FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ
Background. Chronic myeloid leukemia (CML) develops as a result of the appearance of the oncoprotein BCR-ABL, which, due to its tyrosine kinase activity, leads to abnormal cellular signal transduction and blast transformation. fNBP1 is a protein involved in cytoskeletal remodeling, endocytosis, phag...
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Experimental Oncology| _version_ | 1868113233287577601 |
|---|---|
| author | Antonenko, S. Gurianov, D. Kravchuk, I. Tesliuk, M. Telegeev, G. |
| author_facet | Antonenko, S. Gurianov, D. Kravchuk, I. Tesliuk, M. Telegeev, G. |
| author_institution_txt_mv | [
{
"author": "S. Antonenko",
"institution": "Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, Kyiv, Ukraine"
},
{
"author": "D. Gurianov",
"institution": "Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, Kyiv, Ukraine"
},
{
"author": "I. Kravchuk",
"institution": "Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, Kyiv, Ukraine"
},
{
"author": "M. Tesliuk",
"institution": "Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, Kyiv, Ukraine"
},
{
"author": "G. Telegeev",
"institution": "Institute of Molecular Biology and Genetics of the National Academy of Sciences of Ukraine, Kyiv, Ukraine"
}
] |
| author_sort | Antonenko, S. |
| baseUrl_str | https://exp-oncology.com.ua/index.php/Exp/oai |
| collection | OJS |
| datestamp_date | 2026-06-15T10:40:15Z |
| description | Background. Chronic myeloid leukemia (CML) develops as a result of the appearance of the oncoprotein BCR-ABL, which, due to its tyrosine kinase activity, leads to abnormal cellular signal transduction and blast transformation. fNBP1 is a protein involved in cytoskeletal remodeling, endocytosis, phagocytosis, and cell migration, but its functional role in the development of CML is unclear. Aim. to investigate the spatial relationship between fNBP1 and the BCR-ABL oncoprotein in CML cells and to assess the potential involvement of fNBP1 in BCR-ABL-related signaling networks. Materials and Methods. The subcellular localization of fNBP1 and BCR-ABL was studied using immunofluorescence staining followed by confocal microscopy in K562 cells. The obtained images were processed and analyzed using fiji software. The bioinformatic analysis of the fNBP1 expression in different cancer types was performed using the GEPIA platform. Results. The bioinformatic analysis revealed a heterogeneous regulation of the fNBP1 expression in vari- ous malignancies, with the largest increase observed in leukemia. A cytoplasmic punctate distribution of fNBP1 was shown in K562 cells. Partial colocalization between fNBP1 and BCR-ABL was found predominantly in the peripheral cytoplasmic regions. Conclusions. The observed common spatial distribution of fNBP1 and BCR-ABL enhances the understanding of this protein complex’s formation, suggesting a potential role for fNBP1 in CML development. |
| doi_str_mv | 10.15407/exp-oncology.2026.01.040 |
| first_indexed | 2026-06-15T01:00:28Z |
| format | Article |
| fulltext |
40 ISSN 1812-9269. Experimental Oncology 48 (1). 2026
SHORT COMMUNICATION
C i t a t i o n: Antonenko S, Gurianov D, Kravchuk I, Tesliuk M, Telegeev G. FNBP1 in chronic myeloid leukemia: Spatial
association with BCR-ABL and potential implications for targeted therapy. Exp Oncol. 2026; 48(1): 40-45. https://doi.
