Endoscopic treatment for pancreatic diseases: Needle-knife-guided cannulation via the minor papilla.

AIM: To determine the efficacy and safety of meticulous cannulation by needle-knife. METHODS: Three needle-knife procedures were used to facilitate cannulation in cases when standard cannulation techniques failed. A total of 104 cannulations via the minor papilla attempted in 74 patients at our center between January 2008 and June 2014 were retrospectively reviewed. RESULTS: Standard methods were successful in 79 cannulations. Of the 25 cannulations that could not be performed by standard methods, 19 were performed by needle-knife, while 17 (89.5%) were successful. Needle-knife use improved the success rate of cannulation [76.0%, 79/104 vs 92.3%, (79 + 17)/104; P = 0.001]. When the 6 cases not appropriate for needle-knife cannulation were excluded, the success rate was improved further (80.6%, 79/98 vs 98.0%, 96/98; P = 0.000). There were no significant differences in the rates of post-endoscopic retrograde cholangiopancreatography adverse events between the group using standard methods alone and the group using needle-knife after failure of standard methods (4.7% vs 10.5%, P = 0.301). CONCLUSION: The needle-knife procedure may be an alternative method for improving the success rate of cannulation via the minor papilla, particularly when standard cannulation has failed.

Recombinant hemangiopoietin promotes cell adhesion and binds heparin in its multimeric form.

Hemangiopoietin (HAPO) is a novel growth factor stimulating the proliferation of hematopoietic and endothelial progenitor cells in vitro and in vivo. The native protein is a 294­amino acid multimodular protein. The N­terminus constitutes of two somatomedin B (SMB) homology domains that contain 14 cysteines. The central region is a putative heparin­binding domain (pHBD) and the C­terminus contains mucin­like repeats. In the present study, we demonstrated that prokaryotic recombinant human HAPO (rhHAPO) self­associates into a multimeric form with a mass weight of ~129 kDa, suggesting a homologous tetramer. rhHAPO in its multimeric form was found to be more stable and more potent in promoting HESS­5 cell adhesion. Multimeric rhHAPO had a higher affinity to heparin compared with its dimeric form, although there was no significant conformational change. C­terminal repeats-truncated rhHAPO (rhHAPOΔmucin) was also found to be assembled into a multimer, while deletion of pHBD (rhHAPOΔmucin­pHBD) caused the protein to remain in a dimeric form, demonstrating that SMB domains participate in self­aggregation of the molecule and that the pHBD region promotes the tetramerization.