Cerebral chemical dominance and neural regulation of cell division, cell proliferation, neoplastic transformation, and genomic function.
The study assessed the isoprenoid pathway, digoxin synthesis, and neurotransmitter patterns in individuals of differing hemispheric dominance, neurogenetic disorders, and neoplasms. The HMG CoA reductase activity, serum digoxin, magnesium, tryptophan catabolites, tyrosine catabolites, and RBC membrane Na+-K+ ATPase activity were measured in individuals of differing hemispheric dominance. The digoxin status, membrane Na+-K+ ATPase activity, and serum magnesium were assessed in Huntington's disease, trisomy 21, glioblastoma multiforme, and non-Hodgkin's lymphoma (high grade lymphoma). The results showed that right hemispheric, chemically dominant individuals had elevated digoxin synthesis, increased tryptophan catabolites, and reduced tyrosine catabolites, and membrane Na+-K+ ATPase with hypomagnesemia. Left hemispheric, chemically dominant individuals had the opposite patterns. In neurogenetic disorders and neo plasms also hyperdigoxinemia induced membrane Na+-K+ ATPase inhibition, and hypomagnesemia similar to right hemispheric chemical dominance could be demonstrated. The role of hemispheric chemical dominance and hypothalamic digoxin secretion play a key role in the regulation of cell differentiation/proliferation and genomic function. Ninety-five percent of the patients with neurogenetic disorders and neoplasms were right-handed/left hemispheric dominant by dichotic listening test. However, all of them had biochemical patterns similar to right hemispheric chemical dominance. Hemispheric chemical dominance has no correlation to cerebral dominance detected by handness/dichotic listening test.
Kurup
Ravi Kumar
RK
Department of Neurology, Medical College Hospital, Trivandrum, Kerala, India.
Kurup
Parameswara Achutha
PA
D000328:Adult; D001921:Brain / Q000378:metabolism* / Q000473:pathology*; D001932:Brain Neoplasms / Q000378:metabolism / Q000473:pathology; D002455:Cell Division / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D002465:Cell Movement / Q000502:physiology; D002471:Cell Transformation, Neoplastic / Q000473:pathology; D004077:Digoxin / Q000378:metabolism*; D004314:Down Syndrome / Q000378:metabolism / Q000473:pathology; D007839:Functional Laterality / Q000502:physiology*; D015894:Genome, Human; D005909:Glioblastoma / Q000378:metabolism / Q000473:pathology; D006801:Humans; D006816:Huntington Disease / Q000378:metabolism / Q000473:pathology; D006903:Hydroxymethylglutaryl CoA Reductases / Q000378:metabolism; D008228:Lymphoma, Non-Hodgkin / Q000378:metabolism / Q000473:pathology; D008274:Magnesium / Q000378:metabolism; D009474:Neurons / Q000378:metabolism* / Q000473:pathology*; D010042:Ouabain / Q000378:metabolism
C083016:sodium-potassium ATPase inhibitory factor; D010042:Ouabain; D004077:Digoxin; D006903:Hydroxymethylglutaryl CoA Reductases; D008274:Magnesium