Lectins as cell adhesion molecules

doi:10.1016/0959-440X(92)90202-I

Current Opinion in Structural Biology

Volume 2, Issue 5, October 1992, Pages 687-692

https://doi.org/10.1016/0959-440X(92)90202-I Get rights and content

Abstract

Within the past year, there have been major adbances in understanding the structure and function of the selectins, a family of calcium-dependent carbohydrate-binding transmembrane glycoproteins of intermediate molecular size (90–140 kD), and more modest but significant progress has been made for the S-lectins, a family of calcium-independent soluble proteins of small molecular size (14–35 kD). The review stresses the common themes that are emerging within each family and the complementarity of specificity and perhaps function that exists between the two families.

References (31)

M. Bevilacqua et al.
Selectins: a Family of Adhesion Receptors
Cell
(1991)
J.-G. Geng et al.
Neutrophil Recognition Requires a Ca²⁺ Induced Conformational Change in the Lectin Domain of GMP-140
J. Biol Chem
(1991)
M.J. Polley et al.
CD62 and Endothelial Cell-leukocyte Adhesion Molecule 1 (ELAM-1) Recognize the Same Carbohydrate Ligand Sialyl Lewis^x
J.F.M. Leeuwenberg et al.
The Ligand Recognized by ELAM-1 on HL60 Cells is Not Carried by N-linked Oligosaccharides
Eur J Immunol
(1991)
O. Saitoh et al.
Differential Glycosylation and Cell Surface Expression of Lysosomal Membrane Glycoproteins in Sublines of a Human Colon Cancer Exhibiting Distinct Metastatic Potentials
J Biol Chem
(1992)
L.C. Dunlop et al.
Characterization of GMP-140 (P-selectin) as a Circulating Plasma Protein
J Exp Med
(1992)
F.L. Harrison et al.
The 14 kDa β-Galactoside Binding Lectin in Myoblast and Myotube Cultures: Localization by Confocal Microscopy
J Cell Sci
(1992)
M.A. Gitt et al.
Genomic Sequence and Organization of Two Members of a Human Lectin Gene Family
Biochemistry
(1991)
J. Hirabayashi et al.
Effect of Aminoacid Substitution by Site Directed Mutagenesis on the Carbohydrate Recognition and Stability of Human 14 kDa β-Galactoside-binding Lectin
J Biol Chem
(1991)
K. Yamaoka et al.
Overexpression of a β-Galactoside Binding Protein Causes Transformation of BALB3T3 Fibroblast Cells
Biochem Biophys Res Commun
(1991)

C. Foxall et al.

The Three Members of the Selectin Family Recognize a Common Carbohydrate Epitope, the Sialyl Lewis^x Oligosaccharide

J Cell Biol

(1992)

S.J. Singer

Intercellular Communication and Cell-Cell Adhesion

Science

(1992)

D. Tyrrell et al.

Structural Requirements for the Carbohydrate Ligand of E-selectin

E.L. Berg et al.

A Carbohydrate Domain Common to Both Sialyl Le^a and Sialyl Le^x is Recognized by the Endothelial Cell Leukocyte Adhesion Molecule ELAM-1

J Biol Chem

(1991)

Q. Zhou et al.

The Selectin GMP-140 Binds to Sialylated, Fucosylated Lactosaminoglycans on Both Myeloid and Non-myeloid Cells

J Cell Biol

(1991)

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A fimbrial adhesin was identified from an enteroaggregative Escherichia coli strain. The adhesin was purified to 740-fold by sequential chromatography on an affinity matrix and gel filtration column in the FPLC system. The homogeneity of the purified protein was established by analytical isoelectrofocussing (pI 7.25). The native adhesin appeared as a high-molecular-weight aggregative protein as revealed by gel filtration chromatography on Superose 12HR10/30 column. However, in sodium dodecyl sulfate–polyacrylamide gel electrophoresis the molecular weight of the adhesin was found to be 18 kDa and this was further confirmed by gel filtration chromatography on Superose 6HR 10/30 column presence of 6 M guanidine hydrochloride. The N-terminal 15-amino-acid sequence of the adhesin did not show homology with any of the previously reported fimbrial adhesins. The purified adhesin showed adhesion to human erythrocytes in the presence of Ca²⁺ (5 mM). The optimum temperature and pH for the hemadhesion activity was found to be 25°C and 6.5, respectively. The inhibition study clearly suggested that the binding site of the adhesin could recognize galactose as the specific sugar. The fluorescence of 4-methylumbelliferyl-α- $d$ -galactopyranoside was quenched on binding to the adhesin and maximum reversal of fluorescence quenching was observed by competitive substitution titration with raffinose. The adhesin was found to contain one binding site per monomer for its specific sugar residue. The association constant and the free energy of binding were obtained as 3.98 × 10⁵ M⁻¹ and −31.97 kJ/mol, respectively. The adherence of the bacteria to HEp-2 monolayer was inhibited in presence of galactose and this was further supported by a significant reduction in the bacterial adherence to the HEp-2 cells, pretreated with β- $d$ -galactosidase.
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Carbohydrates and glycoconjugatesLectins as cell adhesion molecules

Abstract

Cell

J. Biol Chem

Eur J Immunol

J Biol Chem

J Exp Med

J Cell Sci

Biochemistry

J Biol Chem

Biochem Biophys Res Commun

J Cell Biol

Intercellular Communication and Cell-Cell Adhesion

Science

Structural Requirements for the Carbohydrate Ligand of E-selectin

A Carbohydrate Domain Common to Both Sialyl Lea and Sialyl Lex is Recognized by the Endothelial Cell Leukocyte Adhesion Molecule ELAM-1

J Biol Chem

The Selectin GMP-140 Binds to Sialylated, Fucosylated Lactosaminoglycans on Both Myeloid and Non-myeloid Cells

J Cell Biol

Carbohydrates and glycoconjugates
Lectins as cell adhesion molecules

A Carbohydrate Domain Common to Both Sialyl Le^a and Sialyl Le^x is Recognized by the Endothelial Cell Leukocyte Adhesion Molecule ELAM-1