Biochemical and Biophysical Research Communications
Regular ArticleMechanism of Aminobisphosphonate Action: Characterization of Alendronate Inhibition of the Isoprenoid Pathway
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2020, BoneCitation Excerpt :Frustratingly, these studies were repeatedly turned down for publication by several leading journals (dismissed in a single sentence by one manuscript reviewer as being “too far-fetched”) and took almost 3 years to be published, finally appearing in print in 1998 [9,46] and reprinted in 2005 as an “Anniversary Classic” in J Bone Miner Res; one of the most highly cited articles in the journal's history. Soon after these revelatory findings, the enzyme target in the mevalonate pathway was identified as farnesyl diphosphate synthase (FPP synthase, also known as FDPS), a crucial enzyme at the branch point of isoprenoid lipid and cholesterol biosynthesis (Fig. 4) [6,49–52]. Since then it has become clear that N-BPs can also inhibit, albeit less potently, other enzymes in the mevalonate pathway including isopentenyl diphosphate (IPP) isomerase and geranylgeranyl diphosphate (GGPP) synthase [53,54], as well as squalene synthase [43,55].
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