Expression of galectin-1 in malignant tumors
Galectin-1 is a 14 kDa lectin expressed ubiquitously in mammalian organism. Since its discovery, the lectin was shown to participate in many cellular processes. Involvement in some of them like induction of apoptosis of activated T cells, mediation of cell adhesion and participation in angiogenesi...
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Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України
2009
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irk-123456789-1357292018-06-16T03:07:33Z Expression of galectin-1 in malignant tumors Demydenko, D. Berest, I. Reviews Galectin-1 is a 14 kDa lectin expressed ubiquitously in mammalian organism. Since its discovery, the lectin was shown to participate in many cellular processes. Involvement in some of them like induction of apoptosis of activated T cells, mediation of cell adhesion and participation in angiogenesis suggest that galectin-1 could be utilized by malignant tumors. Indeed expression of galectin-1 is upregulated in tumors of different origin. Many examples point to its important role in a process of cancer metastasis. This review summarizes the data available to date on galectin-1 expression in human malignancies. 2009 Article Expression of galectin-1 in malignant tumors / D. Demydenko, I. Berest // Experimental Oncology. — 2009. — Т. 31, № 2. — С. 74-79. — Бібліогр.: 74 назв. — англ. 1812-9269 http://dspace.nbuv.gov.ua/handle/123456789/135729 en Experimental Oncology Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України |
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Digital Library of Periodicals of National Academy of Sciences of Ukraine |
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DSpace DC |
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Reviews Reviews Demydenko, D. Berest, I. Expression of galectin-1 in malignant tumors Experimental Oncology |
| description |
Galectin-1 is a 14 kDa lectin expressed ubiquitously in mammalian organism. Since its discovery, the lectin was shown to participate
in many cellular processes. Involvement in some of them like induction of apoptosis of activated T cells, mediation of cell adhesion
and participation in angiogenesis suggest that galectin-1 could be utilized by malignant tumors. Indeed expression of galectin-1 is
upregulated in tumors of different origin. Many examples point to its important role in a process of cancer metastasis. This review
summarizes the data available to date on galectin-1 expression in human malignancies. |
| format |
Article |
| author |
Demydenko, D. Berest, I. |
| author_facet |
Demydenko, D. Berest, I. |
| author_sort |
Demydenko, D. |
| title |
Expression of galectin-1 in malignant tumors |
| title_short |
Expression of galectin-1 in malignant tumors |
| title_full |
Expression of galectin-1 in malignant tumors |
| title_fullStr |
Expression of galectin-1 in malignant tumors |
| title_full_unstemmed |
Expression of galectin-1 in malignant tumors |
| title_sort |
expression of galectin-1 in malignant tumors |
| publisher |
Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України |
| publishDate |
2009 |
| topic_facet |
Reviews |
| url |
http://dspace.nbuv.gov.ua/handle/123456789/135729 |
| citation_txt |
Expression of galectin-1 in malignant tumors / D. Demydenko, I. Berest // Experimental Oncology. — 2009. — Т. 31, № 2. — С. 74-79. — Бібліогр.: 74 назв. — англ. |
| series |
Experimental Oncology |
| work_keys_str_mv |
AT demydenkod expressionofgalectin1inmalignanttumors AT beresti expressionofgalectin1inmalignanttumors |
| first_indexed |
2025-07-09T23:59:40Z |
| last_indexed |
2025-07-09T23:59:40Z |
| _version_ |
1837215864131158016 |
| fulltext |
74 Experimental Oncology 31, 74–79, 2009 (June)
Galectin-1 is one of the most important lectins to
date participating in the malignant tumor development.
With more and more data available on its expression in
tumors it is already clear that this lectin is an important
target for cancer diagnostics and treatment.
