Disease relevance of Hmgcr

• The C-terminal region of the B. germanica protein has been expressed as a fusion protein in Escherichia coli and exhibits HMG-CoA reductase activity [1].

Psychiatry related information on Hmgcr

• Hmgcr in the Corpus Allatum Controls Sexual Dimorphism of Locomotor Activity and Body Size via the Insulin Pathway in Drosophila [2].

High impact information on Hmgcr

• The loe phenotype is modified by the level of HMG-CoA reductase and suppressed by the inhibition of this enzyme by statin, which has been used for the treatment of Alzheimer patients [3].
• Although Drosophila cannot synthesize cholesterol de novo, the regulatory role of fly AMPK on HMG-CoA reductase is conserved [3].
• The nucleotide sequence of the Drosophila HMG CoA reductase was determined from genomic and cDNA clones [4].
• A 2,748-base-pair open reading frame encoded a polypeptide of 916 amino acids (Mr, 98,165) that was similar to the hamster HMG CoA reductase [4].
• We show that slam is required at this stage in parallel to HMG Coenzyme A reductase, a previously identified germ cell migration gene [5].

Biological context of Hmgcr

• The C-terminal region is more similar to hamster HMG-CoA reductase than is the Drosophila melanogaster enzyme (79% and 69% conserved residues, respectively), and the potential transmembrane domains at the N-terminal region are structurally conservative with both enzymes [1].
• Germ cell migration in zebrafish is dependent on HMGCoA reductase activity and prenylation [6].

Anatomical context of Hmgcr

• These findings suggest that Hmgcr might orchestrate germ cell migration by promoting the release and/or transport of Hh from the SGPs [7].

Associations of Hmgcr with chemical compounds

• Isopentenoid synthesis in isolated embryonic Drosophila cells. Possible regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity by shunted mevalonate carbon [8].
• Furthermore, in the absence of protein synthesis, fluoromevalonate-stabilized Kc cell HMG-CoA reductase activity [9].
• We found no direct correlation between mevalonate-mediated suppression of Kc cell HMG-CoA reductase activity and the rates of [1-14C]-, [3-14C]-, [5-14C]-, or [5-3H]mevalonate incorporation into either carbon dioxide, neutral lipids, water, or water-soluble isopentenoid pyrophosphate esters [8].
• We have concluded that mevalonate, fluoromevalonate, homomevalonate, and compactin (mevinolin) modulated HMG-CoA reductase activity because they altered isoprenoid carbon flow to a post-isopentenyl 1-pyrophosphate regulatory, signal molecule [9].
• Drosophila HMG-CoA reductase was membrane-bound and required NADPH for catalysis [10].

Other interactions of Hmgcr

• Conversely, ectopic Hmgcr upregulates Hh signaling when it is produced in hh-expressing cells, but has no effect when produced in the receiving cells [7].
• 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCoAr) provides attractive cues to Drosophila germ cells, guiding them toward the embryonic gonad [11].
• This phenotype resulted from mutations in the genes encoding HMG-CoA reductase, downstream enzymes in the mevalonate pathway, and G protein Ggamma1, which is geranylgeranylated, thus representing an end point of isoprenoid biosynthesis [12].
• Similarly to the InR, HMGCR is expressed in the corpus allatum (ca), which is the gland where JH biosynthesis occurs [2].

Analytical, diagnostic and therapeutic context of Hmgcr

• This cDNA clone was isolated using as a probe a partial cDNA of B. germanica HMG-CoA reductase, amplified using the polymerase chain reaction [1].
• Molecular cloning, developmental pattern and tissue expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase of the cockroach Blattella germanica [1].
• Northern-blot analysis of RNA samples from different adult female tissues shows high HMG-CoA reductase mRNA levels in the ovary and lower levels in brain and muscle [1].

References