Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase
Cytokine activity of the isolated recombinant C-terminal domain of mammalian lyrosyl-tRNA synthetasg (TyrRS), which is homologous to a tumor-derived cytokine, endothelial and monocyte activating polypeptide (EMAP-2) has been studied. It was shown that C-domain induced a ~ 2-fold increase of monocyte...
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irk-123456789-1563292019-07-05T16:11:17Z Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase Kornelyuk, A. Tas, M. Dubrovsky, A. Murray, J.C. Приоритетные работы Cytokine activity of the isolated recombinant C-terminal domain of mammalian lyrosyl-tRNA synthetasg (TyrRS), which is homologous to a tumor-derived cytokine, endothelial and monocyte activating polypeptide (EMAP-2) has been studied. It was shown that C-domain induced a ~ 2-fold increase of monocyte chemotaxis. This effect is comparable with the values of chemotaxis induction by EMAP-2 cytokine and proEMAP-2. The truncated catalytic form of bovine TyrRS (2 x 39 kDa) lias no effect on monocyte chemotaxis. C-domain of TyrRS also induced a ~ 3-fold increase in tissue factor activity in cultured human endothelial cells. A hypothesis is forwarded that the isolated C-domain of mammalian TyrRS may be released at proteoiytic cleavage of TyrRS by some protease, activated ui stress conditions, and functions as a mediator via signal transduction through interaction with a putative EMAP-2 receptor. Досліджено цитокінову активність ізольованого рекомбінантного С-кінцевого домена тирозил-тРНК синтетази (тирРС) ссавців, гомологічного ЕМАР-2 цитокіну. Показано, що С-домен індукує збільшення хемотаксису моноцитів у 2 рази. Цей ефект близький до такого, спричиненого ЕМАР-2 та ргоЕМАР-2. Протеолітично модифікована каталітична форма тирРС (2 у- 39 кДа) не впливала на хемотаксис моноцитів. С-домен тирРС також індукує зростання активності тканинного фактора ендотеліальних клітин людини в 3 рази. Пропонується гіпотеза стосовно того, що ізольований С-домен може вивільнятися при протеолітичному розщепленні тирРС певною протеазою, яка активується в стресових умовах, і функціонувати як медіатор шляхом передачі сигналу при взаємодії з рецептором ЕМАР-2 цитокіну Изучена цитокиновая активность изолированного рекомбинантного С-концевого домена тирозил-тРНК синтетазы (тирРС) млекопитающих, гомологичного ЕМАР-2 цитокину. Показано, что С-домен индуцирует увеличение хемотаксиса моноцитов в 2 раза. Этот эффект близок к таковому, вызываемому ЕМАР-2 и ргоЕМАР-2. Пратеолитически модифицированная каталитическая форма тирРС (2 х 39 кДа) не влияет на хемотаксис моноцитов. С-домен тир PC также индуцирует рост активности тканевого фактора эндотелиальных клеток человека в 3 раза. Предложена гипотеза относительно того, что изолированный С-домен может высвобождаться при протеолитическом расщеплении тирРС определенной протеазой, активируемой в стрессовых условиях, и функционировать как медиатор путем передачи сигнала при взаимодействии с рецептором цитокина ЕМАР-2. 1999 Article Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase / A. Kornelyuk, M. Tas, A. Dubrovsky, J.C. Murray // Биополимеры и клетка. — 1999. — Т. 15, № 2. — С. 168-172. — Бібліогр.: 23 назв. — англ. 0233-7657 DOI: http://dx.doi.org/10.7124/bc.000516 http://dspace.nbuv.gov.ua/handle/123456789/156329 577.152.611 en Биополимеры и клетка Інститут молекулярної біології і генетики НАН України |
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Приоритетные работы Приоритетные работы Kornelyuk, A. Tas, M. Dubrovsky, A. Murray, J.C. Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase Биополимеры и клетка |
| description |
