Disease relevance of PZ-Peptide

• Bacteroides intermedius degraded several substrates including PZ peptide [1].

High impact information on PZ-Peptide

• However, if the active site was first blocked by the PZ-peptide and subsequently exposed to the (Pro-Pro-Gly)(5) peptide, the difference Fourier map was indistinguishable from that obtained with the PZ-peptide alone [2].
• Moreover, Pz-peptide transport across Caco-2 cell monolayers could be titrated against mucosal Na+ concentration [3].
• This study was conducted to demonstrate that Na+ played a role in the paracellular transport of 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (Pz-peptide), a hydrophilic proline-containing pentapeptide, across the rabbit colonic mucosa and Caco-2 cell monolayers [3].
• Within this stretch was found PLGP, the amino acid sequence constituting the Pz peptide [4].
• The purified enzyme was identified as the major collagenase of the organism, and it cleaved typical collagenase substrates such as azocoll, a synthetic substrate (4-phenylazobenzyloxy-carbonyl-Pro-Leu-Gly-Pro-D-Arg [Pz peptide]), and a type I collagen fibril [4].

Biological context of PZ-Peptide

• After the ligand was withdrawn, the active site of the Mcg dimer could no longer bind the PZ-peptide [2].
• Hydrolysis of the Pz-peptide was maximal at pH 7 [5].
• This asymmetry in transport was consistent with the ability of Pz-peptide to lower the transepithelial electrical resistance of Caco-2 cell monolayers only from the mucosal side [3].
• Ocular absorption of Pz-peptide and its effect on the ocular and systemic pharmacokinetics of topically applied drugs in the rabbit [6].

Anatomical context of PZ-Peptide

• Two peptidases hydrolyzing the Pz-peptide substrate were identified in bovine semen [7].
• We have demonstrated previously that the Pz-peptide synthetic substrate is cleaved by two distinct spermatozoal peptidases, Pz-peptidases A and B. To facilitate further investigations, Pz-peptidase B was purified from bovine spermatozoa [5].
• The cornea appeared to be more sensitive than the conjunctiva to the penetration enhancement effect of Pz-peptide [6].
• Pz-peptide was extensively uptaked into hepatocytes [8].
• Two PZ-peptidases (EC 3.4.-) (A and B) cleaving a synthetic substrate for collagenase, 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (PZ-peptide) have been separated from the particulate fraction of bovine dental follicle [9].

Gene context of PZ-Peptide

• The activator was isolated, partly purified, and shown to be thermolabile, nondialysable, and had no activity toward casein, haemoglobin, histones, and PZ-peptide [10].

Analytical, diagnostic and therapeutic context of PZ-Peptide

• This method is based on the monitoring of the absorption at 320 nm of 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu (PZ-Pro-Leu), enzymatically formed from the substrate 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (PZ-peptide), after separation by high-performance liquid chromatography using a C18 reversed-phase column by isocratic elution [11].

References