Characterization of a cell surface adhesion molecule expressed by a subset of developing chick neurons

1992 ◽  
Vol 149 (1) ◽  
pp. 213-227 ◽  
Author(s):  
Sanaa El-Deeb ◽  
Steven C. Thompson ◽  
Jonathan Covault
Keyword(s):  
Cell Surface ◽  
Adhesion Molecule ◽  
Surface Adhesion ◽  
A Cell ◽  
Cell Surface Adhesion Molecule

scholarly journals Targeting Opposing Immunological Roles of the Junctional Adhesion Molecule-A in Autoimmunity and Cancer

2020 ◽  
Vol 11 ◽  
Author(s):  
Caio S. Bonilha ◽  
Robert A. Benson ◽  
James M. Brewer ◽  
Paul Garside
Keyword(s):  
Immune Responses ◽  
Adhesion Molecule ◽  
Therapeutic Potential ◽  
Inflammatory Diseases ◽  
Clinical Pathology ◽  
Surface Adhesion ◽  
Pathological Conditions ◽  
Relevant Role ◽  
A Cell ◽  
Cell Surface Adhesion Molecule

The junctional adhesion molecule-A (JAM-A) is a cell surface adhesion molecule expressed on platelets, epithelial cells, endothelial cells and leukocytes (e. g. monocytes and dendritic cells). JAM-A plays a relevant role in leukocyte trafficking and its therapeutic potential has been studied in several pathological conditions due to its capacity to induce leukocyte migration out of inflamed sites or infiltration into tumor sites. However, disruption of JAM-A pathways may worsen clinical pathology in some cases. As such, the effects of JAM-A manipulation on modulating immune responses in the context of different diseases must be better understood. In this mini-review, we discuss the potential of JAM-A as a therapeutic target, summarizing findings from studies manipulating JAM-A in the context of inflammatory diseases (e.g. autoimmune diseases) and cancer and highlighting described mechanisms.

scholarly journals Tst-1, a member of the POU domain gene family, binds the promoter of the gene encoding the cell surface adhesion molecule P0.

1991 ◽  
Vol 11 (3) ◽  
pp. 1739-1744 ◽  
Author(s):  
X He ◽  
R Gerrero ◽  
D M Simmons ◽  
R E Park ◽  
C J Lin ◽  
...  
Keyword(s):  
Nervous System ◽  
Cell Surface ◽  
Gene Family ◽  
Adhesion Molecule ◽  
Surface Adhesion ◽  
Terminal Part ◽  
Gene Encoding ◽  
Helix Loop Helix ◽  
Pou Domain ◽  
Cell Surface Adhesion Molecule

Tst-1, a member of the POU domain gene family, is expressed in specific neurons and in myelinating glia in the mammalian nervous system. Bacterially expressed Tst-1 binds specifically to the promoter of the gene encoding myelin protein P0, a Schwann cell surface adhesion molecule. In cotransfection assays, Tst-1 can specifically repress the P0 promoter. The N-terminal part of Tst-1 protein is highly glycine- and alanine-rich, a structural feature shared by the helix-loop-helix protein TFEB.

scholarly journals Selection of Mimotopes of the Cell Surface Adhesion Molecule Mel-CAM from a Random pVIII-28aa Phage Peptide Library

2002 ◽  
Vol 119 (4) ◽  
pp. 865-869 ◽  
Author(s):  
Christine Hafner ◽  
Ursula Samwald ◽  
Stefan Wagner ◽  
Franco Felici ◽  
Elisabeth Heere-Ress ◽  
...  
Keyword(s):  
Cell Surface ◽  
Adhesion Molecule ◽  
Peptide Library ◽  
Surface Adhesion ◽  
Cell Surface Adhesion Molecule ◽  
Phage Peptide Library ◽  
Selection Of

scholarly journals Tst-1, a member of the POU domain gene family, binds the promoter of the gene encoding the cell surface adhesion molecule P0

1991 ◽  
Vol 11 (3) ◽  
pp. 1739-1744
Author(s):  
X He ◽  
R Gerrero ◽  
D M Simmons ◽  
R E Park ◽  
C J Lin ◽  
...  
Keyword(s):  
Nervous System ◽  
Cell Surface ◽  
Gene Family ◽  
Adhesion Molecule ◽  
Surface Adhesion ◽  
Terminal Part ◽  
Gene Encoding ◽  
Helix Loop Helix ◽  
Pou Domain ◽  
Cell Surface Adhesion Molecule

Tst-1, a member of the POU domain gene family, is expressed in specific neurons and in myelinating glia in the mammalian nervous system. Bacterially expressed Tst-1 binds specifically to the promoter of the gene encoding myelin protein P0, a Schwann cell surface adhesion molecule. In cotransfection assays, Tst-1 can specifically repress the P0 promoter. The N-terminal part of Tst-1 protein is highly glycine- and alanine-rich, a structural feature shared by the helix-loop-helix protein TFEB.

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