Three-dimensional studies on the structure of the tissue surrounding the superior mesenteric artery. 1994

T Nagakawa, and K Mori, and M Kayahara, and T Ohta, and K Ueno, and H Sanada, and I Miyazaki
Second Department of Surgery, School of Medicine (School of Allied Professions), Kanazawa University, Ishikawa, Japan.

The anatomy and topography of tissue surrounding the superior mesenteric artery were examined histopathologically, and the structure surrounding the superior mesenteric artery (SMA) was reconstructed with data from histologic examination and three-dimensional analyses. Specimens were obtained from three autopsy cases without abnormalities, two surgically resected cases of cancer of the pancreatic head, and one autopsy case of cancer of the pancreatic head. The endothelium or basal membrane of blood and lymph vessels were identified immunohistochemically, and the distribution of lymph nodes, blood vessels, lymph vessels, and collagen fibers was determined. The superior mesenteric plexus was found to be a relatively dense structure with a thickness of about 2 mm, composed of collagen fibers and connective tissue, which concentrically enveloped the small arteries, the superior mesenteric artery, nerve bundles, and capillaries. Lymph vessels larger than a few micrometers in diameter were often found outside of the plexus, and this plexus contained no lymph nodes in any sections. The three-dimensional study of the modes of spread along the superior mesenteric artery of pancreatic cancer revealed two types of spread: the tumor extends mainly by neural invasion, and the tumor extends mainly by lymph node metastases. These morphologic features suggest that lymphatic flow in the vicinity of the superior mesenteric artery passes primarily outside of the plexus, and complete excision of lymph nodes close to the superior mesenteric artery with preservation of the superior mesenteric plexus is feasible if there is no neural invasion into retropancreatic tissues.

UI MeSH Term Description Entries
D007091 Image Processing, Computer-Assisted A technique of inputting two-dimensional or three-dimensional images into a computer and then enhancing or analyzing the imagery into a form that is more useful to the human observer. Biomedical Image Processing,Computer-Assisted Image Processing,Digital Image Processing,Image Analysis, Computer-Assisted,Image Reconstruction,Medical Image Processing,Analysis, Computer-Assisted Image,Computer-Assisted Image Analysis,Computer Assisted Image Analysis,Computer Assisted Image Processing,Computer-Assisted Image Analyses,Image Analyses, Computer-Assisted,Image Analysis, Computer Assisted,Image Processing, Biomedical,Image Processing, Computer Assisted,Image Processing, Digital,Image Processing, Medical,Image Processings, Medical,Image Reconstructions,Medical Image Processings,Processing, Biomedical Image,Processing, Digital Image,Processing, Medical Image,Processings, Digital Image,Processings, Medical Image,Reconstruction, Image,Reconstructions, Image
D007797 Laminin Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion. Merosin,Glycoprotein GP-2,Laminin M,Laminin M Chain,Chain, Laminin M,Glycoprotein GP 2,M Chain, Laminin
D008207 Lymphatic Metastasis Transfer of a neoplasm from its primary site to lymph nodes or to distant parts of the body by way of the lymphatic system. Lymph Node Metastasis,Lymph Node Metastases,Lymphatic Metastases,Metastasis, Lymph Node
D009361 Neoplasm Invasiveness Ability of neoplasms to infiltrate and actively destroy surrounding tissue. Invasiveness, Neoplasm,Neoplasm Invasion,Invasion, Neoplasm
D009363 Neoplasm Proteins Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm. Proteins, Neoplasm
D010180 Pancreatectomy Surgical removal of the pancreas. (Dorland, 28th ed) Pancreatectomies
D010190 Pancreatic Neoplasms Tumors or cancer of the PANCREAS. Depending on the types of ISLET CELLS present in the tumors, various hormones can be secreted: GLUCAGON from PANCREATIC ALPHA CELLS; INSULIN from PANCREATIC BETA CELLS; and SOMATOSTATIN from the SOMATOSTATIN-SECRETING CELLS. Most are malignant except the insulin-producing tumors (INSULINOMA). Cancer of Pancreas,Pancreatic Cancer,Cancer of the Pancreas,Neoplasms, Pancreatic,Pancreas Cancer,Pancreas Neoplasms,Pancreatic Acinar Carcinoma,Pancreatic Carcinoma,Acinar Carcinoma, Pancreatic,Acinar Carcinomas, Pancreatic,Cancer, Pancreas,Cancer, Pancreatic,Cancers, Pancreas,Cancers, Pancreatic,Carcinoma, Pancreatic,Carcinoma, Pancreatic Acinar,Carcinomas, Pancreatic,Carcinomas, Pancreatic Acinar,Neoplasm, Pancreas,Neoplasm, Pancreatic,Neoplasms, Pancreas,Pancreas Cancers,Pancreas Neoplasm,Pancreatic Acinar Carcinomas,Pancreatic Cancers,Pancreatic Carcinomas,Pancreatic Neoplasm
D011169 Portal Vein A short thick vein formed by union of the superior mesenteric vein and the splenic vein. Portal Veins,Vein, Portal,Veins, Portal
D011956 Receptors, Cell Surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands. Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D011975 Receptors, Mitogen Glycoprotein molecules on the surface of B- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes. Lectin Receptors,Mitogen Receptors,Receptors, Lectin,Mitogen Receptor,Receptor, Mitogen

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