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148. Amöbenabsceß und Amöbom als chirurgische Probleme (1975)

Guthy, E. A. ; Coburg, A. J. ; Hartmann, M. G.

Springer

Langenbeck's archives of surgery 339 (1975), S. 688-688

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ISSN: 1435-2451

Keywords: Amebiasis ; Complication ; Liver ; Colon ; Amöbiasis ; Komplikation ; Leber ; Colon

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Description / Table of Contents: Zusammenfassung Amöbenabscesse der Leber treten in 90% bei Männern und zu 85 % im rechten Lappen auf. Klinisch imponieren Sepsis, Schmerzen, Hepatomegalie und pulmonale Komplikationen. Die Diagnose wird serologisch gesichert. Die Therapie ist zunächst konservativ. Mischinfektionen, Ruptur, Lokalisation im linken Lappen und erfolglose Therapie sind Operationsindikationen. Amöbome, hypertrophisch-granulierende Colontumoren bei chronischer Amöbencolitis finden sich zu 40% im Caecum, zu 30% im Rectosigmoid. Benigne Histologie und Amöbennachweis sichern die Diagnose. Bis auf Komplikationen konservative Therapie.

Notes: Summary Of amebic hepatic abscesses, 90 percent occur in males, and 85 percent in the right lobe. Sepsis, pain and hepatomegaly, and, in 50 percent of cases, pulmonary complications dominate the clinical picture. Diagnosis is established by serological methods. The initial treatment is conservative. Pyogenic infection, rupture, left-lobe abcess, and lack of response call for surgical intervention. Forty percent of amebomas, rare hypertrophic colonic tumors occurring in chronic amebic colitis, are found in the cecum, and 30 percent in the rectosigmoid. The diagnosis depends on benign histology and the demonstration of amebae. Treatment is conservative unless there are complications.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01257631

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Specific binding of basic fibroblast growth factor to basement membrane-like structures and to purified heparan sulfate proteoglycan of the EHS tumor (1988)

Vigny, M. ; Ollier-Hartmann, M. P. ; Lavigne, M. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Cellular Physiology 137 (1988), S. 321-328

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ISSN: 0021-9541

Keywords: Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: The binding of iodinated basic fibroblast growth factor (bFGF) to low-density heparan sulfate proteoglycan purified from the Engelbreth Holm Swarm (EHS) sarcoma was investigated using different techniques. The tumor clearly contained bFGF, the level being comparable to that found in other tissues such as human or bovine brain. 125I bFGF strongly bound to the basement membrane-like matrix of EHS frozen sections as revealed by autoradiography. Iodinated bFGF bound to purified heparan sulfate proteoglycan but not to laminin or collagen type IV, three components isolated from the same tumor. In contrast, acidic fibroblast growth factor (aFGF) displayed negligible binding to heparan sulfate proteoglycan. Binding of bFGF to frozen sections and to purified proteoglycan could be strongly inhibited by heparin and was displaced by an excess of unlabeled factor and completely suppressed after heparitinase and heparinase treatments. Binding was a function of the salt concentration and was abolished at 0.6 M NaCl. Scatchard analysis indicated the affinity site had a Kd of about 30 nM, a value 10-15 higher than that recently reported by Moscatelli (J. Cell. Physiol., 131:123-130, 1987) in the case of the low-affinity binding sites present on the surface of baby hamster kidney (BHK) cells.

Additional Material: 7 Ill.