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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
Published on: May 4, 2012
Distribution of an endogenous lectin during myogenesis as measured by antilectin antibodies
1Division of Biological Sciences, Section of Neurobiology and Behavior, Cornell University, Ithaca, NY 14850 USA.
Abstract:
Antibodies to electrolectin, a lectin endogenous to embryonic skeletal muscle, have been used to study the distribution of lectin during myogenesis in L(6) cells by using immunohistofluorescence microscopy. Evidence for both surface and cytoplasmic forms of lectin is presented. Cytoplasmic lectin does not appear to be strongly regulated by cell cycle or differentiation; it is uniformly distributed throughout the cytoplasm and all cells have about the same quantity as judged by the intensity of fluorescence. Surface lectin is characterized as being organized into puntate structures which can be found on both the upper and lower surfaces of the cell and occasionally on the surface of the dish. Surface lectin is strongly influenced by the differentiation of cells, i.e. it is highest on mononucleated cells and low on myotubes. Paraformaldehyde fixation causes patches of lectin to develop which are not found when live cells are used. The effect of paraformaldehyde is accentuated by Ca(2+).
