Adhesion/growth-regulatory galectins in the human eye: localization profiles and tissue reactivities as a standard to detect disease-associated alterations

Schlötzer‐Schrehardt, Ursula; André, Sabine; Janko, Christina; Kaltner, Herbert; Kopitz, Jürgen; Gabius, Hans‐Joachim; Herrmann, Martin

doi:10.1007/s00417-012-2021-9

Cited by 21 publications

(13 citation statements)

References 49 publications

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“…Recently this peptide was also identified in tear fluid [27]. Galectin-1 is an example of a protein with potential adhesion/growth regulatory functions in the eye [28], but has not been annotated as a plasma protein. Lengsin is an eye lens-specific member of the glutamine synthetase superfamily [29].…”

Section: Discussionmentioning

confidence: 99%

In-depth mass spectrometric mapping of the human vitreous proteome

et al. 2013

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Mapping of proteins involved in normal eye functions is a prerequisite to identify pathological changes during eye disease processes. We therefore analysed the proteome of human vitreous by applying in-depth proteomic screening technologies. For ethical reasons human vitreous samples were obtained by vitrectomy from “surrogate normal patients” with epiretinal gliosis that is considered to constitute only negligible pathological vitreoretinal changes. We applied different protein prefractionation strategies including liquid phase isoelectric focussing, 1D SDS gel electrophoresis and a combination of both and compared the number of identified proteins obtained by the respective method. Liquid phase isoelectric focussing followed by SDS gel electrophoresis increased the number of identified proteins by a factor of five compared to the analysis of crude unseparated human vitreous. Depending on the prefractionation method proteins were subjected to trypsin digestion either in-gel or in solution and the resulting peptides were analysed on a UPLC system coupled online to an LTQ Orbitrap XL mass spectrometer. The obtained mass spectra were searched against the SwissProt database using the Mascot search engine. Bioinformatics tools were used to annotate known biological functions to the detected proteins. Following this strategy we examined the vitreous proteomes of three individuals and identified 1111 unique proteins. Besides structural, transport and binding proteins, we detected 261 proteins with known enzymatic activity, 51 proteases, 35 protease inhibitors, 35 members of complement and coagulation cascades, 15 peptide hormones, 5 growth factors, 11 cytokines, 47 receptors, 30 proteins of visual perception, 91 proteins involved in apoptosis regulation and 265 proteins with signalling activity. This highly complex mixture strikingly differs from the human plasma proteome. Thus human vitreous fluid seems to be a unique body fluid. 262 unique proteins were detected which are present in all three patient samples indicating that these might represent the constitutive protein pattern of human vitreous. The presented catalogue of human vitreous proteins will enhance our understanding of physiological processes in the eye and provides the groundwork for future studies on pathological vitreous proteome changes.

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Section: Discussionmentioning

confidence: 99%

In-depth mass spectrometric mapping of the human vitreous proteome

et al. 2013

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“…Starting a respective line of research in glycobiology, galectin-3 (gal-3, also referred to as Mac-2 antigen), which is a member of the galectin family and known as potent effector in growth, immune regulation and cell adhesion (Barondes 1997;Kaltner and gabius 2012;liu et al 2012;Vasta et al 2012;Smetana et al 2013;gabius and Kayser 2014), has previously been revealed to be more than a bystander in Oa (reboul et al 2004). gal-3, which is reactive with glycans on cell surfaces or in the extracellular matrix and with intracellular proteins such as bcl-2 (Krzeminski et al 2011;Dawson et al 2013), was first implied to prolong chondrocyte survival in mice by acting within cells (Colnot et al 1999(Colnot et al , 2001.…”

Section: Introductionmentioning

confidence: 99%

Human osteoarthritic knee cartilage: fingerprinting of adhesion/growth-regulatory galectins in vitro and in situ indicates differential upregulation in severe degeneration

