We investigated the usefulness of the endoscopic resection of the tumor of the papilla. Thirty patients have been diagnosed to have the tumor of the papilla on endoscopic examination with a ...side-viewing videoendoscopy. The endoscopic findings were classified as three types (I: tumor type, II: granular type, III: normal-like type). All the 30 adenomas of the papilla diagnosed as adenoma by the biopsy under direct vision on endoscopy and limited to the mucosal layer by imaging modalities. Excision was performed in a radical fashion using pure cutting current. The resected specimen was submitted to histologic analysis by serial sectioning. We compared biopsy specimens with the resected tumor to compare to the pathological diagnosis. We examined the pathological diagnosis and the complications of this endoscopic procedure. The final pathological diagnosis by the resected specimens were cancer in 2 of 30 cases and adenomain the remaining cases. As for the tumor in the margin of the resected specimens, tumor is free in 15 of 30 cases (50%). After treatment, the pathological diagnosis of the biopsy from the edge of the ulcer after the resection is free of the residual tumor in 10 of 15 cases (67%) and positive in the remaining 5 cases (33%). In the 5 cases, we treated the residual tumor by hot biopsy. On the resection of the tumor, perforation of the duodenal wall was not seen. Duodenal bleeding was seen in one case after the resection. A cute pancreatitis was seen in 1 out of 30 cases (3%). Serum Hemoglobin fell beyond 3g/dl in 7 cases. Obstructive jaundice beyond 3mg/dl in total bilirubin was seen in 3 among 30 cases (10%). These complications recovered by conservative therapy. In conclusion the endoscopic resection of the adenoma of the papilla of Vater was a safe treatment and useful in the final pathological diagnosis of the adenoma diagnosed by biopsy.
SHPS-1 is a 120 kDa glycosylated receptor-like protein that contains immunoglobulin-like domains in its extracellular region and four potential tyrosine phosphorylation for SH2 domain binding sites ...in its cytoplasmic region. Epidermal growth factor (EGF) stimulated the rapid tyrosine phosphorylation of SHPS-1 and subsequent association of SHPS-1 with SHP-2, a protein tyrosine phosphatase containing SH2 domains, in Chinese hamster ovary cells overexpressing human EGF receptors. In the cells overexpressing SHPS-1, the tyrosine phosphorylation of SHPS-1 was more evident than that observed in parent cells. However, overexpression of SHPS-1 alone did not affect the activation of MAP kinase in response to EGF. These results suggest that SHPS-1 may be involved in the recruitment of SHP-2 from the cytosol to the plasma membrane in response to EGF.
Endoscopic papillectomy for a duodenal duplication cyst Yoshikawa, Daisuke; Yamao, Takuji; Nakao, Kazuhiko
Digestive endoscopy : official journal of the Japan Gastroenterological Endoscopy Society,
01/2017, Letnik:
29, Številka:
1
Report
SAP-1 (stomach cancer-associated protein-tyrosine phosphatase-1) is a transmembrane-type protein-tyrosine phosphatase that is abundant in the brain and certain cancer cell lines. With the use of a ...“substrate-trapping” approach, p130cas, a major focal adhesion-associated phosphotyrosyl protein, has now been identified as a likely physiological substrate of SAP-1. Expression of recombinant SAP-1 induced the dephosphorylation of p130cas as well as that of two other components of the integrin-signaling pathway (focal adhesion kinase and p62dok) in intact cells. In contrast, expression of a substrate-trapping mutant of SAP-1 induced the hyperphosphorylation of these proteins, indicating a dominant negative effect of this mutant. Overexpression of SAP-1 induced disruption of the actin-based cytoskeleton as well as inhibited various cellular responses promoted by integrin-mediated cell adhesion, including cell spreading on fibronectin, growth factor-induced activation of extracellular signal-regulated kinase 2, and colony formation. Finally, the enzymatic activity of SAP-1, measured with an immunocomplex phosphatase assay, was substantially increased by cell-cell adhesion. These results suggest that SAP-1, by mediating the dephosphorylation of focal adhesion-associated substrates, negatively regulates integrin-promoted signaling processes and, thus, may contribute to contact inhibition of cell growth and motility.
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