Expression of carbonic anhydrases II, IV, VII, VIII and XII in rat brain after kainic acid induced status epilepticus

Halmi, Piia; Parkkila, Seppo; Honkaniemi, Jari

doi:10.1016/j.neuint.2005.08.007

Cited by 73 publications

(90 citation statements)

References 51 publications

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“…The results of the present study suggest that CA III might be another isozyme that is expressed in some neurons, even though its expression and enzyme activity levels are low. In earlier studies, it had also been designated that CA III, as well as other CA isoforms, are present in the epithelial cells of rodent and human choroid plexuses, where they participate in the production of the cerebrospinal fluid and regulation of its ionic content 36,37 . Yet the presence of CA III in the mouse choroid plexus was not detected in this study.…”

Section: Distributionmentioning

confidence: 99%

Carbonic anhydrase III: A neglected isozyme is stepping into the limelight

Harju¹,

Bootorabi

Kuuslahti

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

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Section: Distributionmentioning

confidence: 99%

Carbonic anhydrase III: A neglected isozyme is stepping into the limelight

Harju¹,

Bootorabi

Kuuslahti

et al. 2012

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…The current notion is that the high transport rate through bicarbonate transporters may depend on the local formation of HCO 3 − or perhaps CO 3 2− . It was recently shown that CAXII and perhaps CAIX are also expressed in the choroid plexus [38,49]. Interestingly, CAXII was found in association with the basolateral plasma membrane where more bicarbonate transporters are located.…”

Section: Inhibition Of Carbonic Anhydrases By Acetazolamidementioning

confidence: 99%

Water and solute secretion by the choroid plexus

Prætorius

2006

Pflugers Arch - Eur J Physiol

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The cerebrospinal fluid (CSF) provides mechanical and chemical protection of the brain and spinal cord. This review focusses on the contribution of the choroid plexus epithelium to the water and salt homeostasis of the CSF, i.e. the secretory processes involved in CSF formation. The choroid plexus epithelium is situated in the ventricular system and is believed to be the major site of CSF production. Numerous studies have identified transport processes involved in this secretion, and recently, the underlying molecular background for some of the mechanisms have emerged. The nascent CSF consists mainly of NaCl and NaHCO(3), and the production rate is strictly coupled to the rate of Na(+) secretion. In contrast to other secreting epithelia, Na(+) is actively pumped across the luminal surface by the Na(+),K(+)-ATPase with possible contributions by other Na(+) transporters, e.g. the luminal Na(+),K(+),2Cl(-) cotransporter. The Cl(-) and HCO(3) (-) ions are likely transported by a luminal cAMP activated inward rectified anion conductance, although the responsible proteins have not been identified. Whereas Cl(-) most likely enters the cells through anion exchange, the functional as well as the molecular basis for the basolateral Na(+) entry are not yet well-defined. Water molecules follow across the epithelium mainly through the water channel, AQP1, driven by the created ionic gradient. In this article, the implications of the recent findings for the current model of CSF secretion are discussed. Finally, the clinical implications and the prospects of future advances in understanding CSF production are briefly outlined.

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“…In fact, the most developed research area on CA VII has been linked to drug development, which has led to the discoveries of several potent activators and inhibitors for this isozyme [16,17]. The expression of CA VII protein was first studied in the brain tissue [18]. In previous publications, CA VII has never been investigated in astrocytomas nor has it been determined in any other tumor categories.…”

Section: Introductionmentioning

confidence: 99%

Carbonic anhydrase VII–a potential prognostic marker in gliomas

Bootorabi¹,

Haapasalo²,

Smith³

et al. 2011

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Carbonic anhydrase VII (CA VII) is a cytosolic enzyme expressed in several organs, including the human brain, but it has not been investigated earlier in any tumors. We designed the present study to evaluate CA VII expression in a cohort of human diffuse astrocytomas, mixed oligoastrocytomas and oligodendrogliomas. CA VII immunostaining was correlated to clinicopathologic findings, survival data, and expression of other molecular factors, including Ki-67, p53 protein and epidermal growth factor receptor. CA VII-positive staining was observed in 94% of astrocytomas and 85% of oligodendrogliomas. In the tumor specimens, strong positive areas were often located in close proximity to necrosis. The CA VII immunoreactivity showed positive correlation with tumor malignancy grades of astrocytomas (p = 0.02, chi-square test). In all tumor categories, CA VII-positive staining was often seen in the endothelial cells of neovessels in addition to the tumor cells. CA VII intensity showed no significant association with p53 nor did it correlate with the amplification of epidermal growth factor receptor (analyzed only in astrocytomas) or cell proliferation. Our present results show that CA VII may act as a useful biomarker in histopathologic diagnostics of gliomas. The high expression of CA VII in the tumor cells and endothelium suggests important roles for the enzyme in tumor metabolism. The results also led us to conclude that CA VII might serve as a marker of poor prognosis in diffuse astrocytomas.

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Expression of carbonic anhydrases II, IV, VII, VIII and XII in rat brain after kainic acid induced status epilepticus

Cited by 73 publications

References 51 publications

Carbonic anhydrase III: A neglected isozyme is stepping into the limelight

Carbonic anhydrase III: A neglected isozyme is stepping into the limelight

Water and solute secretion by the choroid plexus

Carbonic anhydrase VII–a potential prognostic marker in gliomas

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