PMID- 30392010
OWN - NLM
STAT- MEDLINE
DCOM- 20200529
LR  - 20200529
IS  - 1432-1424 (Electronic)
IS  - 0022-2631 (Linking)
VI  - 252
IP  - 1
DP  - 2019 Feb
TI  - Inhibition of Sodium-Hydrogen Antiport by Antibodies to NHA1 in Brush Border 
      Membrane Vesicles from Whole Aedes aegypti Larvae.
PG  - 1-16
LID - 10.1007/s00232-018-0053-8 [doi]
AB  - The present research report describes Na(+)/H(+) antiport by brush border 
      membrane vesicles isolated from whole larvae of Aedes aegypti (AeBBMVw). Our 
      hypothesis is that acid quenching of acridine orange by AeBBMVw is predominantly 
      mediated by Na(+)/H(+) antiport via the NHA1 component of the AeBBMVw in the 
      absence of amino acids and ATP. AeNHA1 is a Na(+)/H(+) antiporter that has been 
      postulated to exchange Na(+) and H(+) across the apical plasma membrane in 
      posterior midgut of A. aegypti larvae. Its principal function is to recycle the 
      H(+) and Na(+) that are transported during amino acid uptake, e.g., 
      phenylalanine. This uptake is mediated, in part, by a voltage-driven, 
      Na(+)-coupled, nutrient amino acid transporter (AeNAT8). The voltage is generated 
      by an H(+) V-ATPase. All three components, V-ATPase, antiporter, and nutrient 
      amino acid transporter (VAN), are present in brush border membrane vesicles 
      isolated from whole larvae of A. aegypti. By omitting ATP and amino acids, 
      Na(+)/H(+) antiport was measured by fluorescence quenching of acridine orange 
      (AO) caused by acidification of either the internal vesicle medium (Na(+)(in) > 
      Na(+)(out)) or the external fluid-membrane interface (Na(+)(in) < Na(+)(out)). 
      Vesicles with 100 micromolar Na(+) inside and 10 micromolar Na(+) outside or with 
      0.01 micromolar Na(+) inside and 100 micromolar Na(+) outside quenched 
      fluorescence of AO by as much as 30%. Acidification did not occur in the absence 
      of AeBBMVw. Preincubation of AeBBMVw with antibodies to NHA1 inhibit Na(+)/H(+) 
      antiport dependent fluorescence quenching, indicating that AeNHA1 has a 
      significant role in Na(+)/H(+) exchange.
FAU - Sterling, Kenneth M
AU  - Sterling KM
AD  - Saint James School of Medicine, Albert Lake Drive, The Quarter, Anguilla BWI, 
      2640, Anguilla. ksterling@mail.sjsm.org.
FAU - Harvey, William R
AU  - Harvey WR
AD  - Department of Physiology and Functional Genomics, University of Florida, 
      Gainesville, FL, 32610, USA.
AD  - , Winter Park, USA.
LA  - eng
PT  - Journal Article
DEP - 20181103
PL  - United States
TA  - J Membr Biol
JT  - The Journal of membrane biology
JID - 0211301
RN  - 0 (Antibodies)
RN  - 0 (Ions)
RN  - 0 (Sodium-Hydrogen Exchangers)
SB  - IM
MH  - Aedes/*drug effects/*metabolism
MH  - Animals
MH  - Antibodies/*pharmacology
MH  - Biological Transport/drug effects
MH  - Cytoplasmic Vesicles/*metabolism/ultrastructure
MH  - Hydrogen-Ion Concentration
MH  - Ions/metabolism
MH  - Kinetics
MH  - Larva
MH  - Microvilli/*metabolism/ultrastructure
MH  - Models, Biological
MH  - Sodium-Hydrogen Exchangers/*antagonists & inhibitors
OTO - NOTNLM
OT  - Acidification
OT  - Acridine orange
OT  - AeNAT8
OT  - AeNHA1
OT  - Electrophoretic
OT  - Fluorescence-quench
OT  - H+ V-ATPase
EDAT- 2018/11/06 06:00
MHDA- 2020/05/30 06:00
CRDT- 2018/11/05 06:00
PHST- 2018/03/09 00:00 [received]
PHST- 2018/10/31 00:00 [accepted]
PHST- 2018/11/06 06:00 [pubmed]
PHST- 2020/05/30 06:00 [medline]
PHST- 2018/11/05 06:00 [entrez]
AID - 10.1007/s00232-018-0053-8 [pii]
AID - 10.1007/s00232-018-0053-8 [doi]
PST - ppublish
SO  - J Membr Biol. 2019 Feb;252(1):1-16. doi: 10.1007/s00232-018-0053-8. Epub 2018 Nov 
      3.