Described in the 1980s, galectin-1 was more exten-
sively studied in 1990s. Its first involvement in cancer
was associated with cell adhesion [1]. Later on the lec-
tin was shown to induce apoptosis of activated T-cells
[2], and experiments have confirmed [3] that cancer
cells express galectin-1 also to protect themselves
from immune response. Latest finding is a participation
of galectin-1 in tumor angiogenesis as an angiogenic
factor [4]. Galectin-1 participation in various cellular
processes is well reviewed [5–7].
A purpose of this review was to summarize the data
obtained to date on galectin-1 expression in human
cancers and possibility of its use in diagnostics and
prognosis of the disease outcome. The data is sum-
marized according to tumor origin. The tumor sites are
listed according to the frequency of tumor occurrence
published by American Cancer Society, the Centers for
Disease Control and Prevention, the National Cancer
Institute, and the North American Association of Cent-
ral Cancer Registries [8].
Prostate. Studies of two LNCaP prostate carci-
noma cell line variants as a model of androgen de-
pendent and independent prostate cancer showed
that galectin-1 expression is increased in androgen
independent LNCaP cell line variant [9]. Androgen
dependent LNCaP cell line variant appeared to be sus-
ceptible to galectin-1 induced apoptosis [10]. Pre sence
of core 2N-acetylglucose-aminyl transferase, the en-
zyme which catalyzes addition of polylactose-amine
sequences crucial for galectin-1 binding to O-glycans
on cell surface receptors was crucial for apoptosis of
androgen dependent LNCaP cell line variant induced
by galectin-1 [11]. Increased expression of galectin-1
was observed in stroma of primary prostate carcinoma
samples in comparison to stroma of normal prostate,
and increased galectin-1 expression positively corre-
lated with a poor prognosis of disease outcome [12].
Endothelial cells of capillaries infiltrating to tumor
stroma have strongly increased expression of galec-
tin-1 in comparison to endothelial cells of capillaries in
adjacent normal stroma [13]. Hypothesis of the authors
that carcinoma cells induce galectin-1 expression in en-
dothelial cells was confirmed by incubation of endothe-
lial cells with conditioned media from PC-3 or DU145
prostate carcinoma cells, which significantly increased
galectin-1 expression in endothelial cells. Adhesion
of PC-3 prostate carcinoma cells to endothelial cells
expressing galectin-1 was increased in comparison to
endothelial cells not expressing galectin-1 [13].
Lung. Examination of 159 cases of lung cancer
patient specimens for their capacity to bind galectin-1
demonstrated that patients showing expression of galec-
tin-1 binding sites revealed a better prognosis than those
lacking binding sites or showing a weak reactivity [14].
Galectin-1 protein expression was increased in BEAS
2B (human normal lung epithelial cells) in comparison to
A549 (human malignant lung epithelial cells) [15].
In studies of atypical adenomatous hyperplasia
(AAP) of lung (suggested to develop to peripheral lo-
calized lung carcinomas) alveolar lining cells from AAP
were found to express higher level of galectin-1 and
galectin-1 binding sites. The cells formed spatial clus-
ters. AAP in general was characterized by increased
vascularisation in comparison to normal tissues [16].
Galectin-1 expressing lung tumors where shown to
have poorer prognosis than non expressing ones by
Szoke T. et al. [17, 18].
EXPRESSION OF GALECTIN-1 IN MALIGNANT TUMORS
D. Demydenko*, I. Berest
Department of Molecular Biology, Palladin Institute of Biochemistry
of the National Academy of Sciences of Ukraine, Kiev 01601, Ukraine
Galectin-1 is a 14 kDa lectin expressed ubiquitously in mammalian organism. Since its discovery, the lectin was shown to participate
in many cellular processes. Involvement in some of them like induction of apoptosis of activated T cells, mediation of cell adhesion
and participation in angiogenesis suggest that galectin-1 could be utilized by malignant tumors. Indeed expression of galectin-1 is
upregulated in tumors of different origin. Many examples point to its important role in a process of cancer metastasis. This review
summarizes the data available to date on galectin-1 expression in human malignancies.
