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:3.4.24.3 (
collagenase
)
18,340
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Intracranial hemorrhage (ICH) is a common subtype of stroke with high morbidity and mortality. However, few studies have examined the effects of diabetes on the recovery from ICH-induced brain injury. Therefore, we examined the effects of diabetes on protein levels of aquaporins, neuronal loss, angiogenesis, blood brain barrier (BBB) integrity, and neurological deficits following intra-DH
collagenase
-induced ICH in the hippocampus. We found that diabetic rats exhibited enhanced
AQP9
expression in the hippocampus relative to non-diabetic rats, which was associated with increased behavioral deficits. Additionally, ICH induced neovascularization, proliferation of brain microvascular endothelial cells, and hippocampal neuronal loss. However, ICH-induced neovascularization and proliferation of brain microvascular endothelial cells was severely impaired in diabetic rats. Furthermore, ICH-induced hippocampal neuronal loss was exaggerated in diabetic rats. Finally, ICH impaired BBB integrity in the ipsilateral hemisphere, which was increased in diabetic rats. Taken together, the attenuated brain angiogenesis, increased hippocampal neuronal loss, and impaired BBB integrity in diabetic rats after ICH were associated with enhanced
AQP9
expression. This may suggest that
AQP9
is one of the underlying mechanisms that can mitigate the recovery from ICH in diabetic populations.
...
PMID:Diabetes mitigates the recovery following intracranial hemorrhage in rats. 2781 37
Xenopus laevis
oocytes are a valuable tool for investigating the function of membrane proteins. However, regulations around the world, specifically in Brazil, render the import of
Xenopus laevis
frogs impractical, and, in some cases, impossible. Here, as an alternative, we evaluate the usefulness of the North American aquatic bullfrog
Lithobates catesebeianus
, which is commercially available in Brazil, for the heterologous expression of aquaporin (AQP) proteins. We have developed a method that combines a brief
collagenase
treatment and mechanical defolliculation for isolating individual oocytes from
Lithobates
ovaries. We find that they have a similar size, shape, and appearance to
Xenopus
oocytes and can tolerate and survive following injections with cRNA or water. Furthermore, surface biotinylation, western blot analysis, and measurements of osmotic water permeability (
P
f
) show that
Lithobates
oocytes can express AQPs to the plasma membrane and significantly increase the
P
f
of the oocytes. In fact, the
P
f
values are similar to historical values gathered from
Xenopus
oocytes. Due to the presence of a mercury sensitive cysteine (Cys or C) in the throat of the water channel, the
P
f
of oocytes expressing human (h) AQP1, hAQP1
FLAG
[FLAG, short protein tag (DYKDDDDK) added to the N-terminus of AQP1], hAQP8, and rat (r)
AQP9
was inhibited with the mercurial compound p-chloromercuribenzene sulfonate (pCMBS), whereas AQPs lacking this Cys - hAQP1
C189S
mutant [residue Cys 189 was replaced by a serine (Ser or S)] and hAQP7 - were mercury insensitive. Contrary to previous studies with
Xenopus
oocytes, rAQP3 was also found to be insensitive to mercury, which is consistent with the mercury-sensitive Cys (Cys 11) being located intracellularly. Thus, we consider
Lithobates
oocytes to be a readily accessible system for the functional expression and study of membrane proteins for international researchers who do not currently have access to
Xenopus
oocytes.
...
PMID:
Lithobates catesbeianus
(American Bullfrog) oocytes: a novel heterologous expression system for aquaporins. 2953 Sep 31