Cytokine activity of the isolated recombinant C-terminal domain of mammalian lyrosyl-tRNA synthetasg (TyrRS), which is homologous to a tumor-derived cytokine, endothelial and monocyte activating polypeptide (EMAP-2) has been studied. It was shown that C-domain induced a ~ 2-fold increase of monocyte chemotaxis. This effect is comparable with the values of chemotaxis induction by EMAP-2 cytokine and proEMAP-2. The truncated catalytic form of bovine TyrRS (2 x 39 kDa) lias no effect on monocyte chemotaxis. C-domain of TyrRS also induced a ~ 3-fold increase in tissue factor activity in cultured human endothelial cells. A hypothesis is forwarded that the isolated C-domain of mammalian TyrRS may be released at proteoiytic cleavage of TyrRS by some protease, activated ui stress conditions, and functions as a mediator via signal transduction through interaction with a putative EMAP-2 receptor. |
| format |
Article |
| author |
Kornelyuk, A. Tas, M. Dubrovsky, A. Murray, J.C. |
| author_facet |
Kornelyuk, A. Tas, M. Dubrovsky, A. Murray, J.C. |
| author_sort |
Kornelyuk, A. |
| title |
Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase |
| title_short |
Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase |
| title_full |
Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase |
| title_fullStr |
Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase |
| title_full_unstemmed |
Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase |
| title_sort |
cytokine activity of the non-catalytic emap-2-like domain of mammalian tyrosyl-trna synthetase |
| publisher |
Інститут молекулярної біології і генетики НАН України |
| publishDate |
1999 |
| topic_facet |
Приоритетные работы |
| url |
http://dspace.nbuv.gov.ua/handle/123456789/156329 |
| citation_txt |
Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase / A. Kornelyuk, M. Tas, A. Dubrovsky, J.C. Murray // Биополимеры и клетка. — 1999. — Т. 15, № 2. — С. 168-172. — Бібліогр.: 23 назв. — англ. |
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Биополимеры и клетка |
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ISSN 0233-7657. Биополимеры и клетка. 1999. Т. 15. Ns 2
ПРИОРИТЕТНЫЕ РАБОТЫ
Cytokine activity of the non-catalytic EMAP-2-like
domain of mammalian tyrosyl-tRNA synthetase
Alexander Kornelyuk, Maarten P. R. Tas1, Alexei Dubrovsky, J. Clifford Murray1
Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine
150 Acad. Zabolotnoho vul., Kyiv, 252143, Ukraine
University of Nottingham Laboratory of Molecular Oncology, Cancer Research Campaign Department of Clinical Oncology
City Hospital, Nottingham NG5 1PB, Great Britain
Cytokine activity of the isolated recombinant C-terminai domain of mammalian tyrosyl-tRNA synthetase
(TyrRS)1 which is homologous to a tumor-derived cytokine, endothelial and monocyte activating
polypeptide (EMAP-2) has been studied. It was shown that C-domain induced a ~ 2 -fold increase of
monocyte chemotaxis. This effect is comparable with the values of chemotaxis induction by EMAP-2
cytokine and proEMAP-2. The truncated catalytic form of bovine TyrRS (2 χ 39 kDa) has no effect on
monocyte chemotaxis. C-domain of TyrRS also induced a ~ 3-fold increase in tissue factor activity in
cultured human ehdothelial cells. A hypothesis is forwarded that the isolated C-domain of mammalian
TyrRS may be released at proteolytic cleavage of TyrRS by some protease, activated at stress conditions,
and functions as a mediator via signal transduction through interaction with a pu.ative EMAP-2 receptor.
Introduction. Aminoacy l - t RNA s y n t h e t a s e s
(ARSases) of higher eukaryotes usually possess ami-
no- and/or carboxy-terminal polypeptide extensions
of catalytic enzyme core which are dispensable for
their catalytic activities Il—4]. Tlve functions of these
extensions are related to the complex organization of
protein synthesis apparatus of multicellular orga-
nisms. For example, some mammalian ARSases have
abilities to form a multi-tRNA synthetase complex
which includes 9 ARSases and 3 other auxiliary
protein components I l—3]. On other hand, these
appended domains could be responsible for the poly-
anion binding properties of eukaryotic ARSases and
compartmentalization of components of protein syn-
thesis machinery on the ribosomes [4, 5].
