Binding of neuroendocrine markers and biotinylated sex hormones and the survival in human lung cancer

Kayser, Klaus; Gabius, Hans‐Joachim; Kohler, Ana Flávia; Runtsch, T.

doi:10.1016/0169-5002(90)90058-t

Cited by 6 publications

(1 citation statement)

References 26 publications

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“…In the first step, a conjugation to a labeled scaffold without impairing the ligand activity is performed. Using estradiol and testosterone, attached to albumin as inert carrier, presence of steroid hormone receptors was detected in tissue sections of lung cancer and in pleural effusion of mesothelioma, here with relation to the S-phase-related tumor cell fraction [ 109 , 110 ]. When similarly presented by a carrier, anthracylin reactivity was revealed in sections of small cell lung cancer sections, with prognostic relevance [ 111 ].…”

Section: Introductionmentioning

confidence: 99%

Introduction to glycopathology: the concept, the tools and the perspectives

Gabius

Kayser

2014

Diagn Pathol

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Virtual slidesThe virtual slides for this article can be found here: http://www.diagnosticpathology.diagnomx.eu/vs/1670639891114983.Analyzing the flow of biological information is a fundamental challenge for basic sciences. The emerging results will then lend themselves to the development of new approaches for medical applications. Toward this end, the products of protein/lipid glycosylation deserve special attention. The covalent attachment of sugars to these carriers means much more than just a change of the carriers’ physicochemical properties. In principle, the ubiquitous presence of glycoconjugates and the close inspection of the particular structural ‘talents’ of carbohydrates provide suggestive evidence for information coding by sugars. In fact, the theoretical number of ‘words’ (oligomers) formed by ‘letters’ (monosaccharides) is by far higher than by using nucleotides or amino acids. In other words, glycans harbor an unsurpassed coding capacity. The cyto- and histochemical detection of dynamic changes in the profile of cellular glycans (glycome, the equivalent of the proteome) by sugar receptors such as antibodies used as tools underscores the suitability of carbohydrates for such a task. The resulting staining patterns can be likened to a molecular fingerprint. By acting as ligand (counterreceptor) for endogenous receptors (tissue lectins), glycan epitopes become partners in a specific recognition pair, and the sugar-encoded information can then be translated into effects, e.g. in growth regulation. Of note, expression of both sides of such a pair, i.e. lectin and cognate glycan, can physiologically be orchestrated for optimal efficiency. Indeed, examples how to prevent autoimmune diseases by regulatory T cells and restrict carcinoma growth by a tumor suppressor attest occurrence of co-regulation. In consequence, these glycans have potential to establish a new class of functional biomarkers, and mapping presence of their receptors is warranted. In this review, the cyto- and histochemical methods, which contribute to explore information storage and transfer within the sugar code, are described. This introduction to the toolbox is flanked by illustrating the application of each type of tool in histopathology, with focus on adhesion/growth-regulating galectins. Together with an introduction to fundamental principles of the sugar code, the review is designed to guide into this field and to inspire respective research efforts.

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Section: Introductionmentioning

confidence: 99%

Introduction to glycopathology: the concept, the tools and the perspectives

Gabius

Kayser

2014

Diagn Pathol

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Neoglycoproteins and lectins in human lung cancer: A survey

Kayser¹,

Gabius²

1991

Lectins and Cancer

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Analysis of tumour necrosis factora-specific, lactose-specific and mistletoe lectin-specific binding sites in human lung carcinomas by labelled ligands

Kayser¹,

Gabius

et al. 1992

Vichows Archiv A Pathol Anat

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Receptor sites can be visualized by labelled ligands as an alternative to receptor-specific antibodies, as substantiated for two different receptor classes. Recombinant tumour necrosis factor alpha (TNF) was biotinylated via amino-groups and the resultant probe was applied to formalin-fixed, paraffin-embedded tissue sections of 94 primary bronchial carcinomas and to normal peripheral lung parenchyma. In addition, monoclonal antibodies specific for neuron-specific enolase (NSE) and TNF itself were used. The biotinylated beta-galactoside-specific mistletoe lectin, which exhibits dose-dependent immunomodulatory and toxic potency, and two probes that specifically detect certain types of sugar receptors were employed to illustrate further the feasibility of using ligands for receptor localisation. The tumours comprised 62 small cell lung carcinomas, 10 epidermoid carcinomas, 11 adenocarcinomas and 11 large cell anaplastic carcinomas. Expression of TNF-binding sites was found in 39 of the small cell lung carcinomas and in 13 of the non-small cell lung carcinomas. Binding capacity for the TNF-specific antibody was seen in similar proportions of small cell lung carcinomas and of non-small cell lung carcinomas. None of the normal lung parenchymas revealed significant staining. Binding capacities to mistletoe lectin were seen in all normal lung parenchymas and in nearly all cases of adenocarcinoma (10/11). A correlation between the expression of NSE and the binding capacities to TNF was detected. Endogenous lectins, specific for lactose or beta-GalNAc, were displayed in nearly one half of the small cell lung carcinoma cases (44% or 45% respectively) and in about 25% of the non-small cell lung carcinoma cases.

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Binding of neuroendocrine markers and biotinylated sex hormones and the survival in human lung cancer

Cited by 6 publications

References 26 publications

Introduction to glycopathology: the concept, the tools and the perspectives

Introduction to glycopathology: the concept, the tools and the perspectives

Neoglycoproteins and lectins in human lung cancer: A survey

Analysis of tumour necrosis factora-specific, lactose-specific and mistletoe lectin-specific binding sites in human lung carcinomas by labelled ligands

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