Human IL-36RA production in Escherichia coli with coexpression of E. coli methionine aminopeptidase. II. Comparison of IL-36RA biological activity from different strains

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Human IL-36RA production in Escherichia coli with coexpression of E. coli methionine aminopeptidase. II. Comparison of IL-36RA biological activity from different strains. / Kolobov, A. A.; Kondratyeva, E. V.; Sharafutdinova, T. A.; Kalinin, R. S.; Nimiritsky, P. P.; Stefanov, V. E.; Petrov, A. V.

в: Cell and Tissue Biology, Том 11, № 6, 01.11.2017, стр. 453-457.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

BibTeX

@article{d1d5e9850611446bbdee1124eecf2454,

title = "Human IL-36RA production in Escherichia coli with coexpression of E. coli methionine aminopeptidase. II. Comparison of IL-36RA biological activity from different strains",

abstract = "Proinflammatory cytokines of the interleukin-36 (IL-36) family are involved in the pathogenesis of different skin diseases in human and mice. Administration of exogenous IL-36 receptor antagonist (IL-36RA) may be an approach to therapy of different dermatitises. For its full biological activity, IL-36RA requires cleavage of N-terminal methionine residue. We created three E. coli strains producing IL-36RA coexpressed with E. coli methionine aminopeptidase under control of different promoters. To test the biological activity of IL-36RA from different strains we transfected А549 cells with plasmid carrying the IL-36 receptor gene (IL1RL2). These cells respond to IL-36g treatment with production of IL-8, which can be quantified with ELISA. IL-36RA treatment disrupts IL-36 receptor activation by IL-36g and production of IL-8. Using this system, we proved that IL-36RA from all three producer strains is fully biologically active.",

keywords = "coexpression, interleukin, Interleukin-36 receptor antagonist (IL-36RA), methionine, methionine aminopeptidase (MAP), recombinant protein, А549 cells",

author = "Kolobov, {A. A.} and Kondratyeva, {E. V.} and Sharafutdinova, {T. A.} and Kalinin, {R. S.} and Nimiritsky, {P. P.} and Stefanov, {V. E.} and Petrov, {A. V.}",

note = "Publisher Copyright: {\textcopyright} 2017, Pleiades Publishing, Ltd.",

year = "2017",

month = nov,

day = "1",

doi = "10.1134/S1990519X17060074",

language = "English",

volume = "11",

pages = "453--457",

journal = "Cell and Tissue Biology",

issn = "1990-519X",

publisher = "МАИК {"}Наука/Интерпериодика{"}",

number = "6",

}

RIS

TY - JOUR

T1 - Human IL-36RA production in Escherichia coli with coexpression of E. coli methionine aminopeptidase. II. Comparison of IL-36RA biological activity from different strains

AU - Kolobov, A. A.

AU - Kondratyeva, E. V.

AU - Sharafutdinova, T. A.

AU - Kalinin, R. S.

AU - Nimiritsky, P. P.

AU - Stefanov, V. E.

AU - Petrov, A. V.

PY - 2017/11/1

Y1 - 2017/11/1

N2 - Proinflammatory cytokines of the interleukin-36 (IL-36) family are involved in the pathogenesis of different skin diseases in human and mice. Administration of exogenous IL-36 receptor antagonist (IL-36RA) may be an approach to therapy of different dermatitises. For its full biological activity, IL-36RA requires cleavage of N-terminal methionine residue. We created three E. coli strains producing IL-36RA coexpressed with E. coli methionine aminopeptidase under control of different promoters. To test the biological activity of IL-36RA from different strains we transfected А549 cells with plasmid carrying the IL-36 receptor gene (IL1RL2). These cells respond to IL-36g treatment with production of IL-8, which can be quantified with ELISA. IL-36RA treatment disrupts IL-36 receptor activation by IL-36g and production of IL-8. Using this system, we proved that IL-36RA from all three producer strains is fully biologically active.

AB - Proinflammatory cytokines of the interleukin-36 (IL-36) family are involved in the pathogenesis of different skin diseases in human and mice. Administration of exogenous IL-36 receptor antagonist (IL-36RA) may be an approach to therapy of different dermatitises. For its full biological activity, IL-36RA requires cleavage of N-terminal methionine residue. We created three E. coli strains producing IL-36RA coexpressed with E. coli methionine aminopeptidase under control of different promoters. To test the biological activity of IL-36RA from different strains we transfected А549 cells with plasmid carrying the IL-36 receptor gene (IL1RL2). These cells respond to IL-36g treatment with production of IL-8, which can be quantified with ELISA. IL-36RA treatment disrupts IL-36 receptor activation by IL-36g and production of IL-8. Using this system, we proved that IL-36RA from all three producer strains is fully biologically active.

KW - coexpression

KW - interleukin

KW - Interleukin-36 receptor antagonist (IL-36RA)

KW - methionine

KW - methionine aminopeptidase (MAP)

KW - recombinant protein

KW - А549 cells

UR - http://www.scopus.com/inward/record.url?scp=85038227272&partnerID=8YFLogxK

U2 - 10.1134/S1990519X17060074

DO - 10.1134/S1990519X17060074

M3 - Article

AN - SCOPUS:85038227272

VL - 11

SP - 453

EP - 457

JO - Cell and Tissue Biology

JF - Cell and Tissue Biology

SN - 1990-519X

IS - 6

ER -

ID: 89864833