HEPATOCYTE CELL-SURFACE POLARITY AS DEMONSTRATED BY LECTIN BINDING
HEPATOCYTE CELL-SURFACE POLARITY AS DEMONSTRATED BY LECTIN BINDING
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DOI:
10.1177/36.12.2848070
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发表时间:
1988-12-01
影响因子:
3.2
通讯作者:
JAUREGUI, HO
中科院分区:
文献类型:
--
作者:
MCMILLAN, PN;HIXSON, DC;JAUREGUI, HO
We performed an investigation at the ultrastructural level of the differential distribution of lectin-binding sites among sinusoidal, lateral, and bile canailcular domains of adult rat hepatocytes. Lectin binding to hepatocyt glycocalices was studied in situ or after cellular dissociation by enzymatic (collagenase), chemical (EDTA), and mechanical methods, as well as during cell culture. Using thirteen biotinylated lectins and an avidin-biotin-peroxidase complex (ABC), we have identified lectin-binding sites that are predominantly localized in the bile canalicular [Ricinus communis agglutinin (RCA)] or sinusoidal [Phaseolus vulgaris (PHA)] domains in situ and in mechanically dissociated cells. Lens culinaris (LCA) staining was prominent on sinusoidal surfaces, slight along lateral surfaces, and completely absent in the bile canalicular domain. Concanavalin A (Con A) was unique in binding equally to all domains. Triticum vulgare [wheat germ agglutinin (WGA)] was also bound to all domains, but most intensely to the bile canalicular region. Cells dissociated via collagenase or EDTA treatment exhibited a spherical morphology characterized by many surface microvilli and absence of morphological domains. Lectin binding to dissociated cells was uniformly distributed over the entire cell surface, suggesting a redistribution of lectin receptors that was independent of the separation procedure. Hepatocytes in culture exhibited a partial restoration of morphological domains, but lectin binding polarity was not re-established.