Target intelligence / Profile preview

JAM-A and sialic acid (None)

Target
None
Molecular classification
Receptor, Adhesion molecule, Immunoglobulin superfamily, Glycan, carbohydrate moiety, terminal sugar on glycoproteins/glycolipids
01

Overview

This entry should be split into two specific targets for optimal structured curation: one for “Junctional adhesion molecule A (JAM-A)” and one for “cell-surface sialic acid.” The current form is not a singular canonical target and is flagged as such.

Other names
Junctional adhesion molecule AJAM1F11 receptorF11RN-acetylneuraminic acid (Neu5Ac)sialoglycansialylated glycan
02

Mechanism of action

Antibodies or small molecules may block homophilic/heterophilic adhesion, inhibit downstream signaling (e.g., Rap1 activation), or disrupt tight junctions to alter cell migration/permeability. Viral attachment inhibitors block virus binding to sialic acids; sialyltransferase inhibitors alter glycosylation of surface proteins to reduce cell adhesion, spreading, or immune evasion.

03

Biological functions

Cell adhesion and tight junction formationIntracellular signalingCell migration and polarityModulation of paracellular permeabilityImmune cell transmigrationMediates cell–cell and pathogen–cell interactionsModulates immune recognition and maskingContributes to metastatic potential in cancer cells
04

Disease associations

CancerInflammationCardiovascular diseaseInfectionimmune evasion
05

Safety considerations

Potential effects on normal tissue tight junctions, barrier function, and immune cell trafficking limit therapeutic windowInhibiting sialylation may affect normal tissue protection from immune recognition and disrupt many physiological glycan-dependent processes
06

Interacting drugs

No approved drugs specifically target JAM-A, but it is a subject of anti-cancer and anti-inflammatory therapeutic development

2 more in the full profile.

07

Biomarkers

Circulating or tissue JAM-A as a biomarker for cell adhesion, metastasis, cardiovascular disease, and inflammationCell-surface sialylation level as a marker of malignancy, metastatic potentialin some infections

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