Key Words: galectin-1, cancer, cancer prognosis, cancer treatment.
Received: April 24, 2009.
*Correspondence: Fax: +38 (044) 279-63-65
E-mail: d.v.demydenko@gmail.com
Abbreviations used: AAP — atypical adenomatous hyperpla-
sia; C2GnT-I — 2 beta-1,6-N-acetylglucosaminyltransferase;
CD – cluster of differentiation; CRD – carbohydrate recognition
domain; DLBCL — diffuse large B cell lymphoma; FTS — farnesyl-
thiosalicylic acid; GTP – guanosine tri-phosphate; HER2/neu —
Human Epidermal growth factor Receptor 2/neuroglioblastoma;
HL — Hodgkin lymphoma; HMEC — human mammary epithelial
cell; HNSCC — head and neck squamous cell carcinoma; H-Ras –
Harvey sarcoma Ras; ICC — intrahepatic cholangiocarcinoma;
L-PHA – leuko-phytohemagglutinin; MAPK – mitogen activated
protein kinase; MMP — matrix metalloproteinase; mTOR — mam-
malian target of rapamycin; OSCC – oral squamous cell carci-
noma; PLC – phospholipase C; Ras – rat sarcoma; TGF – tumor
growth factor; VEGF – vascular endothelial growth factor.
Exp Oncol 2009
31, 2, 74–79
Experimental Oncology 31, 74–79, 2009 (June) 75
Reduced proliferation accompanied by downregu-
lation of galectin-1 was observed after treatment of
a lung carcinoma cell line A549 with extract of fun-
gus Antrodia camphorata [19]. Galectin-1 was also
identified among secreted proteins from A549 lung
carcinoma cells [20].
Invasiveness of CL1-5 lung adenocarcinoma cell
line was shown to correlate positively with a level of
galectin-1 expression by the cell line [21].
Breast. Galectin-1 is expressed by MDA-MB-435
human breast carcinoma cells and is accumulated in the
contact site between MDA-MB-435 and human umbili-
qual endothelial cells suggesting the role for galectin-1
in adhesion of the breast carcinoma cells [22].
Different breast cancer cell lines express galec-
tin-1 mRNA as it was shown by Lahm et al. [23]. The
overexpresion of proto-oncogene receptor HER2/neu
(Human Epidermal growth factor Receptor 2/ neuro-
glioblastoma) in immortalized human mammary lumi-
nal epithelial cells upregulated expression of 35 genes
including galectin-1 gene [24].
Farnesylthiosalicylic acid (FTS), which blocks the
binding of GTP-H-Ras(12V) to its membrane acceptor
protein, galectin 1, blocks the functionality of Ras and
the activity of mTOR [25]. FTS also effectively inhibits
the proliferation of MCF-7 breast cancer cells in culture
[25]. Since this agent blocks MAPK as well as mTOR,
it may be useful for the prevention of adaptive hyper-
sensitivity and prolongation of the effects of hormonal
therapy in breast cancer.
Galectin-1 expression was detected in both drug-
sensitive MCF-7 and drug-resistant MCF-7/AdrR cells
[26]. Galectin-1 was present in the cytosol, on the
surface of the cells and in the culture media.
Galectin-1 was shown to be a substrate of matrix
metalloproteinase (MMP)-14 expressed by breast
cancer cells [27].
In metastatic mammary adenocarcinoma LM3
and MCF-7 cells galectin-1 expression is increased in
response to treatment with TGF-beta (tumor growth
factor beta) [28]. Galectin-1 was identified as a me-
tastasis associated protein in the studies of two clones
of human breast carcinoma cell line MDA-MB-435
with different metastatic potential [29]. Correlation
between increased expression of galectin-1 in cancer
associated stromal cells and tumor invasiveness was
also shown [30]. Proteomic profiling of seven breast
cancer cell lines (MDA-MB-231 (metastatic), HCC1428,
AU565, MDA-MB-468, SK-BR-3, MCF7 and BT-474)
in compari son to normal human mammary epithelial
cell (HMEC) line demonstrated that galectin-1 is up-
regulated in the metastatic cell line MDA-MB-231 in
comparison to the rest of the cancer cell lines studied
[31].
