Involvement of semicarbazide-sensitive amine oxidase in tresperimus metabolism in human and in rat.

In vitro metabolism of tresperimus by human vascular semicarbazide-sensitive amine oxidase.

Tresperimus (Cellimis), a new immunosuppressive agent is mainly eliminated through an extensive nonhepatic metabolism, in which the oxidative deamination of the primary amine of the drug takes a preponderant part. We have previously demonstrated the ability of human plasma semicarbazide-sensitive amine oxidase (SSAO) to catalyze this reaction. Therefore, the suitability of human umbilical arter...

Elevated activity of semicarbazide-sensitive amine oxidase in blood from patients with skeletal metastases of prostate cancer.

The semicarbazide-sensitive amine oxidases constitute a group of copper-containing enzymes whose physiological function is unclear. The enzymes are present in various tissues, including blood plasma. At present, the source of the plasma enzyme in humans is not known. Results of a recent study suggested that semicarbazide-sensitive amine oxidase is expressed in the skeleton, e.g. in the spine. U...

Semicarbazide-sensitive Amine Oxidase (SSAO) – Regulation and Involvement in Blood Vessel Damage with Special Regard to Diabetes A Study on Mice Overexpressing Human SSAO

Lysyl oxidase inhibition is responsible for the vascular elastic fiber phenotype.

Lysyl Oxidase Inhibition Is Responsible for the Vascular Elastic Fiber Phenotype To the Editor: In the July issue of Hypertension, Mercier et al1 demonstrated a rat model in which the structural vascular phenotype is modified in response to amine oxidase inhibition by semicarbazide. Under these conditions, the elastic lamellae presented globular masses along their periphery, and focal disorgani...

Semicarbazide-sensitive amine oxidase activity exerts insulin-like effects on glucose metabolism and insulin-signaling pathways in adipose cells.

Semicarbazide-sensitive amine oxidase (SSAO) is very abundant at the plasma membrane in adipocytes. The combination of SSAO substrates and low concentrations of vanadate markedly stimulates glucose transport and GLUT4 glucose transporter recruitment to the cell surface in rat adipocytes by a mechanism that requires SSAO activity and hydrogen peroxide formation. Substrates of SSAO such as benzyl...