Literature DB >> 33661300

MetAP2 inhibition modifies hemoglobin S to delay polymerization and improves blood flow in sickle cell disease.

Melanie Demers1, Sarah Sturtevant1, Kevin R Guertin1, Dipti Gupta1,2, Kunal Desai1, Benjamin F Vieira1, Wenjing Li1, Alexandra Hicks1, Ayman Ismail1, Bronner P Gonçalves3,4,5, Giuseppe Di Caprio4,6, Ethan Schonbrun4, Scott Hansen7, Faik N Musayev8,9, Martin K Safo8,9, David K Wood7, John M Higgins3,4,5, David R Light1.   

Abstract

Sickle cell disease (SCD) is associated with hemolysis, vascular inflammation, and organ damage. Affected patients experience chronic painful vaso-occlusive events requiring hospitalization. Hypoxia-induced polymerization of sickle hemoglobin S (HbS) contributes to sickling of red blood cells (RBCs) and disease pathophysiology. Dilution of HbS with nonsickling hemoglobin or hemoglobin with increased oxygen affinity, such as fetal hemoglobin or HbS bound to aromatic aldehydes, is clinically beneficial in decreasing polymerization. We investigated a novel alternate approach to modify HbS and decrease polymerization by inhibiting methionine aminopeptidase 2 (MetAP2), which cleaves the initiator methionine (iMet) from Val1 of α-globin and βS-globin. Kinetic studies with MetAP2 show that βS-globin is a fivefold better substrate than α-globin. Knockdown of MetAP2 in human umbilical cord blood-derived erythroid progenitor 2 cells shows more extensive modification of α-globin than β-globin, consistent with kinetic data. Treatment of human erythroid cells in vitro or Townes SCD mice in vivo with selective MetAP2 inhibitors extensively modifies both globins with N-terminal iMet and acetylated iMet. HbS modification by MetAP2 inhibition increases oxygen affinity, as measured by decreased oxygen tension at which hemoglobin is 50% saturated. Acetyl-iMet modification on βS-globin delays HbS polymerization under hypoxia. MetAP2 inhibitor-treated Townes mice reach 50% total HbS modification, significantly increasing the affinity of RBCs for oxygen, increasing whole blood single-cell RBC oxygen saturation, and decreasing fractional flow velocity losses in blood rheology under decreased oxygen pressures. Crystal structures of modified HbS variants show stabilization of the nonpolymerizing high O2-affinity R2 state, explaining modified HbS antisickling activity. Further study of MetAP2 inhibition as a potential therapeutic target for SCD is warranted.
© 2021 by The American Society of Hematology.

Entities:  

Mesh:

Substances:

Year:  2021        PMID: 33661300      PMCID: PMC7948285          DOI: 10.1182/bloodadvances.2020003670

Source DB:  PubMed          Journal:  Blood Adv        ISSN: 2473-9529


  48 in total

Review 1.  Sickle-cell haemoglobin polymerization: is it the primary pathogenic event of sickle-cell anaemia?

Authors:  Peter G Vekilov
Journal:  Br J Haematol       Date:  2007-10       Impact factor: 6.998

2.  The high resolution crystal structure of deoxyhemoglobin S.

Authors:  D J Harrington; K Adachi; W E Royer
Journal:  J Mol Biol       Date:  1997-09-26       Impact factor: 5.469

3.  Nucleation-controlled aggregation of deoxyhemoglobin S. Possible difference in the size of nuclei in different phosphate concentrations.

Authors:  K Adachi; T Asakura
Journal:  J Biol Chem       Date:  1979-08-25       Impact factor: 5.157

4.  Preclinical Efficacy and Safety of the Novel Antidiabetic, Antiobesity MetAP2 Inhibitor ZGN-1061.

Authors:  Bryan F Burkey; Niel C Hoglen; Philip Inskeep; Margaret Wyman; Thomas E Hughes; James E Vath
Journal:  J Pharmacol Exp Ther       Date:  2018-02-28       Impact factor: 4.030

5.  5-hydroxymethyl-2-furfural modifies intracellular sickle haemoglobin and inhibits sickling of red blood cells.

Authors:  Osheiza Abdulmalik; Martin K Safo; Qiukan Chen; Jisheng Yang; Carlo Brugnara; Kwaku Ohene-Frempong; Donald J Abraham; Toshio Asakura
Journal:  Br J Haematol       Date:  2005-02       Impact factor: 6.998

6.  Effects of MetAP2 inhibition on hyperphagia and body weight in Prader-Willi syndrome: A randomized, double-blind, placebo-controlled trial.

Authors:  Shawn E McCandless; Jack A Yanovski; Jennifer Miller; Cary Fu; Lynne M Bird; Parisa Salehi; Christine L Chan; Diane Stafford; M Jennifer Abuzzahab; David Viskochil; Sarah E Barlow; Moris Angulo; Susan E Myers; Barbara Y Whitman; Dennis Styne; Elizabeth Roof; Elisabeth M Dykens; Ann O Scheimann; Jaret Malloy; Dongliang Zhuang; Kristin Taylor; Thomas E Hughes; Dennis D Kim; Merlin G Butler
Journal:  Diabetes Obes Metab       Date:  2017-07-13       Impact factor: 6.577

7.  Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese.

Authors:  Jieyi Wang; George S Sheppard; Pingping Lou; Megumi Kawai; Chang Park; David A Egan; Andrew Schneider; Jennifer Bouska; Rick Lesniewski; Jack Henkin
Journal:  Biochemistry       Date:  2003-05-06       Impact factor: 3.162

Review 8.  New developments in anti-sickling agents: can drugs directly prevent the polymerization of sickle haemoglobin in vivo?

Authors:  Esther Oder; Martin K Safo; Osheiza Abdulmalik; Gregory J Kato
Journal:  Br J Haematol       Date:  2016-09-08       Impact factor: 6.998

9.  Erythroid expression of the heme-regulated eIF-2 alpha kinase.

Authors:  J S Crosby; K Lee; I M London; J J Chen
Journal:  Mol Cell Biol       Date:  1994-06       Impact factor: 4.272

10.  Structures of N-terminally processed KRAS provide insight into the role of N-acetylation.

Authors:  Srisathiyanarayanan Dharmaiah; Timothy H Tran; Simon Messing; Constance Agamasu; William K Gillette; Wupeng Yan; Timothy Waybright; Patrick Alexander; Dominic Esposito; Dwight V Nissley; Frank McCormick; Andrew G Stephen; Dhirendra K Simanshu
Journal:  Sci Rep       Date:  2019-07-19       Impact factor: 4.379

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.