Abstract
Belonging to the immunoglobulin superfamily of membrane glycoproteins, carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) are involved in diverse range of cellular processes and disease mechanisms through both homotypic and heterotypic interactions, In particular, CEACAM1 has been found to suppress tumorigenesis, hepatic lipogenesis, and systemic inflammation, but interestingly promotes tumour metastasis, angiogenesis, insulin clearance, and bacterial invasion. Molecular level insights into CEACAM1's behaviour are therefore essential for understanding its structure-function relationships. To this end, we have exploited high spatial- and temporal-resolution fluorescence imaging to elucidate the molecular dynamics and interactions of YFP-tagged CEACAM1 transfected into wild-type HeLa cells. Total internal reflection-fluorescence correlation spectroscopy (ITIR-FCS) enabled direct determination of the local diffusion coefficients of CEACAM1 in different regions of the cell membrane while number and brightness analysis (N&B) and spatial intensity distribution analysis (SpIDA) provided insights into the oligomeric state of CEACAM1. These strategies for characterizing the dynamics of transmembrane receptors in live cells show clear promise for probing glycoprotein function in normal and disease states.
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