: 10.3389/fendo.2018.00524. eCollection 2018.
8.
Grosjean F, Yubero-Serrano EM, Zheng F, Esposito V, Swamy S, Elliot SJ, Cai W, Vlassara H, Salem F, Striker GE.
PLoS One. 2018 Sep 25;13(9):e0204366. doi: 10.1371/journal.pone.0204366. eCollection 2018.
9.
Kubota K, Nakano M, Kobayashi E, Mizue Y, Chikenji T, Otani M, Nagaishi K, Fujimiya M.
PLoS One. 2018 Sep 21;13(9):e0204252. doi: 10.1371/journal.pone.0204252. eCollection 2018.
10.
Cortet B, Lucas S, Legroux-Gerot I, Penel G, Chauveau C, Paccou J.
Joint Bone Spine. 2019 May;86(3):315-320. doi: 10.1016/j.jbspin.2018.08.002. Epub 2018 Aug 8.
Both type 1 and type 2 diabetes mellitus are associated with bone
disorders, albeit via different mechanisms. Early studies in patients
with type 1 diabetes suggested a 10-fold increase in the hip fracture
risk compared to non-diabetic controls. Meta-analyses published more
recently indicate a somewhat smaller risk increase, with odds ratios of 6
to 7. Diminished bone mineral density is among the contributors to the increased fracture risk. Both types of diabetes are associated with decreased bone strength related to low bone turnover. The multiple and interconnected pathophysiological mechanisms underlying the bone disorders seen in type 1 diabetes include insulin deficiency, accumulation of advanced glycation end (AGE) products, bone microarchitecture alterations, changes in bone marrow fat content, low-grade inflammation, and osteocyte dysfunction. The bone alterations are less severe in type 2 diabetes. Odds ratios for hip fractures have ranged across studies from 1.2 to 1.7, and bone mineral density is higher than in non-diabetic controls. The odds ratio is about 1.2 for all bone
fragility fractures combined. The pathophysiological mechanisms are
complex, particularly as obesity is very common in patients with type 2
diabetes and is itself associated with an increased risk of fractures at
specific sites (humerus, tibia, and ankle). The main mechanisms
underlying the bone
fragility are an increase in the risk of falls, sarcopenia, disorders
of carbohydrate metabolism, vitamin D deficiency, and alterations in
cortical bone microarchitecture and bone
matrix. The medications used to treat both types of diabetes do not
seem to play a major role. Nevertheless, thiazolidinediones and, to a
lesser extent, sodium-glucose cotransporter inhibitors may have adverse
effects on bone, whereas metformin may have beneficial effects. For the most part, the standard management of bone
fragility applies to patients with diabetes. However, emphasis should
be placed on preventing falls, which are particularly common in this
population. Finally, there is some evidence to suggest that
anti-fracture treatments are similarly effective in patients with and
without diabetes.
Copyright © 2018 Société française de rhumatologie. Published by Elsevier Masson SAS. All rights reserved.
11.
Kwiatkowski J, Halupczok-Żyła J, Bolanowski M, Kuliszkiewicz-Janus M.
Adv Clin Exp Med. 2018 Oct;27(10):1447-1452. doi: 10.17219/acem/71054. Review.
Diabetes mellitus (DM), a growing health problem itself, is accompanied
by an increased risk of cardiovascular and thrombotic complications. The
imbalance between coagulation and fibrinolysis processes observed in
patients with diabetes may be defined as diabetic thrombophilia. Several
mechanisms are involved in the hypercoagulability state in diabetics,
including endothelial cell damage, altered platelet structure and
function, increased microparticle formation, different structure of
fibrin clots, disturbances in the activity of coagulation factors,
fluctuations in the concentrations of fibrinolysis activators and
inhibitors, and qualitative changes of proteins due to glycation
and oxidation processes. These all are the reasons why DM is the most
common cause of acquired thrombophilia. Moreover, diabetes changes the
efficacy of certain medications. Results of various trials seem to
suggest that thrombolytic drugs are less effective in patients suffering
from this disease. The impact of DM on the effectiveness of treatment
with acetylsalicylic acid (ASA) remains unclear. Awareness of thrombotic
complications in diabetic patients may enable earlier diagnosis and
proper therapy.Free Article
12.
