Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.6.1.3 (
ATPase
)
65,361
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The sarco(endo)plasmic reticulum of animal cells contains an ATP-powered Ca2+ pump that belongs to the P-type family of membrane-bound cation-translocating enzymes. In Schistosoma mansoni, the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) is encoded by the SMA1 and
SMA2
genes. A full-length
SMA2
cDNA clone was isolated, sequenced, and expressed into a yeast Ca2+-ATPase-deficient strain requiring plasmid-borne rabbit SERCA1a for viability. The S. mansoni Ca2+-ATPase supports growth of mutant cells lacking SERCA1a, indicating functional expression in yeast and a role in calcium sequestration. Subcellular fractionation showed that the
SMA2
ATPase
is localized in yeast internal membranes.
SMA2
expression was found to be associated with thapsigargin-sensitive, Ca2+-dependent
ATPase
activity. The activity increased 2-fold upon calcineurin inactivation, which correlates with in vivo stimulated contribution of
SMA2
in calcium tolerance. These results suggest that calcineurin controls calcium homeostasis by inhibiting Ca2+-ATPase activity in an internal compartment.
...
PMID:Schistosoma mansoni Ca2+-ATPase SMA2 restores viability to yeast Ca2+-ATPase-deficient strains and functions in calcineurin-mediated Ca2+ tolerance. 977 93
Schistosoma mansoni
is a parasite that causes bilharzia, a neglected tropical disease affecting hundreds of millions of people each year worldwide. In 2012,
S. mansoni
had been identified as the only invertebrate possessing two SERCA-type Ca
2+
-ATPases, SMA1 and
SMA2
. However, our analysis of recent genomic data shows that the presence of two SERCA pumps is rather frequent in parasitic flatworms. To understand the reasons of this redundancy in
S. mansoni
, we compared SMA1 and
SMA2
at different levels. In terms of sequence and organization, the genes
SMA1
and
SMA2
are similar, suggesting that they might be the result of a duplication event. At the protein level, SMA1 and
SMA2
only slightly differ in length and in the sequence of the nucleotide-binding domain. To get functional information on SMA1, we produced it in an active form in
Saccharomyces cerevisiae
, as previously done for
SMA2
. Using phosphorylation assays from ATP, we demonstrated that like
SMA2
, SMA1 bound calcium in a cooperative mode with an apparent affinity in the micromolar range. We also showed that SMA1 and
SMA2
had close sensitivities to cyclopiazonic acid but different sensitivities to thapsigargin, two specific inhibitors of SERCA pumps. On the basis of transcriptomic data available in GeneDB, we hypothesize that SMA1 is a housekeeping Ca
2+
-
ATPase
, whereas
SMA2
might be required in particular striated-like muscles like those present the tail of the cercariae, the infecting form of the parasite.
...
PMID:Functional characterization of the Ca
2+
-ATPase SMA1 from
Schistosoma mansoni
. 2922 60