org/10.15407/exp-oncology.2026.01.040
© PH “Akademperiodyka” of the NAS of Ukraine, 2026. This is an open access article under the CC BY-NC-ND license
(https://creativecommons.org/licenses/by-nc-nd/4.0/)
Chronic myeloid leukemia (CML) is a clonal hema-
topoietic malignancy characterized by the presence
of the Philadelphia (Ph) chromosome, which arises
from the reciprocal chromosomal translocation
t(9;22)(q34;q11) [1, 2]. This genetic rearrangement
results in the formation of the BCR-ABL fusion gene,
encoding a constitutively active tyrosine kinase,
which serves as the principal molecular driver of
leukemogenesis. The BCR-ABL oncoprotein aber-
rantly phosphorylates numerous downstream sub-
strates, leading to the dysregulation of the key signal-
ing pathways controlling cell proliferation, survival,
and differentiation, thereby promoting the malig-
nant transformation of hematopoietic stem cells [3—
6]. The treatment of CML is primarily based on ty-
rosine kinase inhibitors (TKIs), including imatinib
https://doi.org/10.15407/exp-oncology.2026.01.040
S. Antonenko *, D. Gurianov,
I. Kravchuk, M. Tesliuk, G. Telegeev
Institute of Molecular Biology and Genetics of
the National Academy of Sciences of Ukraine, Kyiv, Ukraine
* Correspondence: E-mail: antonenkoimbg@gmail.com
FNBP1 in Chronic Myeloid Leukemia:
Spatial Association with BCR-ABL
and Potential Implications
for Targeted Therapy
Background. Chronic myeloid leukemia (CML) develops as a result of the appearance of the oncoprotein BCR-ABL,
which, due to its tyrosine kinase activity, leads to abnormal cellular signal transduction and blast transformation. FNBP1
is a protein involved in cytoskeletal remodeling, endocytosis, phagocytosis, and cell migration, but its functional role
in the development of CML is unclear. Aim. To investigate the spatial relationship between FNBP1 and the BCR-ABL
oncoprotein in CML cells and to assess the potential involvement of FNBP1 in BCR-ABL-related signaling networks.
Materials and Methods. The subcellular localization of FNBP1 and BCR-ABL was studied using immunofluorescence
staining followed by confocal microscopy in K562 cells. The obtained images were processed and analyzed using Fiji
software. The bioinformatic analysis of the FNBP1 expression in different cancer types was performed using the GEPIA
platform. Results. The bioinformatic analysis revealed a heterogeneous regulation of the FNBP1 expression in vari-
ous malignancies, with the largest increase observed in leukemia. A cytoplasmic punctate distribution of FNBP1 was
shown in K562 cells. Partial colocalization between FNBP1 and BCR-ABL was found predominantly in the peripheral
cytoplasmic regions. Conclusions. The observed common spatial distribution of FNBP1 and BCR-ABL enhances the
understanding of this protein complex’s formation, suggesting a potential role for FNBP1 in CML development.
Keywords: chronic myeloid leukemia, BCR-ABL, FNBP1, tyrosine kinase, BCR-ABL/FNBP1 colocalization.
ISSN 1812-9269. Experimental Oncology 48 (1). 2026 41
Fnbp1 in Chronic Myeloid Leukemia: Spatial Association with BCR-ABL and Potential Implications
and its derivatives. However, the long-term thera-
peutic efficacy of imatinib is frequently limited due
to the development of drug resistance, which com-
monly arises from mutations within the BCR-ABL
kinase domain [4, 7—9]. These limitations highlight
the need to identify the additional molecular targets
involved in CML pathogenesis and to develop novel
therapeutic strategies [1, 4, 10].
Formin-binding protein 1 (FNBP1), also known
as formin-binding protein 17 (FBP17), belongs to
the F-BAR/EFC protein family, which is widely ex-
pressed in eukaryotic cells [11, 12]. FNBP1 is in-
volved in multiple cellular processes, including cy-
toskeletal remodeling, endocytosis, phagocytosis,
and cell migration, the dysregulation of which may
contribute to malignant transformation [13—17]. In
our previous studies, FNBP1 has been identified as
a novel interacting partner of BCR-ABL [18, 19].
However, despite the well-established role of FNBP1
in membrane dynamics and cytoskeletal organiza-
tion, its potential involvement in BCR-ABL-associ-
ated signaling networks remains largely unexplored.
In this study, we have analyzed the spatial rela-
tionship between FNBP1 and BCR-ABL proteins in
CML cells and compared these patterns with the dis-
tribution of FNBP1 and BCR in an alternative cellu-
lar model. Investigating the spatial arrangement of
proteins involved in BCR-ABL signaling provides
insight into the molecular mechanisms driving CML
and may facilitate identification of the novel regula-
tory factors with potential therapeutic relevance.
