Literature DB >> 4008521

The use of lectins to study normal differentiation and malignant transformation.

A Raedler, E Raedler.   

Abstract

Lectins are polypeptides that specifically recognize carbohydrate residues of glycoproteins and glycolipids. They can be extracted from plants, invertebrates and vertebrates. The binding between lectins and carbohydrate moieties can be blocked by the inhibitory sugar for which the lectin is specific. In analogy to antibodies, lectins can be used to analyse cell surface determinants. Thus, differentiation of cells, in particular of immunocytes, has been studied and lectin receptors are now important markers for distinguishing different developmental stages of T-lymphocytes. In consequence, premature, but already committed, T-cells can be eliminated from human bone marrow by means of lectins prior to transplantation in order to avoid graft-versus-host reactions. Moreover, it has been shown that malignant cells can be distinguished from their non-malignant counterparts by the profile of lectin receptors on their surface. This had led to the use of lectin binding sites as tumour markers in lymphomas and carcinomas.

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Year:  1985        PMID: 4008521     DOI: 10.1007/bf00390364

Source DB:  PubMed          Journal:  J Cancer Res Clin Oncol        ISSN: 0171-5216            Impact factor:   4.553


  44 in total

Review 1.  The lectins: carbohydrate-binding proteins of plants and animals.

Authors:  I J Goldstein; C E Hayes
Journal:  Adv Carbohydr Chem Biochem       Date:  1978       Impact factor: 12.200

Review 2.  Lectins.

Authors:  J C Brown; R C Hunt
Journal:  Int Rev Cytol       Date:  1978

3.  Reactivity of human lymphoid and lymphoblastoid cells with peanut agglutinin: detection of a blood cell subset which lacks detectable membrane HLA.

Authors:  J J Ballet; M Fellous; N Sharon; Y Reisner; M Agrapart
Journal:  Scand J Immunol       Date:  1980       Impact factor: 3.487

4.  Interaction between plant agglutinins and Legionella species.

Authors:  R J Doyle; F Nedjat-Haiem; R D Miller; K F Keller
Journal:  J Clin Microbiol       Date:  1982-05       Impact factor: 5.948

5.  Lectin-defined cell surface glycoconjugates of pancreatic cancer cells and their nonmalignant counterparts.

Authors:  A Raedler; W H Schmiegel; E Raedler; R Arndt; H G Thiele
Journal:  Exp Cell Biol       Date:  1983

6.  Selective inhibition of T suppressor-cell function by a monosaccharide.

Authors:  U H Koszinowski; M Kramer
Journal:  Nature       Date:  1981-01-15       Impact factor: 49.962

7.  Postnatal development of rat cerebellum: massive and transient accumulation of concanavalin A binding glycoproteins in parallel fiber axolemma.

Authors:  J P Zanetta; G Roussel; M S Ghandour; G Vincendon; G Gombos
Journal:  Brain Res       Date:  1978-02-24       Impact factor: 3.252

8.  The localization of lectin binding sites during photoreceptor synaptogenesis in the chick retina.

Authors:  B J McLaughlin; J G Wood; J W Gurd
Journal:  Brain Res       Date:  1980-06-09       Impact factor: 3.252

9.  The use of fluorescein-labelled lectins in the detection and identification of fungi pathogenic for man: a preliminary study.

Authors:  R W Stoddart; B M Herbertson
Journal:  J Med Microbiol       Date:  1978-08       Impact factor: 2.472

10.  Varying expressions of lectin receptors within embryonic cell layers of murine cerebral cortex.

Authors:  E Raedler; A Raedler; S Feldhaus
Journal:  Anat Embryol (Berl)       Date:  1981
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  2 in total

1.  Prognostic significance of Leu-M1 immunostaining in papillary carcinomas of the thyroid gland.

Authors:  S Schröder; W Schwarz; W Rehpenning; T Löning; W Böcker
Journal:  Virchows Arch A Pathol Anat Histopathol       Date:  1987

2.  Glycoconjugates in retinoblastoma. A lectin histochemical study of ten formalin-fixed and paraffin-embedded tumours.

Authors:  T Kivelä
Journal:  Virchows Arch A Pathol Anat Histopathol       Date:  1987
  2 in total

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