Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

During chemical carcinogenesis Langerhans cells (LC) are depleted from the epidermis, disrupting the normal immunological functions of the skin. Tumor promotors but not initiators, have been shown to deplete adenosine triphosphatase (ATPase)-positive LC from the skin and therefore the cutaneous immune system may be impaired during tumor promotion but not initiation. The present study shows that the tumor promotor 12-O-tetradecanoylphorbol 13-acetate (TPA) but not the initiator urethane depletes Ia-positive LC from BALB/c murine ear epidermis, and beta-glucuronidase-positive LC from C57BL mouse tail skin. Sensitization with 2,4-dinitrofluorobenzene (DNFB) through urethane-treated skin resulted in a normal contact sensitivity response when the mice were challenged 5 days later. In contrast, tolerance resulted from sensitization through TPA-treated skin as a result of the generation of suppressor cells. In addition, TPA but not urethane-treated C57BL mouse tail skin survived for an extended time when grafted onto histoincompatible BALB/c mice. Therefore, impairment of the normal immunological functions of skin resulted from treatment with the tumor promotor TPA but not the tumor initiator urethane, which suggests that a loss of LC during tumor promotion may impair immunological protection against skin tumors.
J Invest Dermatol 1988 Mar
PMID:Suppressor cell activation and enhanced skin allograft survival after tumor promotor but not initiator induced depletion of cutaneous Langerhans cells. 296 90

Cutaneous immune reactions are known to show sexual dimorphism. Langerhans cells (LCs) are bone marrow-derived immune cells in the epidermis and are essential to immune reactions in the skin. In the present research, a study was made of the differences in LC density of male and female mice. Epidermal sheets were separated from the skin of the glabrous part of hind limbs and ears of specific pathogen-free (SPF) mice by ethylenediaminetetraacetic acid (EDTA) treatment and stained for adenosine triphosphatase (ATPase) activity. The density of LCs of hind limb epidermis in male C57BL/6 (823 +/- 20/mm2) and BALB/c (1689 +/- 66/mm2) mice was significantly less than that in females (1363 +/- 52/mm2, p less than 0.001; 2249 +/- 105/mm2, p less than 0.001, respectively). Langerhans cell density in the ears of male C57BL/6 (465 +/- 24/mm2) mice was also significantly less than that in females (542 +/- 17/mm2, p less than 0.02). Although ovariectomy failed to bring about any change in the LC density of hind limb epidermis in female C57BL/6 mice, the LC density in male C57BL/6 mice increased significantly at 4 weeks following orchiectomy (sham operation, 564 +/- 27/mm2; castration, 1179 +/- 49/mm2, p less than 0.001). These results indicate that mouse epidermal LC density depends on sex, i.e., male mice have fewer LCs than female mice. The reduction in LC density in males may possibly be caused by the testis.
J Invest Dermatol 1987 May
PMID:Sex differences in the densities of epidermal Langerhans cells of the mouse. 357 27

Langerhans' cells (LCs) appear to be altered in diseases that express a depressed cellular immune response. We measured the density of LCs in the skin of patients with the disseminated form of paracoccidioidomycosis. The study was performed using adenosine triphosphatase staining of epidermal sheets. Sixteen patients with paracoccidioidomycosis were evaluated. They had a highly significant reduction in LCs (LCs, 323 +/- 135/mm2) when compared with the number (LCs, 689 +/- 204/mm2) found in the control subjects. Morphological alterations of these cells were noted in patients with low numbers of LCs. These findings may reflect the depressed cellular immunity secondary to the infection with Paracoccidioides brasiliensis.
Arch Dermatol 1987 Apr
PMID:Langerhans' cells in paracoccidioidomycosis. 382 79

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.
J Invest Dermatol 1984 May
PMID:Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP. 615 Sep 59

