Publications by authors named "G M Giancarlo"

Cervical spondylotic myelopathy (CSM) is a progressively growing pathology to afford by a spinal surgeon due to the aging of the population, associated with better treatment management and the best diagnosis and treatment solutions are greatly discussed. Nowadays that scientific literature is progressively increasing to identify the gold standard in diagnosis and treatment can be very challenging. This is particularly evident in spinal surgery with many different indications not only in different countries but also in the same local reality.

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Background: Natalizumab is a promising option for pediatric multiple sclerosis (MS) patients with active evolution and a poor response to Interferon-beta or Glatiramer Acetate. However, no data are available in large cohorts of patients and after a long-term follow up. Our study was planned to shed lights on this topic.

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Article Synopsis
  • The study examines how gepirone is transformed into its metabolites, particularly 1-(2-pyrimidinyl)-piperazine (1-PP) and 3'-OH-gepirone, in human liver microsomes and using two specific enzymes (CYP3A4 and CYP2D6).
  • It was found that CYP3A4 is primarily responsible for metabolizing gepirone, contributing to over 95% of its clearance in the body at low concentrations, while CYP2D6 plays a minor role.
  • The CYP3A inhibitor ketoconazole significantly reduced the formation of several metabolites, demonstrating the dominant role of CYP3A4 in this process.
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Transformation of escitalopram (S-CT), the pharmacologically active S-enantiometer of citalopram, to S-desmethyl-CT (S-DCT), and of S-DCT to S-didesmethyl-CT (S-DDCT), was studied in human liver microsomes and in expressed cytochromes (CYPs). Biotransformation of the R-enantiomer (R-CT) was studied in parallel. S-CT was transformed to S-DCT by CYP2C19 (K(m) = 69 microM), CYP2D6 (K(m) = 29 microM), and CYP3A4 (K(m) = 588 microM).

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Objectives: To determine the relative contribution of cytochromes P450 (CYP) 2C9 and 2C19 to the formation of 5-(-4-hydroxyphenyl)-5-phenylhydantion (HPPH) from phenytoin (PPH).

Design: Hydroxylation of PPH to form HPPH was studied in vitro using human liver microsomes and microsomes from cDNA-transfected human lymphoblastoid cells.

Results: Formation of HPPH from PPH in liver microsomes had a mean (+/- SEM) apparent Km [substrate concentration corresponding to 50% of maximal reaction velocity (Vmax)] of 23.

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