Materials and Methods
Cell culture. K562 and J774 cells were obtained
from the Bank of Cell Lines from Human and Ani
mal Tissues of the R.E. Kavetsky Institute of Ex-
perimental Pathology, Oncology and Radiobiology
of the National Academy of Sciences of Ukraine.
K562 cells were cultured in RPMI-1640 medium
(Thermo Fisher Scientific) supplemented with 10%
fetal bovine serum (FBS, Sigma-Aldrich), penicillin
(50 U/mL), and streptomycin (100 μg/mL). J774
cells were cultured in DMEM (Thermo Fisher Sci-
entific) supplemented with 10% FBS (Sigma-Al-
drich), penicillin (50 U/mL), and streptomycin
(100 μg/mL). Cell cultures were maintained in a
humidified incubator at 37 °C with 5% CO2. The
cells were subjected to immunofluorescence analy-
sis upon reaching 80% confluency.
Immunofluorescence analysis. K562 cells were
fixed with 4% paraformaldehyde in PBS containing
0.2% Triton X-100 for 20 min to preserve cellular ar-
chitecture and permeabilize membranes. Non-specif-
ic binding sites were blocked with 2% BSA in PBS for
1 h at room temperature. Cells were subsequently in-
cubated with primary anti-FBP17 (Santa Cruz Bio-
technology, USA) and anti-Bcr-Abl (Thermo Fisher
Scientific, USA) antibodies for 1 h at room tempera-
ture. After washing, samples were incubated with the
secondary antibodies conjugated to DyLight 550 and
DyLight 488 (Thermo Fisher Scientific, USA) for 1 h
in the dark to prevent photobleaching. Nuclear DNA
was counterstained with DAPI for 2 min. To preserve
fluorescence and stabilize the specimens for imaging,
the slides were mounted using CitiFluor™ AF1 mount-
ing medium (Science Services, Germany).
Confocal microscopy. Fluorescent imaging was
performed using a confocal laser scanning system
from Leica Microsystems (Germany) with a 90× oil
immersion objective (NA 1.3). The excitation and
emission settings were individually optimized with
the Leica LAS X software to minimize the cross-ex-
citation and fluorescence signal bleed-through.
Bioinformatic analysis. The analysis of FBP17
expression across different cancer types was per-
formed using the GEPIA platform, which inte-
grates transcriptomic data from The Cancer Ge-
nome Atlas (TCGA) and Genotype-Tissue Expres-
sion (GTEx) databases — http://gepia.cancer-pku.
cn/detail.php?gene=FNBP1.
Image analysis. The quantitative analysis of co-
localization was performed using the Fiji software
and the JaCOP plugin [20]. Automated Costes
thresholding was applied for the Pearson correla-
tion coefficient [21]. For Manders M1 and M2,
a coefficient threshold was selected manually only
to include pixels relevant to the cell region of inter-
est and exclude the background [22].
Results and Discussion
The analysis of FNBP1 expression across different
cancer types, performed using the GEPIA platform,
revealed marked variability in FNBP1 expression
among the tumors compared to their corresponding
normal tissues, suggesting a potential association
with oncogenesis or tumor progression (Fig. 1, a).
The elevated FNBP1 expression was observed in se
veral malignancies, including diffuse large B-cell
42 ISSN 1812-9269. Experimental Oncology 48 (1). 2026
S. Antonenko, D. Gurianov, I. Kravchuk, M. Tesliuk, G. Telegeev
lymphoma, pancreatic adenocarcinoma, pheochro-
mocytoma and paraganglioma, and thymoma. The
most pronounced increase in FBP17 expression was
observed in acute myeloid leukemia, where its level
was tenfold higher than in normal hematopoietic
cells, representing the highest differential expression
among all analyzed malignancies. This hyperexpres-
sion may indicate a leukemia-specific regulatory role
of FNBP1 in cytoskeletal remodeling or intracellular
signaling pathways. Notably, in many other cancer
types, the FBP17 expression was reduced compared
to normal tissues, including bladder urothelial car-
cinoma, cervical squamous cell carcinoma and en-
docervical adenocarcinoma, colon adenocarcinoma,
lung adenocarcinoma, lung squamous cell carcino-
ma, prostate adenocarcinoma, rectal adenocarcino-
ma, sarcoma, cutaneous melanoma, thyroid carci-
noma, uterine corpus endometrial carcinoma, and
uterine carcinosarcoma. In other malignancies, the
differences in the FNBP1 expression between tumor
and normal tissues were relatively modest.
