Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0020440 (hypercapnia)
 7,939 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ventral medullary surface (VMS) is known as the site of the central chemosensitive neurons. These neurons sense excess CO(2)/H(+) dissolved in the cerebrospinal fluid that superfuses the VMS and induce hyperventilation. We hypothesized that genes specific for hyperventilation are expressed much more highly in VMS neurons than in extra-VMS neurons in other parts of the central nervous system (CNS). Applying the differential display technique to the brain of adult rats, we differentiated the mRNAs of the VMS neurons from those of cerebral cortex neurons. Seventeen candidate clones were selected, and their sequences were analyzed. Among these 17 clones, one encodes a novel four-transmembrane protein, which we named rat Rhombex-29. Structural analysis and the phylogenic tree showed that rat Rhombex-29 is homologous to the major CNS myelin protein PLP/DM20-M6 family and belongs to the intermediate type between mouse M6b and shark DMgamma. As the embryos grew into adult rats, constant expression of rat Rhombex-29 mRNA was found in the brain. Hypercapnic stimulation increased expression of rat Rhombex-29 mRNA in the VMS neurons but not in the cerebral cortex neurons. These results indicate that the VMS neurons are endowed with a novel gene, rat Rhombex-29, that is sensitive to H(+).
 ...
PMID:Rhombex-29, a novel gene of the PLP/DM20-M6 family cloned from rat medulla oblongata by differential display. 1100 82

The ventral medullary surface (VMS) of the medulla oblongata is known to be the site of the central chemosensitive neurons in mammals. These neurons sense excess H+/CO2 dissolved in the CSF and induce hyperventilation. To elucidate the mechanism of neuronal cell adaptation to changes of H+/CO2, we screened for hypercapnia-induced genes in the VMS. Here, we report cloning and characterization of a novel gene called proton-associated sugar transporter-A (Past-A), which is induced in the brain after hypercapnia and mediates glucose uptake along the pH gradient. Past-A comprises 751 amino acid residues containing 12 membrane-spanning helices, several conserved sugar transport motifs, three proline-rich regions, and leucine repeats. Past-A transcript was expressed predominantly in the brain. Moreover, the Past-A-immunoreactive neural cells were found in the VMS of the medulla oblongata, and the number of immunoreactive cells was increased by hypercapnic stimulation. Transient transfection of Past-A in COS-7 cells leads to the expression of a membrane-associated 82 kDa protein that possesses a glucose transport activity. The acidification of extracellular medium facilitated glucose uptake, whereas the addition of carbonyl cyanide m-chlorophenylhydrazone, a protonophore, inhibited glucose import. Together, our results indicate that Past-A is a brain-specific glucose transporter that may represent an adaptation mechanism regulating sugar homeostasis in neuronal cells after hypercapnia.
 ...
PMID:Past-A, a novel proton-associated sugar transporter, regulates glucose homeostasis in the brain. 1241 39