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Three different forms of human pancreatic procarboxypeptidase A have been isolated.
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Knockdown of cpa6 mRNA also reduced levels of mRNAs encoding neuropeptide precursors (bdnf, npy, chga, pcsk1nl, tac1, nts, edn1), a neuropeptide processing enzyme (cpe), transcription factor (c-fos), and molecules implicated in glutamatergic signaling
CPA4 functions in neuropeptide processing and regulation in the extracellular environment
Serum CPA4 concentration combined with lymph node involvement may be used as accurate predictors of liver metastasis in colorectal cancer.
CPA4 as a negative regulator of adipogenesis that is down-regulated by FGF-1 (Montrer FGF1 Anticorps). Expression of CPA4 in subcutaneous adipose tissue correlated negatively with insulin (Montrer INS Anticorps) sensitivity.
The crystal structure of the human CPA4 carboxypeptidase in complex with SmCI, a peptide protease inhibitor.
NvCL form Nerita versicolor is a tight-binding inhibitor that interacts with the active site of the CPA4 in a substrate-like manner.
CPA4 gene is imprinted, with preferential expression from the maternal allele in many fetal tissues, but not in fetal brain.
The three-dimensional structure of procarboxypeptidase-A4 (hPCPA4) has been solved and shows the features of related metallocarboxypeptidase zymogens, with a preformed alpha/beta/-hydrolase active-enzyme moiety (hCPA4) and an inhibiting pro-domain (PD).
This gene is a member of the carboxypeptidase A/B subfamily, and it is located in a cluster with three other family members on chromosome 7. Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. This gene could be involved in the histone hyperacetylation pathway. It is imprinted and may be a strong candidate gene for prostate cancer aggressiveness.
, carboxypeptidase A4-like
, carboxypeptidase A3