Colon. Galectin-1 expression was much higher it the
stromal cells of colorectal carcinomas than adenomas and
normal tissue as was it shown by Sanjuan X. et al. [32].
Expression of galectin-1 and its binding sites was
higher in mild dysplasias, severe dysplasias and invasive
carcinomas of the colon than in normal cases [33]. From
four cell lines (HCT-15, LoVo, DLD-1 and CoLo201), only
CoLo201 expressed galectin-1 mRNA and protein. From
the cell lines only DLD-1 was not able to bind galectin-1.
Galectin-1 added to the media had no effect on growth
of the cell lines. The level of galectin-1 expression was
related inversely to the growth rate of HCT-15, LoVo,
DLD-1 and CoLo201 cells xenografted in vivo into nude
mice - the higher was the galectin-1 expression level, the
lower was growth rate of the cells. The influence (inhibi-
tion) of galalectin-1 on migration of HCT-15, LoVo, and
CoLo201 was also shown [33].
Patients with galectin-1 positive colon tumors on
Dukes A (invasion into but not through the bowel wall)
and Dukes B (invasion through the bowel wall but not
involving lymph nodes) stages had shorter survival pe-
riods than those with galectin-1 negative colon tumors
on the same stages [34].
Important role for galectin-1 in adhesion of colon
cancer cell line with metastatic phenotype CoLo 201
was demonstrated [35]. The regulation of adhesion was
dependent on carbohydrate binding ability of galectin-1.
MAPK and PLC inhibitors decreased the adhesion. Intra-
cellular galectin-1 overexpression induced apoptotic cell
death in CoLo 201 cells, while exogenous galectin-1 was
not able to induce apoptosis in these cells [35].
Galectin-1 expression is upregulated in KM12 hu-
man colon carcinoma cell line upon sodium butyrate
treatment [36]. The treatment induces acquisition
of differentiated phenotype by the cell line. There is
an interesting observation that although HCT-116
and HT-29 colon cancer cell lines express galectin-1
mRNA, only HCT-116 cells express the protein [26].
Urinary tract, kidney. Bladder transitional cell
carcinomas were examined for the level of expres-
sion of galectin-1 mRNA [37]. Higher grade tumors
expressed significantly higher levels of galectin-1
mRNA than low grade tumors or the cells of normal
bladder. Western blot and imunohystochemical analy-
sis showed similar results on the protein level.
Galectin-1 expression is upregulated in bladder
cancer tissue in comparison to normal bladder tissue
as it was shown by Sheng K.H. et al. [38].
Galectin-1 mRNA is upregulated in cytoplasm of
parenhimal cells of urothelial tumors, and upregulation
correlates with tumor grading [39].
Lymphoid tissue. Treatment of diffuse large B cell
lymphoma (DLBCL) cell line HBL-2 and Burkitt’s lympho-
ma cell line HBL-8 with neuraminidases, which remove
sialic acid from the cell surface, enhances their adhesion
to galectin-1 [40]. The sialation could have a clinical
outcome since diffuse large B cell lymphoma patients
with sialylated type of leuko-phytohemagglutinin (L-PHA)
reactive oligosaccharides had a poor prognosis.
Upregulation of galectin-1 as well as galectin-1-
binding carbohydrates expression in cutaneous T
cell lymphomas (CTCL) in comparison to pseudolym-
phoma and atopic dermatitis was demonstrated [41].
Chemotherapy with pegylated liposomal doxorubicine
decreased the expression of galectin-1 and galectin-
1-binding carbohydrates in CTCL.