Overall, this analysis demonstrates heterogeneous
regulation of the FNBP1 expression across different
malignancies, indicating a context-dependent role
of this protein in tumor biology. These findings
highlight the importance of further investigating
FNBP1-mediated signaling networks, particularly in
hematological malignancies, including CML.
Our previous studies identified FNBP1 as one of
the interacting partners of the BCR-ABL oncopro-
tein [18, 19]; however, the mechanism underlying
the formation of this protein complex remained un-
clear. To further study the molecular mechanisms of
the interaction between these target proteins, we in-
vestigated their subcellular localization in K562 cells
using an immunofluorescence analysis followed by
confocal microscopy (Fig. 2, a). FNBP1 exhibited a
cytoplasmic distribution characterized by discrete
punctate structures. The merged images revealed the
regions of the partial overlap between the fluores-
cence signals of FNBP1 and BCR-ABL. These colo-
calization sites were predominantly detected in pe-
ripheral cytoplasmic regions, as was demonstrated
by a multichannel pixel intensity plot profile in a se-
lected region of interest (Fig. 2, b), suggesting the site
of FNBP1/BCR-ABL complex formation and indi-
cating the potential involvement of these proteins in
the shared signaling networks and intracellular com-
Fig. 1. The role of FNBP1 in cancer. FNBP1 expression in normal samples (gray box) and tumor samples (red box) from
patients with cancer compiled with GEPIA data from the Cancer Genome Atlas and the Genotype Tissue Expression da-
tabases. ACC — adrenocortical carcinoma, BLCA — bladder urothelial carcinoma, BRCA — breast invasive carcinoma,
CESC — cervical squamous cell carcinoma and endocervical adenocarcinoma, CHOL — cholangiocarcinoma, COAD —
colon adenocarcinoma, DLBC — diffuse large B-cell lymphoma, ESCA — esophageal carcinoma, GBM — glioblastoma
multiforme, HNSC — head and neck squamous cell carcinoma, KICH — kidney chromophobe carcinoma, KIRC — renal
clear cell carcinoma, KIRP — renal papillary cell carcinoma, LAML — acute myeloid leukemia, LGG — low grade glioma,
LIHC — hepatocellular carcinoma, LUAD — lung adenocarcinoma, LUSC — lung squamous cell carcinoma, OV — ovar-
ian serous cystadenocarcinoma, PAAD — pancreatic adenocarcinoma, PCPG — pheochromocytoma and paraganglioma,
PRAD — prostate adenocarcinoma, READ — rectal adenocarcinoma, SARC — sarcoma, SKCM — cutaneous melanoma,
STAD — stomach adenocarcinoma, TGCT — testicular germ cell tumors, THCA — thyroid carcinoma, THYM — thy-
moma, UCEC — uterine corpus endometrial carcinoma, UCS — uterine carcinosarcoma
ISSN 1812-9269. Experimental Oncology 48 (1). 2026 43
Fnbp1 in Chronic Myeloid Leukemia: Spatial Association with BCR-ABL and Potential Implications
partments, A quantitative image analysis was per-
formed using the Pearson correlation coefficient and
the Manders overlap coefficient (Fig. 2, c).
Our previous studies demonstrated the coloca
lization of FNBP1 and BCR during phagocytosis in
J774 cells [18]. A comparative analysis of these re-
sults with the data obtained for K562 cells (Table)
showed that the incorporation of BCR into the
BCR-ABL oncogenic protein is accompanied by a
change in the pattern of its spatial association with
FNBP1, which may reflect the reorganization of the
intracellular signaling networks in leukemic cells.