Recently the amino acid sequences of bovine and
human TyrRS were determined [6, 7], revealing a
high sequence homology (51 % identity) between the
C-terminal, non-catalytic domain of TyrRS and the
novel cytokine-like molecule endothelial-monocyte-
activating polypeptide (EMAP-2) [6—8 ]. Previously,
we have shown , that bovine tyrosyl-tRNA synthetase
(a2-dimer, 2 χ 59 kDa) could be isolated from bovine
© A l . KORNELYUK, M. P. R. TAS1 A. U DUBROVSKY,
J . C . MURRAY, 1 9 9 9
liver both as the full-length protein and as a pro-
teolyt ical ly-modif ied active enzyme form (2 χ
χ 39 kDa), which lacks its C-terminal polypeptide
extension [9, 10]. Both distinct molecular forms of
TyrRS displayed the similar catalytic constants in
tRNA aminoacylation reaction [9. 101. Moreover, the
dispensable C-terminal polypeptide extension of bovi-
ne TyrRS revealed a significant contribution to the
non-specific affinity of this enzyme for RNA [11].
A novel putative cytokine, EMAP-2, modulates a
variety of properties of endothelial cells, monocytes
and leukocytes in vitro, and induces an acute inflam-
matory reaction in vivo [12, 16]. Based on the
sequence similarity of mammalian TyrRS C-domain
and EMAP-2, we have forwarded the hypothesis thai
the isolated C-domain may also display the cytokine
activity, similar to EMAP-2 cytokine [8 ]. In order to
verify this hypothesis we have cloned and expressed
the isolated non-catalytic C-terminal domain of bovi-
ne TyrRS [17].
In this work we have discovered several cytokine-
like activities of the isolated C-domain of TyrRS in
vitro which are compared with the properties of
recombinant EMAP-2 cytokine.
Materials and Methods. Proteins isolation. Clo-
168
CYTOKINE AC TIVITY OF THE NON CArALYTIC.' EMAP-2-LIKE DOMAIN
ning and bacterial expression of the C-terminal
domain of bovine TyrRS was performed as described
earlier [17]. The BamHI cDNA fragment encoding
residues D322-S528 of bovine TyrRS was cloned into
the pET15h vector for bacterial expression and recom-
binant protein was expressed in BL21(DE3) Esche-
richia coli ceils harboring the pEYCD2 plasmid. The
supernatant was loaded onto Ni-NTA column and
6His-tagged recombinant protein was eluted with
300 mM imidazole.
Recombinant human EMAP-2 and proEMAP-2
were isolated and characterized as previously des-
cribed [18 ].
Monocyte chemotaxis: Freshly-isolated monocy-
tes were then suspended in RPMI-1640 medium with
10 % foetal calf serum, at 2 χ IO6 cells per ml.
Solutions of proteins (TyrRS C-domain, 39 kDa
TyrRS and EMAP-2) or chemotactic peptide, formyl-
methionyl-Ieucyl-phenyalanine (fMLP) (31 μΐ) at the
indicated concentrations were placed in the bottom
wells of ChemTx micro-chemotaxis plates (Neuro
Probe, Inc.) in triplicate. The filter was placed on top
of the solution in such a way as to provide fluid
continuity between the upper and lower chambers. An
aliquot of monocyte suspension (27 μΐ) was then
placed on top of the filter above each well, and the
plates incubated with lids on for 1.5 hr at 37 °С in
air /5 % CO2. After incubation, cells binding to the
membrane were fixed by the addition of 15 μΐ of
ice-cold 20 % formaldehyde in phosphate-buffered
saline, and those that had migrated to the underside
of the membrane were counted with a haemocyto-
meter.
