The data used in this analysis are baseline assessments.
α-amidation is a final, essential step in the biosynthesis of about half of all peptide hormones and neurotransmitters.
Peptidylglycine α-amidating monooxygenase (PAM), with enzymatic domains that utilize Cu and Zn, is the only enzyme that catalyzes this reaction.
Analysis of larger samples will be important to verify the genotype-phenotype associations observed.
; serum samples were diluted 10-fold into 20 m M Na TES, p H 7.4, 10 m M mannitol, 1 mg/ml bovine serum albumin, 1% TX-100 (Surfact-Amps X-100) (Thermo Scientific) and 4 μl of the dilution (0.4 μl of serum) was assayed in triplicate in 100 m M Na MES, p H 5.5[) yielded maximal levels of PHM activity for serum samples in both the upper and lower quintiles.
PAL activity was assayed in triplicate from the same dilutions (0.2 μl of serum) using a trace amount of , inductively coupled plasma mass spectrometry analysis of Cu and Zn were performed using an Agilent 7700x equipped with an ASX 500 autosampler at a radio frequency power of 1550 W, argon plasma gas flow rate of 15 L/min, and argon carrier gas flow rate of 1.04 L/min.
Cu and Zn were measured in kinetic energy discrimination mode using He gas (4.3 m L/min).
While the list of biologically active peptide products continues to grow, our understanding of the complex network of peptidergic signaling pathways and their clinical relevance remains modest.
Peptidylglycine α-amidating monooxygenase (PAM), an integral membrane protein, is the only enzyme known to catalyze the α-amidation reaction.
Tissue-specific endoproteolytic cleavage of PAM can produce soluble PHM and PAL, which can be secreted and remain active outside the cell[).
Animal models suggest that one mechanism of regulating PAM expression involves changes in its m RNA stability.
Despite their diversity, many secreted peptides share a common biosynthetic pathway.