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Lectins selectins

Interact with specific carbohydrates Lectins, selectins (cell adhesion lectins), antibodies... [Pg.515]

A striking new discussion of the "sugar code" looks at polysaccharides as informational molecules, with detailed discussions of lectins, selectins, and oligosaccharide-bearing hormones. [Pg.1126]

Various proteins involved in cell—cell (e.g., sperm-oocyte), virus-cell, bactmum-ceH, and hormone—cell interactions C tain plasma proteins of coldwat fish Lectins, selectins (cell adhesion lectins), antibodies Various proteins involved in hwmone and drug action Calnexin, calreticulin... [Pg.65]

These interactions involve adhesion proteins called selectins, which are found both on the rolling leukocytes and on the endothelial cells of the vascular walls. Selectins have a characteristic domain structure, consisting of an N-terminal extracellular lectin domain, a single epidermal growth factor (EGR) domain, a series of two to nine short consensus repeat (SCR) domains, a single transmembrane segment, and a short cytoplasmic domain. Lectin domains, first characterized in plants, bind carbohydrates... [Pg.283]

C-type lectins Characterized by a Ca +-dependent carbohydrate recognition domain (CRD) includes the mammalian asialoglycoprotein receptor, the selectins, and the mannosebinding protein... [Pg.518]

Figure 47-10. Schematic diagram of the structure of human L-selectin. The extracellular portion contains an amino terminal domain homologous to C-type lectins and an adjacent epidermal growth factor-like domain. These are followed by a variable number of complement regulatory-like modules (numbered circles) and a transmembrane sequence (blackdiamond). A short cytoplasmic sequence (open rectangle) is at the carboxyl terminal. The structures of P- and E-selectin are similar to that shown except that they contain more complement-regulatory modules.The numbers of amino acids in L-, P-, and E- selectins, as deduced from the cDNA sequences, are 385,789, and 589, respectively. (Reproduced, with permission, from Bevilacqua MP, Nelson RM Selectins. J Clin Invest 1993 91 370.)... Figure 47-10. Schematic diagram of the structure of human L-selectin. The extracellular portion contains an amino terminal domain homologous to C-type lectins and an adjacent epidermal growth factor-like domain. These are followed by a variable number of complement regulatory-like modules (numbered circles) and a transmembrane sequence (blackdiamond). A short cytoplasmic sequence (open rectangle) is at the carboxyl terminal. The structures of P- and E-selectin are similar to that shown except that they contain more complement-regulatory modules.The numbers of amino acids in L-, P-, and E- selectins, as deduced from the cDNA sequences, are 385,789, and 589, respectively. (Reproduced, with permission, from Bevilacqua MP, Nelson RM Selectins. J Clin Invest 1993 91 370.)...
LPS Lipopolysaccharide L-selectin Leucocte selectin, formerly knovm as monoclonal antibody that recognizes murine L-selectin (MEL-14 antigen), leucocyte cell adhesion molecule-1 (LeuCAM-1), lectin cell adhesion molecule-1 (LeCAM-1 or LecCAM-1), leucocyte adhesion molecule-1 (LAM-1)... [Pg.284]

There are three types of selectins responsible for the attachment of leukocytes to the endothelium, as shown in Table 3.1. Selectins possess three types of domains a C-type lectin domain, an epidermal growth-factor-like domain and between two and nine regulatory domains. [Pg.101]

Adhesion proteins belonging to this group contain a lectin-like domain, a single EGF repeat, and a number of repeats of a protein domain related to the complement binding protein motif (LI). Like most other adhesion proteins, selectins are transmembrane proteins. Selectins bind to carbohydrate groups using... [Pg.150]

Sandros, J., Rozdzinski, E., Zheng, J., Cowburn, D., and Tuomanen, E. (1994). Lectin domains in the toxin of Bordetella pertussis Selectin mimicry linked to microbial pathogenesis. Glycoconj.. 11,501-506. [Pg.156]

Selectins mediate contact by binding to carbohydrate-containing receptors on leucocytes through their N-terminal lectin domain. Sialyl-Lewis X (Neu5Aca2-3-Gaipi-4(Fucal-3)Glc-NAc) and derivatives thereof were shown to bind to the selectins and subsequently inhibit ischaemia-induced leucocyte infiltration in the liver [76-78]. A similar compound prevented antigen-induced late bronchial responses and airway hyper-responsiveness in allergic sheep [79]. [Pg.182]

The selectins are a family of vascular cell surface receptors that are characterized by lectin-like domains at their amino termini, an adjacent epidermal growth factorlike domain, followed by multiple, short consensus repeat units homologous to those of the complement regulatory proteins. Platelet express P-selectin (CD62 ... [Pg.237]

Selectins are a family of plasma membrane lectins that mediate cell-cell recognition and adhesion in a wide range of cellular processes. One such process is the movement of immune cells (T lymphocytes) through the capillary wall, from blood to tissues, at sites of infection or inflammation (Fig. 7-33). At an infection site, P-selectin on the surface of capillary endothelial cells interacts with a specific oligosaccharide of the glycoproteins of circu-... [Pg.263]

Selectins are plasma membrane lectins that bind carbohydrate chains in the extracellular matrix or on the surfaces of other cells, thereby mediating the flow of information between cell and matrix or between cells. [Pg.267]

Duclermortier, P., Lardans, V., Serra, E., Trottein, F. and Dissous, C. (1 999) Biomphalaria glabrata embryonic cells express a protein with a domain homologous to the lectin domain of mammalian selectins. Parasitology Research 85, 481-486. [Pg.240]

The majority of more recent structures relate to the sialyl Lewis X blood group carbohydrate receptor function for the selectin family of eukaryote lectins that mediate leucocyte-endothelial cell interaction during the initial stages of extravasation ( neutrophil rolling ) (20). These structures are the sialyl Le , Le, and Le sequences and several 6 sulfo GlcNAc and 3 sulfo Gal derivatives found in both protein and sphingolipid glycoconjugates (21-24). [Pg.1949]


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See also in sourсe #XX -- [ Pg.11 , Pg.917 ]




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