Sheets of ethylenediaminetetraacetic acid (EDTA)-separated epidermis were examined using scanning electron, transmission electron, and light microscopy; sheets were also examined after staining for adenosine triphosphatase (ATPase) activity. Staining was improved by longer incubation with EDTA and by elimination of Trismal buffer as a tissue rinse. EDTA-separated epidermis showed better retention of ultrastructural integrity when washed with phosphate-buffered saline. The ATPase staining procedures described in this present study are ultrastructurally specific for the Langerhans cell.
J Invest Dermatol 1983 Feb
PMID:EDTA separation and ATPase Langerhans cell staining in the mouse epidermis. 621 8

An enzyme histochemical and cytochemical study of normal dermal microvasculature showed that respiratory enzymes, lipase and non-specific esterase occurred in all vascular segments. Lysosomal enzymes were also widely distributed and acid phosphatase activity was localized in lysosomes, Golgi apparatus and small portions of endoplasmic reticulum of both endothelial cells and pericytes. Alkaline phosphatase activity, however, was confined to the arterial side and tip of the capillary loop where it occurred in vesicles along the luminal surface of the endothelium and in junctions between endothelial cells. The localization of nucleoside phosphatase activity within the endothelium varied according to substrate; with adenosine triphosphate as substrate, the reaction product occurred in vesicles distributed throughout the endothelial cells; with adenosine diphosphate it was limited to vesicles along the luminal surface; and with adenosine monophosphate, activity was mostly localized to the lateral surfaces of endothelial cells. These findings suggest functional variation between different vascular segments and between various components of the endothelium. Attempts to demonstrate a specific Na+K+ adenosine triphosphatase (transport ATPase) within the endothelium were not successful.
Br J Dermatol 1981 May
PMID:Human dermal microvasculature: II. Enzyme histochemical and cytochemical study. 723 11

Epidermal Langerhans cells are known to be the major controlling element in the development of contact hypersensitivity. Haptenic molecules permeating the skin are taken up locally by Langerhans cells and then presented to T lymphocytes in the regional lymph nodes. Despite the presence of functional Langerhans cells, however, subsensitizing doses of hapten applied epicutaneously induce tolerance. We examined epidermal Langerhans cells at the site of contact with picryl chloride or oxazolone in BALB/c and C57B1/6 mice with regard to their responding to either subsensitizing or sensitizing doses of allergen. Subsensitizing doses did not interfere with the membranous adenosine triphosphatase system on Langerhans cells, known to relate to functional readiness of the cell. Accordingly, on electron microscopy the ultrastructure of Langerhans cells was found to be like that in untreated skin. In contrast, sensitizing doses caused a significant depletion of adenosine triphosphatase-positive Langerhans cells, and electron microscopy revealed marked cellular activation of Langerhans cells, with enlarged nuclei and increased numbers of mitochondria and Birbeck granules. Furthermore, subsensitizing doses induced tolerance regardless of whether Langerhans cells were functionally intact or had their function blocked arbitrarily. Blocking was achieved either by preceding ultraviolet B irradiation at the site of application or by painting of a sensitizer before painting another sensitizer on the same site. Moreover, not even surgical removal of the site within minutes after painting could prevent the induction of tolerance. The data suggest that subsensitizing doses of contact allergens painted on normal murine skin bypass involvement of epidermal Langerhans cells.
J Invest Dermatol 1996 Aug
PMID:Induction of low zone tolerance to contact allergens in mice does not require functional Langerhans cells. 875 70

The presence of specific adenosine triphosphatase (ATPase) is demonstrated in the eccrine sweat gland units in the scalp of the rhesus monkey (0.2 moles/kg dry wt/hr) and in the sole of the pigtail macaque (1 mole/kg dry wt/hr). This ATPase is activated by combination of Na+ and K+, and this activation is counteracted by ouabain (10(-5) M) which is a specific inhibitor of Na+ transport. Thus, the occurrence of Na-K-ATPase in the sweat gland unit provides an enzymatic basis for participation of active transport of Na+ in the tissue.
J Invest Dermatol 1966 May
PMID:Enzymatic basis for active transport of Na+ in the sweat gland unit. 2562 67


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