76 Experimental Oncology 31, 74–79, 2009 (June)
CD7– cells of the early stages of cutaneous T cell
lymphoma (Sezary syndrome) were resistant to
galectin-1 induced cell death, what possibly led to
their accumulation at the late stages of the disease
[42]. Although SeAx/i CD7+ cell line was susceptible
to galectin-1 induced apoptosis, CD7+ HH cell line
was not susceptible to galectin-1induced apopotosis
suggesting that altered glycosilation of CD7 was re-
sponsible for this [42]. It was shown that the basis for
resistance to galectin-1 induced cell death in CD7+ HH
cells from mucosis fungoides is in core 2 beta-1,6-N-
acetylglucosaminyltransferase (C2GnT-I) deficiency
[43]. C2GnT-I is the enzyme, which creates core 2
O-glycan ligands for galectin-1.
Galectin-1 was expressed in Hodgkin lymphoma
(HL) cell lines L540, L1236, HDLM2, L428. 26 of 42 ca-
ses of classic HL were positive for galectin-1, whereas
nodular lymphocyte predominant HL was negative
for galectin-1 [44]. High expression of galectin-1 was
associated with male gender, older patients, reduced
CD8+ T cell infiltration at the tumor site, and an impaired
latent membrane protein 1 and 2-specific CD8+ T-cell
responses. Proliferation and interferon-gamma expres-
sion by Epstein — Barr virus-specific T cells was inhibi-
ted by exposure to recombinant galectin-1 in vitro.
Neoplastic Reed–Sternberg (RS) cells of classical
Hodgkin lymphomas (cHL) overexpressed galectin-1.
Galectin-1 was directly involved in maintenance of im-
munosuppressive microenvironment in cHL [3].
Galectin-1 is selectively expressed by malignant RS
cells in > 90% of primary cHLs in contrast to diffuse
large B-cell lymphoma, primary mediastinal large B-
cell lymphoma, and nodular lymphocyte-predominant
Hodgkin lymphoma which do not express the lectin
[45]. The anaplastic large cell lymphomas (ALCL) also
express galectin-1.
Skin. Galectin-1 mediates A375 and A2058 mela-
noma cell lines adhesion to laminin in carbohydrate
dependent fashion [46].
Blocking of galectin-1 expression in vivo stimulates
antitumor immunity and promotes tumor rejection in
a case of melanoma in mice [47].
Pancreas. Significantly higher level of galectin-1
was detected in pancreatic cancer tissue stromal
fibroblasts and extracellular matrix, than in normal
pancreatic tissue [48]. Galectin-1 mRNA and protein
levels were significantly higher in poorly differentiated
tumors than in that of well/moderately differentiated.
Pancreatic cancer metastases showed no galectin-1
expression. Galectin-1 protein was upregulated in
pancreatic ductal adenocarcinoma in comparison to
normal pancreatic tissue [49].
Upper digestive tract. Galectin-1 was upregu-
lated in tongue carcinoma tissues compared to normal
mucosa [50].
The lectin was overexpressed in the tumor-asso-
ciated stroma of the oral squamous cell carcinomas
(OSCC) as well as the invasion front during early oral
carcinogenesis [51]. During the metastasis significant
galectin-1 expression was detected only at the tumor
invasion front. It is suggested that galectin-1 upregula-
tion at the tumor invasion site might be a predictor of
early metastasis in oral carcinogenesis.
Galectin-1 is upregulated in cancer-associated en-
dothelial cells in the specimens of OSCC in comparison
to adjacent nontumor mucosa [52]. It was also demon-
strated that galectin-1 increased the proliferation and
adhesion of endothelial cells (EC), and enhanced EC
cell migration in combination with VEGF.
Invasivness of OSCC cell lines positively correlates
with galectin-1 expression [21]. Decrease of galectin-1
expression in most invasive HSC-3 cell line caused by
siRNA to galectin-1, decreased invasiveness of the cell
line. In contrary, overexpression of galectin-1 in poorly
invasive OEC-M1 cell line increased invasiveness. It
was also shown that in OSCC tissue galectin-1 was
upregulated in metastatic lesions in lymph nodes in
comparison to primary tumor sites.
