Abstract
A novel lymphocyte-specific immunoglobulin superfamily protein (19A) has been cloned. The predicted 335-amino-acid sequence of 19A represents a Type 1 membrane protein with homology with the CD2 family of receptors. A molecular model of the two predicted extracellular immunoglobulin-like domains of 19A has been generated using the crystal structure of CD2 as a template. In isolated lymphocytes, expression of 19A is induced by various activation stimuli, and enforced expression of the 19A gene promotes homotypic cell adhesion in a B-cell-line model. Collectively these data imply that the 19A protein plays a role in regulation of lymphocyte adhesion.
MeSH Terms
Amino Acid Sequence
B-Lymphocytes/cytology,metabolism
Base Sequence
Blotting, Northern
CD2 Antigens/chemistry
Cell Adhesion
Cell Line
Cloning, Molecular
DNA, Complementary/metabolism
Humans
Immunoglobulins/chemistry
Lymphocyte Activation
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
RNA/metabolism
Receptors, Immunologic/biosynthesis,chemistry
Sequence Homology, Amino Acid
Signaling Lymphocytic Activation Molecule Family
Time Factors
Tissue Distribution
Transfection
Chemicals
CD2 Antigens
DNA, Complementary
Immunoglobulins
Receptors, Immunologic
SLAMF7 protein, human
Signaling Lymphocytic Activation Molecule Family
RNA
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Murphy John J
Infection and Immunity Research Group, Division of Life Sciences, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NN, UK. john.murphy@kcl.ac.uk
Hobby Paul
Vilarino-Varela Juan
Bishop Benjamin
Iordanidou Panagiota
Sutton Brian J
Norton John D
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