Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP

M. B. Chaker, M. D. Tharp, P. R. Bergstresser

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Langerhans cells (LCs) in mammalian epidermis possess the ectoenzyme Ca++/Mg++-dependent adenosine triphosphate (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 interchange-ability 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.

Original languageEnglish (US)
Pages (from-to)496-500
Number of pages5
JournalJournal of Investigative Dermatology
Volume82
Issue number5
StatePublished - 1984

Fingerprint

Langerhans Cells
Adenosine Monophosphate
Adenosine
Adenosine Diphosphate
Rodentia
Adenosine Triphosphate
Epidermis
Adenosine Triphosphatases
endopolyphosphatase
Diphosphates
Dendritic Cells
Suspensions
Staining and Labeling
Substrates
Adenine Nucleotides
Divalent Cations
Ouabain
Interchanges
diadenosine triphosphate
Cations

ASJC Scopus subject areas

  • Dermatology

Cite this

Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP. / Chaker, M. B.; Tharp, M. D.; Bergstresser, P. R.

In: Journal of Investigative Dermatology, Vol. 82, No. 5, 1984, p. 496-500.

Research output: Contribution to journalArticle

Chaker, M. B. ; Tharp, M. D. ; Bergstresser, P. R. / Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP. In: Journal of Investigative Dermatology. 1984 ; Vol. 82, No. 5. pp. 496-500.
@article{9b08e68db8f248cdaede6700fbe2ba2b,
title = "Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP",
abstract = "Langerhans cells (LCs) in mammalian epidermis possess the ectoenzyme Ca++/Mg++-dependent adenosine triphosphate (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 interchange-ability 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.",
author = "Chaker, {M. B.} and Tharp, {M. D.} and Bergstresser, {P. R.}",
year = "1984",
language = "English (US)",
volume = "82",
pages = "496--500",
journal = "Journal of Investigative Dermatology",
issn = "0022-202X",
publisher = "Nature Publishing Group",
number = "5",

}

TY - JOUR

T1 - Rodent epidermal Langerhans cells demonstrate greater histochemical specificity for ADP than for ATP and AMP

AU - Chaker, M. B.

AU - Tharp, M. D.

AU - Bergstresser, P. R.

PY - 1984

Y1 - 1984

N2 - Langerhans cells (LCs) in mammalian epidermis possess the ectoenzyme Ca++/Mg++-dependent adenosine triphosphate (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 interchange-ability 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.

AB - Langerhans cells (LCs) in mammalian epidermis possess the ectoenzyme Ca++/Mg++-dependent adenosine triphosphate (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 interchange-ability 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.

UR - http://www.scopus.com/inward/record.url?scp=0021279875&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021279875&partnerID=8YFLogxK

M3 - Article

C2 - 6150959

AN - SCOPUS:0021279875

VL - 82

SP - 496

EP - 500

JO - Journal of Investigative Dermatology

JF - Journal of Investigative Dermatology

SN - 0022-202X

IS - 5

ER -