Procoagulant activity assay. Human umbilical vein
endothelial cells (HUVEC) were isolated essentially
by the method of Jaffe et al. [19]. Confluent en-
dothelial monolayers at passages 2 to 3 were used to
assess tissue factor-dependent procoagulant activity
[20 I. Coagulation was initiated by the addition of 100
μ\ of 30 mM CaCl2 solution at 37 °С and the time for
visible fibrin strand/gel formation was determined.
Procoagulant activity of endothelial monolayers was
expressed as tissue factor equivalents (TFE, pg/106
cells) [20].
Results and Discussion. Purification of recom-
binant C-domain of TyrRS, expressed in E. coli cells
after induction by IPTG and containing a 6His-tag,
has been performed by metal-chelation chromato-
graphy. According to gel-electrophoresis data, the
homogeneity of recombinant protein was about 95 %
[17].
Since EMAP-2 cytokine has been shown to indu-
ce migration of monocytes and polymorphonuclear
leukocytes in vitro [12, 18], we therefore examined
the effects of TyrRS C-domain on monocyte migra-
tion, using a micro-chemotaxis chamber assay. The
addition of Ty rRS C-doniain to the lower chamber led
to a ~ 2-fold enhancement of monocyte migration
(Fig. 1). Monocyte migration was induced by C-
domain in the range I pM—10 nM (between 1 ρ M
and 100 pM this increase was significant, p< 0.05) at
levels slightly greater than that induced by recom-
binant EMAP-2 over a similar concentration range,
but not as high as those achieved with 10 nM control
chemotactic peptide fMLP. In contrast to isolated
C-domain, the truncated 39K form of mammalian
TyrRS, which lacks this domain, did not affect
monocyte migration (Fig. 1).
A defining biological activity of EMAP-2 is its
ability to induce tissue-factor-dependent procoagulant
activity on the surface of endothelial cells in vitro, and
furthermore to potentiate procoagulant activiity indu-
ced by tumour necrosis factor (TNF) in vitro (12].
Therefore we studied the abilities of TyrRS C-domain
and EMAP-2 polypeptide to induce tissue factor-
mediated procoagulant activity on the surface of
cultured HUV EC.
The exposure of endothelial cells to isolated
C-domain for 4 hr at concentrations of 1 — KM) pM led
to a dose-dependent increase in cell surface tissue
factor between 0,36 and 0.77 pg TFE/IO6 cells on
endothelial cells (Fig. 2, a). EMAP-2 also induced the
enhancement of tissue factor activity in a dose-de-
pendent manner (Fig. 2, b), but maximum activity
was observed at lower mediator concentration at about
1 pM.
Our data suggest that the isolated C-domain of
mammalian TyrRS reveals cytokine-like activities
both as a chemotactic factor for monocytes and as an
inducer of tissue factor expression on human endo-
thelial cells similar to EMAP-2 cytokine. We propose,
therefore, that the C-domain of TyrRS could poten-
tially mimic the action of EMAP-2 cytokine through
the interactions with complementary sites on the
specific receptor.
Moreover, the cellular effects of TyrRS C-domain
that we have observed, in particular the induction of
tissue factor activity, cannot be fully explained by an
interaction of its N-terminal region with a receptor.
As indicated earlier, the chemotactic and tissue fac-
tor-inducing activity of EMAP-2 are believed to reside
within different regions of the molecule [14]. Since
we have also observed tissue factor induction in
response to the TyrRS C-domain, it is possible that
other functional domains of this C-terminal module,
except its N-terminal region, could be involved in its
cytokine activities.
If the EMAP-2-Ике domain of TyrRS is released
169
KORNELYUK A. I. ET AL.