Perusko M, van Roest M, Stanic-Vucinic D, Simons PJ, Pieters RHH, Cirkovic Velickovic T, Smit JJ.
Mol Nutr Food Res. 2018 Sep;62(17):e1800341. doi: 10.1002/mnfr.201800341. Epub 2018 Jul 29.
13.
Kovačić M, Mitrović-Ajtić O, Beleslin-Čokić B, Djikić D, Subotički T, Diklić M, Leković D, Gotić M, Mossuz P, Čokić VP.
Cell Oncol (Dordr). 2018 Oct;41(5):541-553. doi: 10.1007/s13402-018-0392-6. Epub 2018 Jun 26.Abstract PURPOSE:
Previously,
the family of S100A proteins has been found to be associated with
inflammation and myelopoiesis and to be able to induce or support
myeloproliferation during chronic inflammation. Here, we studied the
inflammatory myeloid-related proteins S100A4, S100A8, S100A9 and S100A12
in myeloproliferative neoplasms (MPNs) in order to assess the
involvement of chronic inflammation in the pathogenesis of MPN. METHODS: We analyzed the S100A4, S100A8, S100A9 and S100A12 mRNA and protein levels in the bone marrow
and circulation of 140 patients with MPN and 15 healthy controls using
Western blotting, microarray-based mRNA expression profiling and ELISA
assays, respectively. In addition we performed functional studies on the
proliferation-related AKT and ERK1/2 signaling pathways in MPN-derived
granulocytes using Western blotting and proteomic analyses. RESULTS: We found that the S100A mRNA levels were increased in MPN patient-derived circulatory CD34+ cells, and that their protein expression levels were also augmented in their granulocytes and bone marrow
stroma cells, depending on the JAK2V617F mutation allele burden. We
also found that calreticulin (CALR) mutations were related to reduced
S100A8 plasma levels in primary myelofibrosis (PMF). The S100A8 plasma
levels were found to be increased in MPN, the S100A9 plasma levels in
PMF and essential thrombocythemia (ET), and the S100A12 plasma levels in
polycythemia vera (PV). These S100A plasma levels showed a positive
correlation with the systemic inflammation marker IL-8, as well as with
the numbers of leukocytes and thrombocytes, depending on the JAK2V617F
mutation status. Additionally, we found that heterodimeric S100A8/9 can
inhibit the AKT pathway in MPN-derived granulocytes mediated by the
Toll-like receptor 4 (TLR4), depending on the CALR mutation status.
Conversely, we found that blocking of the receptor for advanced glycation
end products (RAGE) increased the S100A8/9-mediated inhibition of AKT
signaling in the MPN-derived granulocytes. Moreover, we found that
heterodimeric S100A8/9 generally induced TLR4-mediated ERK1/2
dephosphorylation proportionally to the JAK2V617F mutation allele
burden. TLR4/RAGE blocking prevented the S100A8/9-mediated inhibition of
ERK1/2 phosphorylation in PV. CONCLUSIONS:
From our data we conclude that the S100A8 and S100A9 granulocyte and plasma levels are increased in MPN patients, along with inflammation markers, depending on their JAK2V617F mutation allele burden. We also found that S100A8/9-mediated inhibition of the proliferation-related AKT and ERK1/2 signaling pathways can be decreased by CALR mutation-dependent TLR4 blocking and increased by RAGE inhibition in MPN.
From our data we conclude that the S100A8 and S100A9 granulocyte and plasma levels are increased in MPN patients, along with inflammation markers, depending on their JAK2V617F mutation allele burden. We also found that S100A8/9-mediated inhibition of the proliferation-related AKT and ERK1/2 signaling pathways can be decreased by CALR mutation-dependent TLR4 blocking and increased by RAGE inhibition in MPN.