In particular, a reduced correlation was found be-
tween FNBP1 and BCR-ABL compared to BCR.
There was also a marked reduction in the M1 coef-
ficient (the overlap of BCR-ABL with FNBP1) com-
FNBP1
а
b c
0.1 0.2 0.3 0.4 0.5 0.6 0.7
0.9
0.6
0.4
0.2
0
Pi
xe
l i
nt
en
sit
y v
alu
e,
a.u
.
Pearson
Fig. 2. Colocalization of FNBP1 with BCR-ABL in K562 cells. a — confocal images of cells stained for FNBP1 (green) and
BCR-ABL (red). Nuclei are counterstained with DAPI (blue). The overlap of the localization signals is seen (yellow); b —
the multichannel plot profile of the overlapping localization signals of BCR-ABL and FNBP1 inside the region of interest
(Fig. 2, a). The Y axis indicates pixel intensity values for each channel; the X axis indicates distance in microns for the selected
area (Fig 2, a); c — the quantitative analysis of BCR-ABL and FNBP1 colocalization
44 ISSN 1812-9269. Experimental Oncology 48 (1). 2026
S. Antonenko, D. Gurianov, I. Kravchuk, M. Tesliuk, G. Telegeev
pared to the BCR/FNBP1 pair in J774 cells, which
is explained by the fact that only a relatively small
fraction of the total BCR-ABL pool associates with
FNBP1. It should be emphasized that the expres-
sion level of FNBP1 in K562 cells is relatively low
compared to J774 cells. The reduced amount of this
adaptor protein potentially limits the proportion of
BCR-ABL molecules that are able to participate in
co-protein complexes, which is consequently re-
flected in the decrease in the M1 coefficient value.
Another factor that may contribute to this differ-
ence is the distinct cellular context and functional
roles of these proteins. In macrophages, FNBP1 is in-
volved in membrane remodeling and actin cytoskel-
eton dynamics during phagocytosis, a process that is
likely facilitated by its interaction with BCR. In K562
leukemia cells, the constitutively active BCR-ABL ki-
nase is involved in multiple oncogenic signaling path-
ways and is distributed across different intracellular
compartments. As a result, only a fraction of the BCR-
ABL molecules can colocalize with membrane struc-
tures or endocytic domains containing FNBP1.
At the same time, the M2 coefficient (overlap of
FNBP1 with BCR-ABL) remained high, indicating that
a significant portion of FNBP1 is spatially associated
with both BCR and BCR-ABL, which may indicate an
important role of BCR in the FNBP1 function.
Taken together, these data support the existence of
a partial spatial association between FNBP1 and BCR-
ABL in leukemic cells while suggesting that the inter-
action occurs in specific cytoplasmic microdomains
rather than throughout the entire BCR-ABL pool.
Such a compartmentalized colocalization is consistent
with the proposed role of FNBP1 as a membrane-as-
sociated adaptor protein involved in actin remodeling
and vesicular trafficking, processes which may con-
tribute to the spatial regulation of BCR-ABL signal-
ing. Thus, the identification of BCR-ABL–associated
signaling networks is essential for understanding the
molecular mechanisms underlying CML pathogene-
sis and may provide a rationale for the development
of novel therapeutic strategies targeting specific pro-
tein complexes formed by this oncoprotein.
Funding
This work was supported by the Simons Founda-
tion: Award ID: SFI-PD-Ukraine-00017453.