Toegel

Bieder

André

et al. 2014

Histochem Cell Biol

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The apparent connection of galectin-3 to chondrocyte survival and osteoarthritis-like cartilage modifications in animal models provided incentive for the mapping of seven members of this family of adhesion/growth-regulatory proteins in human cartilage specimens. Starting with work in vitro, RT-qPCR analyses and immunocytochemistry revealed gene transcription and protein presence in cultured OA chondrocytes, especially for galectin-1, galectin-3 and galectin-8. Immunohistochemistry in clinical specimens with mild and severe cartilage degeneration detected galectins in chondrocytes-with upregulation, especially of galectin-1 in areas of severe degeneration-accompanied by α2,6-sialylation in the pericellular matrix. Given the possibility for additive/antagonistic activities between galectins, these results direct further research toward examining cellular effects of (1) these proteins (alone or in combination) on chondrocytes and (2) remodeling of the chondrocyte glycophenotype.

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“…In addition to the plant lectins listed in Table 1, we tested human lectins as probes, with the intention of defining chondrocyte reactivity for galectins, known to be endogenous adhesion/growth-regulatory effectors on the cell surface and intracellularly [19]. When labeled, these probes enable the delineation of the status and any alterations of cellular binding capacity, with the potential to detect disease-associated changes [5,20,21]. Homodimeric proto-type galectin-1 (Gal-1) and chimera-type galectin-3 (Gal-3) were selected, because Gal-1 is implicated in the regulation of chondrocyte growth/catabolism, while Gal-3 appears to exert a protective role on articular cells [22-24].…”

Section: Introductionmentioning

confidence: 99%

Glycophenotyping of osteoarthritic cartilage and chondrocytes by RT-qPCR, mass spectrometry, histochemistry with plant/human lectins and lectin localization with a glycoprotein

et al. 2013

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IntroductionThis study aimed to characterize the glycophenotype of osteoarthritic cartilage and human chondrocytes.MethodsArticular knee cartilage was obtained from nine osteoarthritis (OA) patients. mRNA levels for 27 glycosyltransferases were analyzed in OA chondrocytes using RT-qPCR. Additionally, N- and O-glycans were quantified using mass-spectrometry. Histologically, two cartilage areas with Mankin scores (MS) either ≤4 or ≥9 were selected from each patient representing areas of mild and severe OA, respectively. Tissue sections were stained with (1) a selected panel of plant lectins for probing into the OA glycophenotype, (2) the human lectins galectins-1 and -3, and (3) the glycoprotein asialofetuin (ASF) for visualizing β-galactoside-specific endogenous lectins.ResultsWe found that OA chondrocytes expressed oligomannosidic structures as well as non-, mono- and disialylated complex-type N-glycans, and core 2 O-glycans. Reflecting B4GALNT3 mRNA presence in OA chondrocytes, LacdiNAc-terminated structures were detected. Staining profiles for plant and human lectins were dependent on the grade of cartilage degeneration, and ASF-positive cells were observed in significantly higher rates in areas of severe degeneration.ConclusionsIn summary, distinct aspects of the glycome in OA cartilage are altered with progressing degeneration. In particular, the alterations measured by galectin-3 and the pan-galectin sensor ASF encourage detailed studies of galectin functionality in OA.

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Adhesion/growth-regulatory galectins in the human eye: localization profiles and tissue reactivities as a standard to detect disease-associated alterations

Abstract: That the galectins have characteristic localization/reactivity profiles supports the concept of a network with potential for non-overlapping functions. The reported data thus prompt to proceed to the respective analysis of specimens from ocular diseases.

Cited by 21 publications

References 49 publications

In-depth mass spectrometric mapping of the human vitreous proteome

In-depth mass spectrometric mapping of the human vitreous proteome

Human osteoarthritic knee cartilage: fingerprinting of adhesion/growth-regulatory galectins in vitro and in situ indicates differential upregulation in severe degeneration

Glycophenotyping of osteoarthritic cartilage and chondrocytes by RT-qPCR, mass spectrometry, histochemistry with plant/human lectins and lectin localization with a glycoprotein

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