14.
Jin X, Liu L, Zhang Y, Xiang Y, Yin G, Lu Y, Shi L, Dong J, Shen C.
J Diabetes Res. 2018 Mar 22;2018:2527406. doi: 10.1155/2018/2527406. eCollection 2018.
15.
Nagareddy PR, Noothi SK, Flynn MC, Murphy AJ.
J Endocrinol. 2018 Jul;238(1):R1-R11. doi: 10.1530/JOE-18-0082. Epub 2018 May 2. Review.
16.
Najar M, Fayyad-Kazan M, Raicevic G, Fayyad-Kazan H, Meuleman N, Bron D, Lagneaux L.
Cell J. 2018 Jul;20(2):250-258. doi: 10.22074/cellj.2018.5104. Epub 2018 Mar 18.
17.
Li R, Wang J, Zhu F, Li R, Liu B, Xu W, He G, Cao H, Wang Y, Yang J.
Mol Immunol. 2018 May;97:45-55. doi: 10.1016/j.molimm.2018.02.014. Epub 2018 Mar 19.
18.
Kim JH, Kim KA, Shin YJ, Kim H, Majid A, Bae ON.
J Toxicol Environ Health A. 2018;81(9):266-277. doi: 10.1080/15287394.2018.1440185. Epub 2018 Feb 23.Abstract
Endothelial cells
(ECs) maintain the structure and function of blood vessels and are
readily exposed to exogenous and endogenous toxic substances in the
circulatory system. Bone marrow-derived
endothelial progenitor cells (EPCs) circulate in the blood and
differentiate to EC, which are known to participate in angiogenesis and
regeneration of injured vessels. Dysfunction in EPC contributes to
cardiovascular complications in patients with diabetes, but the precise
molecular mechanisms underlying diabetic EPC abnormalities are not
completely understood.
The aim of this study was to investigate the mechanisms underlying diabetic EPC dysfunction using methylglyoxal (MG), an endogenous toxic diabetic metabolite. Data demonstrated that MG decreased cell viability and protein expression of vascular endothelial growth factor receptor (VEGFR)-2 associated with functional impairment of tube formation in EPC. The generation of advanced glycation end (AGE) products was increased in EPC following exposure to MG.
Blockage of receptor for AGE (RAGE) by FPS-ZM1, a specific antagonist for RAGE, significantly reversed the decrease of VEGFR-2 protein expression and angiogenic dysfunction in MG-incubated EPC. Taken together, data demonstrated that MG induced angiogenic impairment in EPC via alterations in the AGE/RAGE-VEGFR-2 pathway which may be utilized in the development of potential therapeutic and preventive targets for diabetic vascular complications.
The aim of this study was to investigate the mechanisms underlying diabetic EPC dysfunction using methylglyoxal (MG), an endogenous toxic diabetic metabolite. Data demonstrated that MG decreased cell viability and protein expression of vascular endothelial growth factor receptor (VEGFR)-2 associated with functional impairment of tube formation in EPC. The generation of advanced glycation end (AGE) products was increased in EPC following exposure to MG.
Blockage of receptor for AGE (RAGE) by FPS-ZM1, a specific antagonist for RAGE, significantly reversed the decrease of VEGFR-2 protein expression and angiogenic dysfunction in MG-incubated EPC. Taken together, data demonstrated that MG induced angiogenic impairment in EPC via alterations in the AGE/RAGE-VEGFR-2 pathway which may be utilized in the development of potential therapeutic and preventive targets for diabetic vascular complications.
19.
Wang B, Yu J, Wang T, Shen Y, Lin D, Xu X, Wang Y.
Acta Diabetol. 2018 May;55(5):419-427. doi: 10.1007/s00592-018-1109-z. Epub 2018 Feb 8.
20.
Tachibana M.
Yakugaku Zasshi. 2018;138(2):143-148. doi: 10.1248/yakushi.17-00158. Review. Japanese.
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