Expression of membrane-bound carbonic anhydrase isozyme XII in mouse and rat tissues
نویسندگان
چکیده
Background and aims: Carbonic anhydrase XII (CA XII) is a membrane-bound isozyme expressed in some normal human tissues, upregulated in some cancers, and is showed to be a hypoxia-inducible gene product. The expression of CA XII mRNA has been demonstrated in mouse kidney. This study concentrated on the research of the expression of CA XII in all mouse tissues, and later on in rat brain tissues. Methods: mRNA transcription was studied by PCR in mouse tissues and by reverse transcriptase-PCR (RT-PCR) in rat tissues. CA XII protein in mouse tissues was studied by Immunohistochemistry (biotin streptavidin complex method). The studies on rat brain tissues were made by in situ hybridization and northern blot methods after kainic acidinduced status epilepticus. In situ hybridization showed the location of the expression where as northern blot served as a measure of quantity of the expression. Results: CA XII mRNA is expressed in mouse kidney, brain, lung, testis and embryos. In embryos the expression became stronger with increasing age indicating developmental regulation. CA XII protein has a very limited expression distribution (mouse kidney and colon). In rat brain tissues CA XII mRNA is expressed mainly in dentate ganule cells, cortex and choroid plexus. Kainic acid stimulated the expression throughout the cortical layer. Conclusions: The high expression of CA XII in mouse kidney and colon suggests a role for CA XII in the maintenance of body ion and pH homeostasis in the mouse. Kainic acid stimulates CA XII expression throughout the cortical layer. The physiological significance of the observed cortical induction of CA XII remains obscure, but the high expression of CA XII in the choroid plexus suggests an analogous role for this membrane-bound isozyme. CA II is known to participate in CSF secretion.
منابع مشابه
Transmembrane carbonic anhydrase isozymes IX and XII in the female mouse reproductive organs
BACKGROUND Carbonic anhydrase (CA) classically catalyses the reversible hydration of dissolved CO2 to form bicarbonate ions and protons. The twelve active CA isozymes are thought to regulate a variety of cellular functions including several processes in the reproductive systems. METHODS The present study was designed to investigate the expression of transmembrane CAs, CA IX and XII, in the mo...
متن کاملExpression of carbonic anhydrase IV in mouse placenta.
Carbonic anhydrase (CA) facilitates acid-base transport in several tissues. Acidosis upregulates membrane-bound SDS-resistant hydratase activity in various tissues and CA IV mRNA in rabbit kidney. This study was designed to assess whether the expression of membrane-bound CA IV isozyme in mouse placenta is regulated developmentally and by maternal ammonium chloride loading at the end of pregnanc...
متن کاملExpression of membrane-associated carbonic anhydrase isoforms IV, IX, XII, and XIV in the rabbit: induction of CA IV and IX during maturation.
Several carbonic anhydrase (CA) isoforms are associated with plasma membranes. It is probable that these enzymes interact with anion transporters to facilitate the movement of HCO3- into or out of the cell. A better knowledge of CA isoform expression in a given tissue would facilitate a systematic examination of any associations with such transporters. We examined the expression of CAs IV, IX, ...
متن کاملThe Most Recently Discovered Carbonic Anhydrase, CA XV, Is Expressed in the Thick Ascending Limb of Henle and in the Collecting Ducts of Mouse Kidney
BACKGROUND Carbonic anhydrases (CAs) are key enzymes for physiological pH regulation, including the process of urine acidification. Previous studies have identified seven cytosolic or membrane-bound CA isozymes in the kidney. Recently, we showed by in situ hybridization that the mRNA for the most novel CA isozyme, CA XV, is present in the renal cortex. CA XV is a unique isozyme among mammalian ...
متن کاملInhibition of membrane-associated carbonic anhydrase isozymes IX, XII and XIV with a library of glycoconjugate benzenesulfonamides.
A library of glycoconjugate benzenesulfonamides that contain diverse carbohydrate-triazole tails were investigated for their ability to inhibit the enzymatic activity of the three human transmembrane carbonic anhydrase (CA) isozymes hCA IX, hCA XII and hCA XIV. These isozymes have their CA domains located extracellularly, unlike the physiologically dominant hCA II, and are of immense current in...
متن کامل