Cytochrome P450 human

Research Area: Immuno and CKS
Cytochromes are a type of protein belonging to superfamilies containing heme as a cofactor, making them hemoproteins. These proteins, also known as CYPs, serve as substrates in enzymatic reactions. The term "P450" originates from the enzyme′s maximum optical density peak at 450 nm when in its reduced state combined with carbon monoxide. Cytochromes are present in various tissues throughout the human body, with a predominant presence in intestinal and hepatic tissues.

Cytochrome P450 human has been used in aflatoxin B1 (AFB1) metabolites analysis to study its effects on AFB1-induced cytotoxicity and micronuclei formation in human hepatocyte (L-02) and human lymphoblastoid (TK6) cells. It has also been used in cell-free cytochrome P4501B1 (CYP1B1) inhibition assays.

Cytochromes play a crucial role in metabolizing a wide range of xenobiotic compounds and are engaged in diverse functions such as steroid metabolism, deactivation of drugs and procarcinogens, metabolism of fatty acids, detoxification of xenobiotic substances, and breakdown of exogenous compounds. It facilitates the oxidation of substances using iron. CYP is well-established that changes in CYP enzymes often occur as a common consequence of immune system activation following infection and inflammation. Despite the overlapping effects of cytokines, the activity of human P450s is independently regulated in infection and inflammation.

Cytochrome P450 is a heterogeneous family of isozymes whose primary function is to oxidize small molecules, both as a function of intermediary metabolism (e.g., fatty acids) and to detoxify exogenous compounds (drugs or toxins). Some isoforms have narrow substrate specificity, while others are promiscuous. The CYP1A1 isoform catalyzes 7-deethylation of ethoxyresorufin. Cytochrome P450 (CYP) plays an important role in detoxifying xenobiotics, cellular metabolism and homeostasis. One of the main mechanisms of drug-drug interactions is the induction or inhibition of these enzymes. CYP enzymes are transcriptionally activated by a variety of xenobiotics and by endogenous substrates via receptor-dependent pathways. Inhibition of these enzymes is a major factor in metabolism-based drug-drug interactions, and many chemotherapeutic medications can cause drug interactions by either inhibiting or inducing the cytochrome p450 enzyme system.

Solution in 100 mM potassium phosphate buffer, pH 7.4.

Microsomes containing human CYP1B1 and recombinant human NADPH-P450 reductase.

Tested for the ability to catalyze the 7-deethylation of ethoxyresorufin.

One unit will reduce 1 nanomole of cytochrome C per minute at pH 7.4 at 37 deg C.