Epithelial tissues in head and neck squamous cell
carcinomas (HNSCC) exhibited lower amounts of
galectin-1 and their respective binding sites than their
corresponding normal counterparts [53].
Galectin-1 expression is upregulated and secretion
to the media is induced by hypoxia in FaDu cells (cell
line of a squamous cell carcinoma of the hypopha-
rynx) [54]. Staining of tumor tissues from 101 HNSCC
patients showed correlation of expression of galec-
tin-1 and carbonic anhydrase IX (a hypoxia marker).
Galectin-1 and CD3 (T cell marker) staining could be
used in prognostic purposes. Three groups could be
distinguished — favourable (negative to weak galec-
tin-1 staining and strong CD3 staining), intermediate
(strong staining for both markers or negative to weak
staining of both markers) and unfavourable (strong
galectin-1 and negative to weak CD3 staining).
Serum galectin-1 levels are higher in patients with
HNSCC and successful treatment reduces galectin-1 con-
tent in serum as it was shown by Saussez S. et al. [55].
Thyroid gland. Most aggressive and undifferen-
tiated anaplastic thyroid carcinomas consistently exhibi-
ted a marked increase of galectin-1 expression [56].
Thyroid malignancies of epithelial origin (i. e., papil-
lary and follicular carcinomas) and metastatic lymph
nodes from a papillary carcinoma expressed high
levels of galectin-1 [57]. Medullary thyroid carcinomas
had weaker and variable expression of galectin-1.
Benign thyroid adenomas and adjacent normal thyroid
tissue expressed no galectin-1.
Concentration of galectin-1 was increased in the
sera of patients with benign thyroid lesions in compari-
son to healthy individuals [58].
Stomach. Examination of transcription profiling of
metastatic gastric cancer TMC-1 cells and the non-in-
vasive gastric cancer SC-M1 cell showed higher galec-
tin-1 expression in TMC-1 cells suggesting galectin-1
as a metastasis marker in gastric cancer [59].
Brain, nervous system. High galectin-1 mRNA
levels in glioma tissues and glioma cell lines was demon-
strated [60]. High galectin-1 protein content in glioma
tissues was confirmed by immunohisochemistry.
Experimental Oncology 31, 74–79, 2009 (June) 77
Galectin-1 expression is higher in astrocytomas,
anaplastic astrocytomas, glioblastomas in comparison
to pilocytic astrocytomas [61]. All glioblastoma cell
lines examined contained galectin-1.
Expression of galectin-1 was shown in all studied
human glioma types [62]. The level of galectin-1 ex-
pression correlated with the grade only in the group of
astrocytic tumors. Patients with high-grade astrocytic
tumors that had high level of galectin-1 expression,
had shorter survival periods than those with low level
of galectin-1 expression. In human glioblastoma xeno-
grafts, galectin-1 was preferentially expressed in the
more invasive parts of these xenografts. The authors
also showed that migration of U373 astrocytes was
stimulated by galectin-1.
Immunohistochemical analysis of galectin-1 ex-
pression of human U87 and U373 glioblastoma xeno-
grafts from the brains of nude mice showed a higher
level of galectin-1 expression in invasive areas of the
xenografts in comparison to the non-invasive areas
[63]. Galectin-1 added to the culture media increased
cell motility levels of human U87 glioblastoma cells.
Temozolomide (the standard treatment for glioma
patients), increases galectin-1 expression in human
Hs683 glioblastoma cell line, and the reduction of ga-
lectin-1 expression in these cells by siRNA increases
the anti-tumor effects of temozolomide as well as the
other chemotherapeutic agents [64].
