Development of Long-Acting Human Adrenomedullin Fc-Fusion Proteins.

adrenomedullin hypotensive effect immunoglobulin G recombinant protein

Journal

Biology
ISSN: 2079-7737
Titre abrégé: Biology (Basel)
Pays: Switzerland
ID NLM: 101587988

Informations de publication

Date de publication:
19 Jul 2022
Historique:
received: 22 04 2022
revised: 15 07 2022
accepted: 15 07 2022
entrez: 14 9 2022
pubmed: 15 9 2022
medline: 15 9 2022
Statut: epublish

Résumé

(1) Background: Human adrenomedullin (hAM) is a hypotensive peptide hormone that exerts powerful anti-inflammatory effects. AM also had therapeutic effects in various animal experimental models of disease. However, treatment required continuous administration as the half-life of native AM is short in blood. To resolve this, we developed four human IgG1 and IgG4 Fc-fusion proteins containing full-length hAM or hAM residues 6-52. (2) Methods: We used mammalian cells to produce recombinant Fc-AM derivatives and tested the pharmacokinetics and biological activity of Fc-AM. (3) Results: We developed four Fc-fusion AMs (Fc-AM), which are long-acting AM derivatives in mammalian cells. Fc-AM had a prolonged half-life in blood and retained its ability to bind to the AM

Identifiants

pubmed: 36101452
pii: biology11071074
doi: 10.3390/biology11071074
pmc: PMC9312564
pii:
doi:

Types de publication

Journal Article

Langues

eng

Subventions

Organisme : Japan Agency for Medical Research and Development
ID : A513

Références

Biochem Biophys Res Commun. 1993 Apr 30;192(2):553-60
pubmed: 8387282
Nature. 1998 May 28;393(6683):333-9
pubmed: 9620797
J Biochem. 2021 Dec 4;170(4):445-451
pubmed: 33964134
Adv Drug Deliv Rev. 2015 Aug 30;91:109-24
pubmed: 25703189
Nucl Med Biol. 2018 Dec;67:36-42
pubmed: 30388434
Intensive Care Med. 2021 Nov;47(11):1284-1294
pubmed: 34605947
Br J Pharmacol. 2018 Jan;175(1):3-17
pubmed: 29059473
MAbs. 2011 Sep-Oct;3(5):415-6
pubmed: 21785279
Clin Chim Acta. 1999 Sep;287(1-2):131-43
pubmed: 10509902
Clin Chem. 1999 Feb;45(2):244-51
pubmed: 9931047
Circulation. 2004 Jul 27;110(4):426-31
pubmed: 15262849
Intensive Care Med Exp. 2019 May 15;7(1):25
pubmed: 31093784
J Biol Chem. 2000 Sep 22;275(38):29602-9
pubmed: 10882736
Br J Clin Pharmacol. 2001 Aug;52(2):165-8
pubmed: 11488773
Crit Care. 2014 Jun 16;18(3):152
pubmed: 25041977
Biol Pharm Bull. 2020;43(11):1799-1803
pubmed: 33132326
Drug Des Devel Ther. 2020 Jan 06;14:1-11
pubmed: 32021087
Diabetes Metab Res Rev. 2010 May;26(4):287-96
pubmed: 20503261
Drug Dev Res. 2017 Jun;78(3-4):129-134
pubmed: 28449192
Shock. 2018 Dec;50(6):648-654
pubmed: 29324627
J Gastroenterol. 2021 Feb;56(2):147-157
pubmed: 33140199
Peptides. 2001 Nov;22(11):1753-63
pubmed: 11754961
Peptides. 2014 Jul;57:118-21
pubmed: 24874704
J Biol Chem. 2001 Apr 13;276(15):12292-300
pubmed: 11116141
Biochem Biophys Res Commun. 2020 Aug 27;529(3):778-783
pubmed: 32736707
Biotechnol Adv. 2012 Sep-Oct;30(5):1158-70
pubmed: 21968146
Mol Med Rep. 2016 May;13(5):3724-34
pubmed: 27035412
MAbs. 2009 May-Jun;1(3):281-7
pubmed: 20065645
J Biochem. 2019 Aug 1;166(2):157-162
pubmed: 30895298

Auteurs

Sayaka Nagata (S)

Frontier Science Research Center, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan.

Motoo Yamasaki (M)

Frontier Science Research Center, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan.

Nobuko Kuroishi (N)

Frontier Science Research Center, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan.

Kazuo Kitamura (K)

Frontier Science Research Center, University of Miyazaki, 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan.

Classifications MeSH