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Cytochrome P450 1B1 is a key enzyme involved in the production of potentially carcinogenic estrogen metabolites and the activation of environmental carcinogens and is the predominant member of the CYP1 family expressed in normal breast tissue and breast cancer. Estrogen has been proposed to trigger breast cancer development via an initiating mechanism involving its metabolite, catechol estrogen (CE). CYP1B1 catalyzes the conversion of 17-beta-estradiol to the catechol estrogen metabolites 2-

Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (beta-amyloid precursor protein). Probably represents the last step of maturation of gamma-secretase, facilitating endoproteolysis of presenilin and conferring gamma-secretase activity.

Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP4 may act as a regulator of adult uterine morphology and function. Increases apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake. [SUBCELLULAR LOCATION] Secreted. Expresse

The protein encoded by this gene acts as a homotetramer to catalyze the conversion of homocysteine to cystathionine, the first step in the transsulfuration pathway. The encoded protein is allosterically activated by adenosyl-methionine and uses pyridoxal phosphate as a cofactor. Defects in this gene can cause cystathionine beta-synthase deficiency (CBSD), which can lead to homocystinuria. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, May

CtBP1 associates in complexes with histone deacetylases (HDAC), the G9a histone methyltransferase, and LSD1 histone demethylase illustrating its role in transcriptional repression. Through its association with centrosomes, CtBP1 appears to also play a role in mitosis and Golgi complex organization.

Monoamine oxidase (MAO) is an enzyme of the mitochondrial outer membrane and catalyzes the oxidative deamination of biogenic amines throughout the body (1). MAO is critical in the neuronal metabolism of catecholamine and indolamine transmitters (2). Cultured skin fibroblasts show both MAO-A and MAO-B and both MAOs differ in molecular structure (1). MAO-A, the primary type in fibroblasts, preferentially degrades serotonin and norepinephrine (3). Only MAO-B is present in platelets and only