Genome-wide Expression Profiling (with Focus on the Galectin Network) in Tumor, Transition Zone and Normal Tissue of Head and Neck Cancer: Marked Differences Between Individual Patients and the Site of Specimen Origin

Živicová, Veronika; Brož, Petr; Fík, Zdeněk; Mifkova, Alzbeta; Plzák, Jan; Čada, Zdeněk; Kaltner, Herbert; Kučerová, Jana; Gabius, Hans‐Joachim; Smetana, Karel

doi:10.21873/anticanres.11565

Cited by 17 publications

(20 citation statements)

References 16 publications

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“…This demonstrates that the present study provides a solid base for further studies on gal-4 functions. Furthermore the presented results illustrate the value of the approach on a proof-of-principle level, encouraging further applications in this field, that is for other galectins and their mixtures that are present (patho)physiologically in colon cancer, for example, also galectins-1, -2, -3, -7, and -8 besides gal-4, detected by network analysis (24,63), and other types of cancer (64).…”

Section: Discussionmentioning

confidence: 55%

Detection of malignancy‐associated phosphoproteome changes in human colorectal cancer induced by cell surface binding of growth‐inhibitory galectin‐4

et al. 2018

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Emerging evidence on efficient tumor growth regulation by endogenous lectins directs interest to determine on a proof‐of‐principle level the range of information on alterations provided by full‐scale analysis using phosphoproteomics. In our pilot study, we tested galectin‐4 (gal‐4) that is a growth inhibitor for colon cancer cells (CRC), here working with the LS 180 line. In order to cover monitoring of short‐ and long‐term effects stable isotope labeling by amino acids in cell culture‐based quantitative phosphoproteomic analyses were conducted on LS 180 cell preparations collected 1 and 72 h after adding gal‐4 to the culture medium. After short‐term treatment, 981 phosphosites, all of them S/T based, were detected by phosphoproteomics. Changes higher than 1.5‐fold were seen for eight sites in seven proteins. Most affected were the BET1 homolog (BET1), whose level of phosphorylation at S50 was about threefold reduced, and centromere protein F (CENPF), extent of phosphorylation at S3119 doubling in gal‐4‐treated cells. Phosphoproteome analysis after 72 h of treatment revealed marked changes at 33 S/T‐based phosphosites from 29 proteins. Prominent increase of phosphorylation was observed for cofilin‐1 at position S3. Extent of phosphorylation of the glutamine transporter SLC1A5 at position S503 was decreased by a factor of 3. Altered phosphorylation of BET1, CENPF, and cofilin‐1 as well as a significant effect of gal‐4 treatment on glutamine uptake by cells were substantiated by independent methods in the Vaco 432, Colo 205, CX 1, and HCT 116 cell lines. With the example of gal‐4 which functions as a tumor suppressor in CRC cells, we were able to prove that cell surface binding of the lectin not only markedly influences the cell proteome, but also has a bearing on malignancy‐associated intracellular protein phosphorylation. These results underscore the potential of this approach to give further work on elucidating the details of signaling underlying galectin‐triggered growth inhibition a clear direction. © 2018 IUBMB Life, 71(3):364–375, 2019

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Section: Discussionmentioning

confidence: 55%

Detection of malignancy‐associated phosphoproteome changes in human colorectal cancer induced by cell surface binding of growth‐inhibitory galectin‐4

et al. 2018

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“…29 Considering initial evidence for functional networking among galectins, it becomes reasonable that upcoming studies proceed with the immunohistochemical analysis of further members of this lectin family (such as Gal-8), at best reaching the level of comprehensive fingerprinting. [45][46][47][48] When setting the distribution profiles of Gal-1 and -3 in relation to tissue degradation, the total scores of immunopositivity significantly correlated with histopathological degeneration and MRI grading. At the level of IVD components, immunopositivity for Gal-1 and -3 at all sites, except for EP and the NP matrix in the case of Gal-1, independently correlated with total histopathological degeneration scores of the specimens.…”

Section: Discussionmentioning

confidence: 99%

“…In rat NP cells, Gal‐3 knock‐down led to increased susceptibility to FasL‐induced cell death, and a functional cooperation between tumor necrosis factor‐α and Gal‐3 on IL‐1β, IL‐6, and CCL2 expression had been reported . Considering initial evidence for functional networking among galectins, it becomes reasonable that upcoming studies proceed with the immunohistochemical analysis of further members of this lectin family (such as Gal‐8), at best reaching the level of comprehensive fingerprinting …”

Section: Discussionmentioning

confidence: 99%

Galectins‐1 and ‐3 in Human Intervertebral Disc Degeneration: Non‐Uniform Distribution Profiles and Activation of Disease Markers Involving NF‐κB by Galectin‐1