Galectin-1 expression in the human glioblastoma
multiforme cell lines positively correlated with migra-
tory abilities and invasiveness [65]. Analysis of human
glioma samples revealed that increased galectin-1 ex-
pression was associated with a higher tumor grade.
Ovary. Examination of galectin-1 expression in
30 human epithelial ovary carcinoma samples by Wes-
tern and Northern blotting and by immunohistoche-
mistry showed that 95% of ovary carcinoma samples
had higher galectin-1 mRNA level and 57% higher
protein level in cancer epithelial cells in comparison
to normal ovary [66]. Higher level of galectin-1 was
detected by immunohistochemistry in stroma of car-
cinomas than in stroma of normal ovary. Galectin-1
protein expression was detected in AZ364, SK-OV-3,
and AZ224 but not in OVCAR-3, AZ419, and AZ382
human ovary carcinoma cell lines. Conditioned media
from AZ364, AZ224, OVCAR-3, AZ382 induced galec-
tin-1 expression in cultured 84BR fibroblasts. Positive
influence of galectin-1 on above mentioned cell lines
adhesion to laminin and fibronectin was also shown.
Liver. Galectin-1 expression was shown by immu-
nohystochemistry in intrahepatic cholangiocarcinoma
(ICC) while no galectin-1 expression was seen in normal
bile ducts [67]. ICC cells with higher galectin-1 expres-
sion level had higher proliferation rate. Galectin-1 was
also strongly expressed in the cancerous stroma of ICC.
Cholangiocarcinoma cell line, CCKS1 expressed galec-
tin-1 in the cytoplasm and secreted to the medium.
Galectin-1 mRNA was upregulated in primary he-
patocellular carcinomas in comparison to non tumor
liver tissues [68].
Myeloid tissue. Galectin-1 is expressed in bone
marrow samples of multiple myeloma patients. The
lectin promotes survival of CD45RA– primary myeloma
cells and myeloma cell lines, while reduces the viable
cell number in CD45RA+ B cell lines [69].
Uterine, cervix. Galectin-1 expression is in-
creased in endometrial cancer cells in comparison to
normal adjacent endometrium [70].
Galectin-1 expression in stromal cells adjacent to
neoplastic endothelia in cervical neoplasias increases
with elevation of histopathologic grade of cervical tis-
sues [71]. Number of samples with strong staining for
galectin-1 increased from low-grade squamous intra-
epithelial lesions to high-grade squamous intraepithelial
lesions and to invasive squamous cell carcinomas.
Galectin-1 binding inhibitors. (E)-methyl
2-phenyl-4-(b-D-galactopyranosyl)-but-2-enoate
15 was shown to be a selective inhibitor of galectin-1
carbohydrate recognition domain (CRD) with inhibitory
potency of 313 μM [72]. Divalent carbamate 19, one of
the 1,4-substituted 1,2,3-triazoles with a Kd value as
low as 3.2 μM for galectin-1, was described by Tejler
et al. [73]. There are also other molecules with inhibi-
tory potency for galectin-1 CRD described by different
groups (not cited due to space restrictions).
Although with most of the binding partners galectin-1
interacts through its CRD, it is worth mentioning that
the lectin also interacts with oncogenic form of H-Ras
(H-Ras(12V)) in complex with GTP, stabilising ancho-
rage of the complex to the membrane and promoting
oncogenic transformation by activated H-Ras(12V). This
interaction is blocked by farnesylthiosalicylic acid [74].
CONCLUDING REMARKS
In most of the cases described, galectin-1 is up-
regulated in tumors in comparison to normal tissue.
Moreover, the presence of the lectin is associated with
metastases and poor prognosis of disease outcome.
Taking all above mentioned into account, the use of
galectin-1 detection for diagnostics of cancer should
be promoted and use of galectin-1 inhibitors as well
as siRNA in combination with other antitumor agents
should be considered. It is necessary to note that the
expression of galectin-1 on mRNA level is not always
accompanied by protein expression [26].
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