Fig. 1. Induction of monocytes migration by recombinant C-domain of TyrRS and EMAP-2 proteins as studied by micro-chemotaxis chamber
assay. Cell migration assays were performed as described under «Materials and Methods*. Data shown the standard deviations estimated with
medium aloue control. Chemotactic peptide fMLP was used as a positive control
Fig. 2. Induction of procoagulant activity of tissue factor in human endothelial cells by recombinant C-domain of TyrRS (A) or EMAP-2
cytokine (B). Results are the means of 6 replicates pooled from 2 separate experiments
170
CYTOKJNE ACTIVITY OF THE NON-CATALYTIC EMAP-2-LIKE OOMdlN
after proteolytic cleavage at the loop, connecting the
catalytic 39 kDa enzyme core and this C-domain, it
could be involved as a mediator in signal transduction
process through the interactions with a putative
EMAP-2 receptor. The nature of the EMAP-2 recep-
tor is not known, although cross-linking studies have
demonstrated binding of EMAP-2-derived peptides to
a 73K protein associated with the monocyte cell
surface [21 ], suggesting the existence of a distinct
receptor.
Recently, it was shown that in cultured cells
post-translatiorial processing of proEMAP-2 into ma-
ture cytokine EMAP-2 occurred coincidentally with
apoptosis programmed cell death [22 ]. It is well
known that during apoptosis process some proteases,
e. g. interleukin-1 converting enzyme (ICE, caspase)
are activated [22]. It is possible to propose, that
mammalian TyrRS could be cleaved during apoptotis
proteolytic cascade, or other protease activation pro-
cess.
It is interesting to note, that other component of
protein biosynthesis machinery, auxiliary p43 protein
of multi-synthetase complex, is proposed to be a
precursor of EMAP-2 cytokine [23 ].
Our results suggest a novel non-canonical func-
tion of mammalian aminoacyl-tRNA synthetases in
higher eukaryotic cells, which may be associated with
signal transduction process. Furthermore this function
may only be expressed in conditions where cellular
proteases are activated.
Acknowledgements. This work was supported by
the Cancer Research Campaign and by a Wellcome
Trust Travel Grant to A. I. K.
О. I. Корнелюк, Μ. Tac, О. Л. Дубровський, Дж. К. Мюррей
Цитокінова активність некаталітичного EMAP-2-подібного
домена тирозил-тРНК синтетази ссавців
Резюме
Досліджено цитокінову активність ізольованого рекомбінант-
ного С-кінцевого домена тирозил-тРНК синтетази (тирРС)
ссавців, гомологічного ЕМАР-2 цитокіну. Показано, що С-до-
мен індукує збільшення хемотаксису моноцитів у 2 рази. Цей
ефект близький до такого, спричиненого ЕМАР-2 та
ргоЕМАР-2. Протеолітично модифікована каталітична фор-
ма тирРС (2 χ 39 кДа) не впливала на хемотаксис моноцитів.
С-домен тирРС. також індукує зростання активності тка-
нинного фактора ендотеліальних клітин людини в З рази.
Пропонується гіпотеза стосовно пюго, що ізольований С-до-
мен може вивільнятися при протеолітичному розщепленні
тирРС певною протеазою, яка активується в стресових
умовах, і функціонувати як медіатор шляхом передачі сигналу
при взаємодії з рецептором ЕМАР-2 цитокіну.
А. И. Корнелюк, М. Tac, A. Л. Дубровский, Дж. К. Мюррей
Цитокиновая активность некаталитического EMAP-2-подэбного
домена тирозил-тРНК синтетазы млекопитающих
Резюме
Изучена цитокиновая активность изолированного рекомби-
нантного С-концевого домена тирозил-тРНК синтетазы
(тирРС) млекопитающих, гомологичного ЕМАР-2 цитокину.
Показано, что С-домен индуцирует увеличение хемотаксиса
моноцитов в 2 раза. Этот эффект близок к таковому,
вызываемому ЕМАР-2 и ргоЕМАР-2. Протеолитически моди-
фицированная каталитическая форма тирРС (2 χ 39 к Да) не
влияет на хемотаксис моноцитов. С-домен тирРС также
индуцирует рост активности тканевого фактора эндогпели-
альных клепюк человека в J' раза. Предложена гипотеза отно-
сительно того, что изолированный С-домен может высвобож-
даться при протеолитическом расщеплении тирРС определен-
ной протеазой, активируемой в стрессовых условиях, и функ-
ционировать как медиа/пор путем передачи сигнала при взаи-
модействии с рецептором цитокина ЕМАР-2.
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