Elshamly

Kinslechner

Grohs

et al. 2019

Journal Orthopaedic Research

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Degeneration of the human intervertebral disc (IVD) is assumed to underlie severe clinical symptoms, in particular chronic back pain. Since adhesion/growth‐regulatory galectins are linked to arthritis/osteoarthritis pathogenesis by activating a pro‐degradative/‐inflammatory gene expression signature, we hypothesized a similar functional involvement of galectins in IVD degeneration. Immunohistochemical evidence for the presence of galectins‐1 and ‐3 in IVD is provided comparatively for specimens of spondylochondrosis, spondylolisthesis, and spinal deformity. Immunopositivity was detected in sections of fixed IVD specimens in each cellular compartment with age‐, disease‐, and galectin‐type‐related differences. Of note, presence of both galectins correlated with IVD degeneration, whereas correlation with age was seen only for galectin‐3. In addition, staining profiles for these two galectins showed different distribution patterns in serial sections, an indication for non‐redundant functionalities. In vitro, both galectins bound to IVD cells in a glycan‐dependent manner. However, exclusively galectin‐1 binding triggered a significant induction of functional disease markers (i.e., IL6, CXCL8, and MMP1/3/13) with involvement of the nuclear factor‐kB pathway. This study thus gives direction to further network analyses and functional studies on galectins in IVD degeneration. © 2019 The Authors. Journal of Orthopaedic Research® published by Wiley Periodicals, Inc. on behalf of Orthopaedic Research Society. J Orthop Res 37:2204–2216, 2019

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“…Infrared spectra were recorded on a Bruker Alpha FTIR equipped with a Bruker universal ATR sampling accessory. 1 H and 13 C NMR spectra were recorded on Bruker Avance DPX300 and Bruker Avance 500 Ultrashield spectrometers equipped with QNP 1 H/ 13 C/ 19 F/ 31 P and inverse TBI 1 H/ 31 P/BB probes, respectively. Standard Bruker software was used for acquisition and processing routines.…”

Section: General Methodsmentioning

confidence: 99%

Multivalent Lactose–Ferrocene Conjugates Based on Poly(Amido Amine) Dendrimers and Gold Nanoparticles as Electrochemical Probes for Sensing Galectin-3

Martos-Maldonado

Quesada-Soriano

Garcı́a-Fuentes

et al. 2020

Preprint

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Galectin-3 is considered a cancer biomarker and bioindicator of fibrosis and cardiac remodeling, and, therefore, it is desirable to develop convenient methods for its detection. Herein, an approach based on the development of multivalent electrochemical probes with high galectin-3 sensing abilities is reported. The probes consist of multivalent presentations of lactose-ferrocene conjugates scaffolded on poly(amido amine) (PAMAM) dendrimers and gold nanoparticles. Such multivalent lactose-ferrocene conjugates are synthesized by coupling of azidomethylferrocene-lactose building blocks on alkyne-functionalized PAMAM, for the case of the glycodendrimers, and to disulfide-functionalized linkers that are then used for the surface modification of citrate-stabilized gold nanoparticles. The binding and sensing abilities towards galectin 3 of both ferrocene-containing lactose dendrimers and gold nanoparticles have been evaluated by means of isothermal titration calorimetry, UV-vis spectroscopy, and differential pulse voltammetry. The highest sensitivity by electrochemical methods to galectin-3 was shown by lactosylferrocenylated gold nanoparticles, which are able to detect the lectin in nanomolar concentrations.

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Genome-wide Expression Profiling (with Focus on the Galectin Network) in Tumor, Transition Zone and Normal Tissue of Head and Neck Cancer: Marked Differences Between Individual Patients and the Site of Specimen Origin

Abstract: These results underline special features at each site of specimen origin as well as the importance of analyzing galectins as a network and of defining the expression status of the individual patient prior to reaching clinically relevant conclusions.

Cited by 17 publications

References 16 publications

Detection of malignancy‐associated phosphoproteome changes in human colorectal cancer induced by cell surface binding of growth‐inhibitory galectin‐4

Detection of malignancy‐associated phosphoproteome changes in human colorectal cancer induced by cell surface binding of growth‐inhibitory galectin‐4

Galectins‐1 and ‐3 in Human Intervertebral Disc Degeneration: Non‐Uniform Distribution Profiles and Activation of Disease Markers Involving NF‐κB by Galectin‐1

Multivalent Lactose–Ferrocene Conjugates Based on Poly(Amido Amine) Dendrimers and Gold Nanoparticles as Electrochemical Probes for Sensing Galectin-3

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