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Protein
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Coefficients
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М1: BCR/BCR-ABL
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Submitted: March 16, 2026
С. Антоненко, Д. Гур’янов, І. Кравчук, М. Теслюк, Г. Телегєєв
Інститут молекулярної біології і генетики
Національної академії наук України, Київ, Україна
FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ:
ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ
МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ
Стан питання. Хронічна мієлоїдна лейкемія (ХМЛ) розвивається в результаті появи онкопротеїну BCR-ABL,
який завдяки своїй тирозинкіназній активності призводить до порушення передачі клітинних сигналів та бласт-
ної трансформації. FNBP1 — це білок, який бере участь у ремоделюванні цитоскелета, ендоцитозі, фагоцитозі
та міграції клітин, але його функціональну роль у розвитку ХМЛ не з’ясовано. Мета. Дослідити просторовий
зв›язок між FNBP1 та онкопротеїном BCR-ABL у клітинах ХМЛ та оцінити потенційну участь FNBP1 у сигнальних
мережах, пов’язаних з BCR-ABL. Матеріали та методи. Субклітинну локалізацію FNBP1 та BCR-ABL вивчали за
допомогою імунофлуоресцентного аналізу з подальшою конфокальною мікроскопією в клітинах K562. Отримані
зображення обробляли та аналізували за допомогою програмного забезпечення Fiji. Біоінформатичний аналіз
експресії FNBP1 у різних типах раку проводили за допомогою платформи GEPIA. Результати. Біоінформатичний
аналіз виявив гетерогенну регуляцію експресії FNBP1 у різних злоякісних новоутвореннях, причому найбільш
виражене збільшення спостерігалося при лейкемії. У клітинах K562 було показано цитоплазматичний точковий
розподіл FNBP1. Часткова колокалізація між FNBP1 та BCR-ABL була виявлена переважно в периферичних ци-
топлазматичних ділянках. Висновки. Виявлений спільний просторовий розподіл FNBP1 та BCR-ABL покращує
розуміння формування цього білкового комплексу та свідчить про потенційну роль FNBP1 у розвитку ХМЛ.
Ключові слова: хронічна мієлоїдна лейкемія (ХМЛ), BCR-ABL, FNBP1, тирозинкіназа, колокалізація BCR-
ABL/FNBP1.
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| id | oai:ojs2.ex.aqua-time.com.ua:article-616 |
| institution | Experimental Oncology |
| keywords_txt_mv | keywords |
| language | English |
| last_indexed | 2026-06-16T01:00:10Z |
| publishDate | 2026 |
| publisher | PH Akademperiodyka |
| record_format | ojs |
| resource_txt_mv | exp-oncologycomua/c3/6d73daa5b8059a563829a541290350c3.pdf |
| spelling | oai:ojs2.ex.aqua-time.com.ua:article-6162026-06-15T10:40:15Z FNBP1 in Chronic Myeloid Leukemia: Spatial Association with BCR-ABL and Potential Implications for Targeted Therapy FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ Antonenko, S. Gurianov, D. Kravchuk, I. Tesliuk, M. Telegeev, G. хронічна мієлоїдна лейкемія (ХМЛ), BCR-ABL, fNBP1, тирозинкіназа, колокалізація BCR- ABL/fNBP1 chronic myeloid leukemia, BCR-ABL, fNBP1, tyrosine kinase, BCR-ABL/fNBP1 colocalization Background. Chronic myeloid leukemia (CML) develops as a result of the appearance of the oncoprotein BCR-ABL, which, due to its tyrosine kinase activity, leads to abnormal cellular signal transduction and blast transformation. fNBP1 is a protein involved in cytoskeletal remodeling, endocytosis, phagocytosis, and cell migration, but its functional role in the development of CML is unclear. Aim. to investigate the spatial relationship between fNBP1 and the BCR-ABL oncoprotein in CML cells and to assess the potential involvement of fNBP1 in BCR-ABL-related signaling networks. Materials and Methods. The subcellular localization of fNBP1 and BCR-ABL was studied using immunofluorescence staining followed by confocal microscopy in K562 cells. The obtained images were processed and analyzed using fiji software. The bioinformatic analysis of the fNBP1 expression in different