A New Surface Marker on T Lymphocytes of Human Peripheral Blood

Hammarström, Sten; Hellström, U.; Perlmann, Peter; Dillner, Marie-Louis

doi:10.1084/jem.138.5.1270

Cited by 102 publications

(35 citation statements)

References 15 publications

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“…Murine mature and immature thymocytes may be distinguished by their different reactivities with PNA (main specificity D-Gal(81-3)-D-GalNAc) [3] and B and T lymphocytes by their different binding to both HPA [4] and SBA [5] (main specificity iV-acetyl-D-galactosamine), suggesting that the HPA binding structures may be different from those binding to SBA. Little is known about the cell surface carbohydrate structures involved in the binding to these 3 lectins [6,7].…”

Section: Affinity Chromatography Liposome Membranementioning

confidence: 99%

Binding specificities of the lectins from Helix pomatia, soybean and peanut against different glycosphingolipids in liposome membranes

Månsson¹,

Olofsson²

1983

FEBS Letters

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The binding specificities of the lectins from Helixpomatia, soybean and peanut against glycosphingolipids containing Blinked terminal D-galactose and N-acetyl-D-galactosamine and the role of sialic acid as a modulator of the binding specificity were investigated. The test system used consisted of liposomes containing the glycosphingolipids and lectins coupled to gel columns. Of the investigated glycosphingolipids only ganglioside GM2 bound to soybean agglutinin while Heiixpomatia agglutinin was found to bind only GA2. Peanut agglutinin showed good affinity both for ganglioside GM1 and its asialoderivative GA1 . LectinGanglioside G&cosphingolipid

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Section: Affinity Chromatography Liposome Membranementioning

confidence: 99%

Binding specificities of the lectins from Helix pomatia, soybean and peanut against different glycosphingolipids in liposome membranes

Månsson¹,

Olofsson²

1983

FEBS Letters

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“…St Louis, Mo.) [9], Different concentrations (O.O.V-0.30 U/nil) of ihe enzyme was tested. In some experiments NANAse treatment was carried oul before fixation of sections.…”

Section: Methodsmentioning

confidence: 99%

“…HP haemaggluiinin has previously been shown to bind to neuratninidase-treatcd T lymphocytes from different species (e.g. man, rat, mouse and cow) [8,9,12,16,23]. In contrast, most normal B lymphocytes are HP-receplor-negative [12].…”

mentioning

confidence: 99%

Localization of T‐Lymphocyte Areas in Human Lymphoid Tissues by Fluorochrome‐Labelled Helix pomatia A Haemagglutinin

Zeromski¹,

Hammarström²,

Hellström³

et al. 1982

Scand J Immunol

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Fluorochrome-labelled Helix pomatia A haemagglutinin (HP) stained T-dependent areas in cryostat tissue sections of human lymph node, tonsil, and spleen and thymocytes within thymic medulla but not within thymic cortex. Neuraminidase treatment of the tissue section was a prerequisite for the positive cell staining. The staining was cell-membrane-associated, and the histological pattern was essentially the same as that observed in parallel sections treated with monoclonal antibodies to T cells (OKT3, Leu-1). In addition, blood vessel walls and connective tissue were also stained by HP conjugates. The latter staining was independent of neuraminidase treatment, resistant to alpha-galactosidase treatment and was not blocked by pretreatment with anti-fibronectin antibody. Body types of staining reaction were specific inasmuch as unlabelled HP and the competitive sugar hapten N-acetyl-D-galactosamine blocked the reaction, Frozen, formalin-fixed tissue sections showed the same stainability and reaction pattern as unfixed sections.

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“…In humans, T and B lymphocytes have been separated on affinity columns of Helix pomatia, after the lymphocytes are predigested with neuraminidase [118,119]. Similarly, wheat germ agglutinin has been used to obtain subsets of human T lymphocytes with differing abilities to respond to mitogens [120].…”

Section: Affinity Chromatographymentioning

confidence: 99%

The application of lectins to the characterization and isolation of mammalian cell populations

1987

Cancer Metast Rev

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Mammalian cells invariably contain a vast array of glycosylated moieties, both inside the cell and on the cell surface. There is an increasing awareness of the utility of these carbohydrates in delineating the phenotype or function of many populations of cells. To this end lectins are extremely useful reagents. Lectins are carbohydrate-binding proteins and glycoproteins of non-immune origin derived from numerous plants and animals. A wide variety of lectins with many distinct carbohydrate specificities have been isolated. Historically the most common laboratory techniques utilizing lectins have been agglutination, mitogen stimulation, and fluorescence techniques. Recent advances in the development and conjugation procedure for labels and matrices have led to the creation of numerous novel lectin-based assays. Lectins are currently used not only to identify cells with specified carbohydrate groups, but also to quantitate the carbohydrate groups or to isolate the carbohydrate-bearing cells or structures.

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A New Surface Marker on T Lymphocytes of Human Peripheral Blood

Abstract: from Clostrldium perfringens [type VI, 1-3 U/rag (NAN-lactose substrate), Sigma Chemical Co., St. Louis, Mo.] at 37°C for 45 rain. 25.106 lymphocytes in 1 ml of Tris-buffered Hanks'

Cited by 102 publications

References 15 publications

Binding specificities of the lectins from Helix pomatia, soybean and peanut against different glycosphingolipids in liposome membranes

Binding specificities of the lectins from Helix pomatia, soybean and peanut against different glycosphingolipids in liposome membranes

Localization of T‐Lymphocyte Areas in Human Lymphoid Tissues by Fluorochrome‐Labelled Helix pomatia A Haemagglutinin

The application of lectins to the characterization and isolation of mammalian cell populations

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