Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP.
Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP.
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啮齿动物表皮朗格汉斯细胞对 ADP 的组织化学特异性高于对 ATP 和 AMP 的组织化学特异性。
DOI:
10.1111/1523-1747.ep12261031
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发表时间:
1984
期刊:
影响因子:
--
通讯作者:
Bergstresser,PR
中科院分区:
文献类型:
--
作者:
Chaker,MB;Tharp,MD;Bergstresser,PR
Langerhans cells (LCs) in mammalian epidermis possess the ectoenzyme Ca++/Mg++-dependent adenosine triphosphatase (ATPase), which has served as a useful histochemical marker for these dendritic cells in a variety of tissue preparations. Since ATPase represents only one of several potential cell surface polyphosphatases, we investigated the capacities of 3 related adenine nucleotide substrates to identify rodent epidermal LCs. Cell surface ATPase activity was not inhibited in the presence of ouabain and was observed to be strictly divalent cation-dependent, with complete interchangeability between Ca++and Mg++. Optimal staining in the presence of either cation occurred at a 20 mM concentration. Substrate concentration dependence was also observed, with optimal staining at 0.33 mM adenosine 5′-triphosphate (ATP). On an equimolar basis, however, adenosine 5'-diphosphate (ADP) was superior to ATP for the identification of LCs both in whole mounts of epidermis and in suspensions of disaggregated epidermal cells. The substrate adenosine 5'-monophosphate (AMP) stained follicular epithelial cells in both rodent species but failed to identify epidermal LCs in the mouse and only weakly stained these dendritic cells in rat epidermis. We conclude from these studies that ADP demonstrates greater specificity for LC surface polyphosphatase activity than ATP and that the inadvertent inclusion of AMP during identification procedures for epidermal cell suspensions will falsely identify cells other than LCs.