cancer types was performed using the GEPIA platform. Results. The bioinformatic analysis revealed a heterogeneous regulation of the fNBP1 expression in vari- ous malignancies, with the largest increase observed in leukemia. A cytoplasmic punctate distribution of fNBP1 was shown in K562 cells. Partial colocalization between fNBP1 and BCR-ABL was found predominantly in the peripheral cytoplasmic regions. Conclusions. The observed common spatial distribution of fNBP1 and BCR-ABL enhances the understanding of this protein complex’s formation, suggesting a potential role for fNBP1 in CML development. Стан питання. Хронічна мієлоїдна лейкемія (ХМЛ) розвивається в результаті появи онкопротеїну BCR-ABL, який завдяки своїй тирозинкіназній активності призводить до порушення передачі клітинних сигналів та бласт- ної трансформації. fNBP1 — це білок, який бере участь у ремоделюванні цитоскелета, ендоцитозі, фагоцитозі та міграції клітин, але його функціональну роль у розвитку ХМЛ не з’ясовано. Мета. Дослідити просторовий зв›язок між fNBP1 та онкопротеїном BCR-ABL у клітинах ХМЛ та оцінити потенційну участь fNBP1 у сигнальних мережах, пов’язаних з BCR-ABL. Матеріали та методи. Субклітинну локалізацію fNBP1 та BCR-ABL вивчали за допомогою імунофлуоресцентного аналізу з подальшою конфокальною мікроскопією в клітинах K562. Отримані зображення обробляли та аналізували за допомогою програмного забезпечення fiji. Біоінформатичний аналіз експресії fNBP1 у різних типах раку проводили за допомогою платформи GEPIA. Результати. Біоінформатичний аналіз виявив гетерогенну регуляцію експресії fNBP1 у різних злоякісних новоутвореннях, причому найбільш виражене збільшення спостерігалося при лейкемії. У клітинах K562 було показано цитоплазматичний точковий розподіл fNBP1. Часткова колокалізація між fNBP1 та BCR-ABL була виявлена переважно в периферичних ци- топлазматичних ділянках. Висновки. Виявлений спільний просторовий розподіл fNBP1 та BCR-ABL покращує розуміння формування цього білкового комплексу та свідчить про потенційну роль fNBP1 у розвитку ХМЛ. PH Akademperiodyka 2026-06-14 Article Article application/pdf https://exp-oncology.com.ua/index.php/Exp/article/view/616 10.15407/exp-oncology.2026.01.040 Experimental Oncology; Vol. 48 No. 1 (2026): Experimental Oncology; 40-45 Експериментальна онкологія; Том 48 № 1 (2026): Експериментальна онкологія; 40-45 2312-8852 1812-9269 10.15407/exp-oncology.2026.01 en https://exp-oncology.com.ua/index.php/Exp/article/view/616/461 Copyright (c) 2026 Experimental Oncology https://creativecommons.org/licenses/by-nc-nd/4.0/ |
| spellingShingle | хронічна мієлоїдна лейкемія (ХМЛ) BCR-ABL fNBP1 тирозинкіназа колокалізація BCR- ABL/fNBP1 Antonenko, S. Gurianov, D. Kravchuk, I. Tesliuk, M. Telegeev, G. FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ |
| title | FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ |
| title_alt | FNBP1 in Chronic Myeloid Leukemia: Spatial Association with BCR-ABL and Potential Implications for Targeted Therapy |
| title_full | FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ |
| title_fullStr | FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ |
| title_full_unstemmed | FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ |
| title_short | FNBP1 ПРИ ХРОНІЧНІЙ МІЄЛОЇДНІЙ ЛЕЙКЕМІЇ: ПРОСТОРОВА АСОЦІАЦІЯ З BCR-ABL ТА ПОТЕНЦІЙНІ МОЖЛИВОСТІ ДЛЯ ТАРГЕТНОЇ ТЕРАПІЇ |
| title_sort | fnbp1 при хронічній мієлоїдній лейкемії: просторова асоціація з bcr-abl та потенційні можливості для таргетної терапії |
| topic | хронічна мієлоїдна лейкемія (ХМЛ) BCR-ABL fNBP1 тирозинкіназа колокалізація BCR- ABL/fNBP1 |
| topic_facet | хронічна мієлоїдна лейкемія (ХМЛ) BCR-ABL fNBP1 тирозинкіназа колокалізація BCR- ABL/fNBP1 chronic myeloid leukemia BCR-ABL fNBP1 tyrosine kinase BCR-ABL/fNBP1 colocalization |
| url | https://exp-oncology.com.ua/index.php/Exp/article/view/616 |
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