Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils.

Détails

ID Serval
serval:BIB_5F745C3DE0F8
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils.
Périodique
Journal of Biological Chemistry
Auteur(s)
Ord D.C., Ernst T.J., Zhou L.J., Rambaldi A., Spertini O., Griffin J., Tedder T.F.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
05/1990
Peer-reviewed
Oui
Volume
265
Numéro
14
Pages
7760-7767
Langue
anglais
Résumé
The leukocyte adhesion molecule-1 (LAM-1, TQ1, Leu-8), expressed by human lymphocytes, neutrophils, monocytes, and their precursors, is a member of the selectin family of cellular adhesion/homing receptors which play important roles in leukocyte-endothelial cell interactions. These cell surface molecules contain an amino-terminal lectin-like domain followed by an epidermal growth factor-like domain and a variable number of short consensus repeat sequences similar to those found in C3/C4 binding proteins. In this report, the structure of the lyam-1 gene that encodes the LAM-1 protein was determined by isolating overlapping genomic DNA clones that hybridized with a LAM-1 cDNA probe. The lyam-1 gene spans greater than 30 kilo base pairs of DNA and is composed of at least 10 exons. The 5' end of the LAM-1 mRNA was mapped by primer extension analysis revealing a single initiation region for transcription. Exons II through X contain translated sequences; exon II encodes the translation initiation codon; exon III, the leader peptide; IV, the lectin-like domain; V, the epidermal growth factor-like domain; VI and VII, the short consensus repeat units; exon VIII, the transmembrane region; exon IX encodes seven amino acids containing a potential phosphorylation site; and exon X encodes the five remaining amino acids of the cytoplasmic tail and the long 3' untranslated region. Sequencing of LAM-1 cDNA clones derived from neutrophils revealed that the protein expressed by neutrophils would be identical in sequence with the protein expressed by lymphocytes and cDNAs that would encode different isoforms of LAM-1 protein were not detected. In addition, the level of LAM-1 expression by lymphocytes and neutrophils from two patients with paroxysmal nocturnal hemoglobinuria, a disorder in which linkage of phosphatidylinositol anchors to proteins is defective, was similar to that of normal controls. Therefore, the usage of exons II through X results in the generation of a single major LAM-1 protein product expressed by lymphocytes and neutrophils.
Mots-clé
Base Sequence, Cell Adhesion Molecules/genetics, Cloning, Molecular, Codon, DNA/genetics, DNA Probes, Exons, Gene Expression, Hemoglobinuria, Paroxysmal/blood, Humans, Introns, L-Selectin, Lymphocytes/metabolism, Molecular Sequence Data, Neutrophils/metabolism, Nucleic Acid Hybridization, Polymerase Chain Reaction, Promoter Regions, Genetic, Protein Biosynthesis, Restriction Mapping
Pubmed
Web of science
Création de la notice
25/01/2008 16:31
Dernière modification de la notice
20/08/2019 15:17
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