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Zheng-Wang Chen

Publications and source records attributed to Zheng-Wang Chen.

5 recordsLinked to original sources
PubMed2006

[Purification and characterization of weak-acid antibacterial peptide MD7095 from Musca domestica larvae].

Musca domestica,which belongs to insecta, diptera, cyclorrhapha, muscidae, is the most common muscae and the richest resource. It is very significant and valuable to isolate antibacterial peptides from Musca domestica and to develop these peptides into antibacterial medicine. Due to purify a pure peptide from the natural materials (animal, plant and microorganism tissue) is very difficult and complex, few research is going on. It had been reported that the most antibacterial peptides from Musca domestica were alkaline, no weak-acid antibacterial peptides had been reported so far. Based on a high sensitivity detection method, using dilute acetic acid extraction, alginic acid absorption, NaCl salting-out, Sephadex G-25 gel filtration, CMC23 ion-exchange chromatography, electrophoresis, a group of weak-acid antibacterial peptides had been purified from Musca domestica larvae and partial characterized. The peptides had characters of broad antibacterial spectrum and low minimum bactericidal concentration against Gram-positive bacterium such as Bacillus thuringiensis, Bacillus subtilis, Staphylococcus aureus and Gram-negative bacterium such as Pseudomonas aeruginosa, Escherichia coli. The peptides were very stable to keep the antibacterial activity even kept in 95 degrees C for 120 min and frozen-thawed for 10 times. A weak-acid antibacterial peptide MD7095 had been purified in high degree of purity by electro-elution,and was determined Mr 7095Da with MALDI-TOF-MS and pl 5.59 with IEF-PAGE. Peptide mass fingerprinting (PMF) analysis showed MD7095 was a novel bioactive peptide. Few peptides with antibacterial activity against Bacillus thuringiensis had been reported. Observation by scanning electron microscopy (SEM), it was suggested that the bioactivity mechanism of antibacterial peptides from Musca domestica larvae against Bacillus thuringiensis was to perforate cell membrane and lead to bacterium lysis and die. It is hopeful to develop the antibacterial peptides from Musca domestica to candidate medicine.

Animals↗
PubMed2005

Preparation and identification of monoclonal antibodies against pea albumin 1b (PA 1b).

PA 1b (pea albumin 1b), extracted from pea seeds, is thermostable and is multifunctional. It has an attractive peros toxicity, and is also involved in the regulation of callus growth and cell proliferation. Here we report the preparation of monoclonal antibodies (MAbs) against this peptide for further investigation of peptide distribution and functions. PA 1b was coupled to carrier protein using the two-step glutaraldehyde method as an immunal antigen. Five stable cell lines producing anti-PA 1b MAbs were obtained. We analyzed their isotypes, titer, and affinity and found that those MAbs belong to the G(1) and G(2b) subclasses with kappa light chain, respectively. Using these antibodies, a competitive inhibition ELISA was developed, and approximately 15 nmol/L of antigen was detected.

Albumins↗
PubMed2004

GIP1-39, a novel insulinotropic peptide form and aspects on its mechanism of action.

GIP1-39, a novel chain-length form of GIP (gastric inhibitory polypeptide or glucose-dependent insulinotropic polypeptide), has been purified recently from porcine intestine and found to exist abundantly in this tissue. We have characterized that GIP1-39 is an insulinotropic peptide, and demonstrated that GIP1-39 is more potent in stimulating insulin secretion from rat pancreatic islets than GIP1-42, the insulinotropic polypeptide reported originally. Therefore, we have further investigated some aspects on the mechanism behind the insulinotropic effect of GIP1-39 in single rat pancreatic beta cells. GIP1-39 at 100 nM was able to significantly increase intracellular Ca2+ concentration ([Ca2+]i), and capable of enhancing exocytosis assessed by membrane capacitance measurement. The novel GIP1-39 might be a more optimal molecular pattern in stimulating insulin secretion and deserves to be further investigated biologically and clinically.

Amino Acid Sequence↗
PubMedDate not supplied

CAPD peritonitis induces the production of a novel peptide, daintain/allograft inflammatory factor-1.

OBJECTIVES: To study the occurrence of a novel macrophage-derived peptide, daintain/allograft inflammatory factor-1 (AIF-1), in dialysate from continuous ambulatory peritoneal dialysis (CAPD) patients at commencement and after a follow-up period of therapy and during peritonitis. In addition, we studied peptide production in response to bacterial stimulation of monocytes and macrophages. DESIGN: Peritoneal fluid and supernatants from cells stimulated with different bacteria were analyzed for daintain/AIF-1. PATIENTS AND SETTING: Peritoneal fluid was obtained from 5 patients at commencement of CAPD therapy and during 8 weeks' follow-up, and from 14 patients (10 males, 4 females) during CAPD peritonitis and during the noninfected steady state. All patients were admitted to the Karolinska Hospital. A human monocyte cell-line, THP-1 was differentiated to macrophages, and both monocytes and macrophages were stimulated with live and heat-inactivated Escherichia coli, Staphylococcus aureus, and S. epidermidis. Cells were also stimulated with interleukin (IL)-1beta and interferon gamma (IFNgamma). Daintain/AIF-1 was analyzed with radioimmunoassay technique and IL-8 with enzyme immunoassay technique. RESULTS: An increased production of daintain/AIF-1 was observed in the first spent dialysate in the newly started CAPD patients, with a decrease during the follow-up period (p < 0.05). During peritonitis, the first spent dialysate revealed significantly higher levels of daintain/AIF-1 (3.9 ng/mL) compared to the noninfected state (0.8 ng/mL), with production normalizing after 9-12 days. Bacterial stimulation with E. coli, S. aureus, or S. epidermidis induced higher daintain/AIF-1 response in monocytes compared to macrophages (p < 0.05). Live bacteria induced higher production of the peptide compared to heat-inactivated bacteria (p < 0.05). Interleukin-1beta and IFNgamma were used to stimulate monocytes and macrophages; however, no daintain/AIF-1 production was found, although increased IL-8 levels were detected. CONCLUSION: CAPD peritonitis induces a high and prominent daintain/AIF-1 response. Bacteria are able to induce a response of the peptide from monocytes and macrophages, and it is likely that the virulent parts of the bacteria are heat-labile structures. The early rise in daintain/ AIF-1 might be used as a marker of CAPD peritonitis.

Adult↗