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  • GIP  (3)
  • Cell & Developmental Biology  (2)
  • Insulinoma  (2)
  • Rat liver  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1091 (1991), S. 356-363 
    ISSN: 0167-4889
    Keywords: Cholecystokinin-8 ; GIP ; GLP-1 (7-36) amide ; Insulin secretion ; Priming ; Rat pancreas
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Regulatory Peptides 37 (1992), S. 205-212 
    ISSN: 0167-0115
    Keywords: Bile secretion ; Glucose production ; Peptide YY ; Perfusion ; Rat liver
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1433-8580
    Keywords: Camostate (FOY 305) ; Degradation ; Rat liver ; HPLC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The elimination of the low molecular weight proteinase inhibitor camostate (FOY 305) was studied in rats after oral administration and in the the situ perfused rat liver. After feeding of camostate (400 mg/kg b. w.) only the metabolites (FOY 251, GBA) were detected in blood samples withdrawn from the portal and hepatic vein. This indicated a rapid degradation of FOY 305 after absorption from the gut lumen. The hepatic extraction of the anti-proteolytic active metabolite FOY 251 during a single liver passage was 23%. It remained almost constant over the period of 120 min. In the perfused rat liver, FOY 305 was given in concentrations comparable to the in vivo studies. It was eliminated by 20%. In these experiments, the compound was metabolized to FOY 251 and in minor amounts to guanidino-benzoate (GBA), the latter being an anti-proteolytic ineffective degradation product. In conclusion, a low hepatic extraction of FOY 305 led to pharmacologically effective concentrations of the active metabolite FOY 251 in the circulation after oral ingestion of the proteinase inhibitor.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 8 (1972), S. 250-259 
    ISSN: 1432-0428
    Keywords: Insulinoma ; immunohistologic investigation of B-cell tumours ; peroxidase labelled antibodies ; insulin and C-peptide in B-cells ; insulin concentration of insulinomas ; difference between insulin in normal and tumour B-cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Résumé 14 insulinomes ont été soumis à un examen immunohistologique à l'aide de la méthode de l'anticorps marqué à la peroxydase. 8 tumeurs ont été étudiées immédiatement après leur extirpation. 7 d'entre elles réagissaient avec les sérums anti-insuline et anti-porcine-C-peptide, mais non avec le sérum anti-glucagon. Un seul carcinome à cellules B avec un contenu en insuline inhabituellement bas, a été négatif. Un an après l'inclusion dans la paraffine, la réaction immunohistologique avec le sérum anti-insuline avait nettement diminué dans les tumeurs, mais non dans les îlots du pancréas adjacent. Chez 6 patients, on disposait de fragments de la tumeur et du pancréas normal inclus dans la paraffine depuis 1 à 4 ans. Dans ce groupe, 4 tumeurs avec un contenu élevé en insuline, n'avaient qu'une faible réaction immunohistologique avec un sérum antiinsuline, et deux tumeurs (l'une avec un contenu élevé en insuline, l'autre avec un contenu faible) ont eu une réaction immunohistologique négative, tandis que les îlots du pancréas adjacent réagissaient fortement dans les six cas. Donc, la réaction immunohistologique de l'insuline dans les tumeurs à cellules B, mais non dans les îlots normaux, dépend du temps écoulé entre l'inclusion dans la paraffine et le moment où elles sont examinées. Seules les tumeurs fixées dans du liquide de Bouin, mais non dans la solution de Karnovsky, ont eu une réaction immunohistologique positive, tandis que les îlots du pancréas adjacent réagissaient positivement après fixation dans la solution de Karnovsky. Ces résultats suggèrent qu'il existe des différences entre l'insuline du pancréas normal et l'insuline des tumeurs. Une comparaison entre la coloration à l'aldéhyde-thionine et l'immunohistologie indique la supériorité de l'immunohistologie dans l'identification des cellules tumorales produisant de l'insuline.
    Abstract: Zusammenfassung 14 insulinproduzierende Tumoren wurden mittels Peroxydase-markierter Antikörper immunhistologisch untersucht. 8 Tumoren gelangten unmittelbar postoperativ zur Untersuchung. Hiervon ließen sich 7 mit einem Antiserum gegen Insulin und Schweine-C-Peptid, nicht aber mit einem Antiserum gegen Glucagon anfärben. Dagegen reagierte ein B-Zellcarcinom mit einer sehr niedrigen Insulinkonzentration mit keinem dieser Seren. Bereits ein Jahr nach der Einbettung in Paraffin ließ die Anfärbbarkeit dieser Tumoren mit einem Antiinsulinserum deutlich nach, während die Inseln des umgebenden normalen Pankreas mit dem gleichen Serum unverändert stark reagierten. — Von 6 weiteren Inseladenomen standen außerdem 1– 4 Jahre altes paraffineingebettetes Tumor- und Pankreasgewebe zur Verfügung. 4 dieser Tumoren hatten eine erhöhte Insulinkonzentration, reagierten immunhistologisch jedoch mit einem Antiinsulinserum nur schwach. Die beiden restlichen Tumoren — einer mit einer hohen, der andere mit einer niedrigen Insulinkonzentration — verhielten sich immunhistologisch negativ. Im Gegensatz zu den Tumoren ließen sich die Inseln des umgebenden Pankreas sämtlicher 6 Fälle mit einem Insulinantiserum gut anfärben. Somit scheint der erfolgreiche immunhistologische Nachweis von Insulin in insulinproduzierenden Tumoren von der Dauer der Einbettung des Tumormaterials in Paraffin abzuhängen. Das Insulin in den Pankreasinseln unterliegt dagegen diesem „Alterungseffekt“ nicht. — TumorInsulin läßt sich nur in Bouin-fixiertem, nicht aber in Karnovsky-fixiertem Gewebe immunhistologisch nachweisen, während das Insulin des normalen Pankreas auch nach Karnovsky-Fixation immunhistologisch nachweisbar ist. Die Befunde sprechen für Unterschiede zwischen normalem pankreatischen und Tumor-Insulin. — Die Färbung der B-Zellen von Tumoren mit Aldehyd-Thionin gelingt seltener als der immunhistologische Nachweis von Insulin in diesen Zellen. Die immunhistologische Untersuchung ist daher zur Identifizierung von B-Zelltumoren den üblichen spezifischen Färbungen überlegen.
    Notes: Summary 14 insulinomas were examined immunohistologically using the peroxidase labelled antibody method. 8 tumours were investigated immediately after extirpation. 7 of these reacted with insulin and porcine-C-peptide antisera but not with glucagon antiserum. Only a B-cell carcinoma with an unusually low insulin concentration was negative. One year after embedding in paraffin the immunohistologic reaction with insulin antiserum had markedly decreased in the tumours; however, not in the islet of the adjacent pancreas. From 6 patients 1 to 4 years old paraffin-embedded material of the tumour and the normal pancreas was available. In this group 4 tumours with an elevated insulin concentration reacted immunohistologically only weakly with an insulin antiserum and two tumours (one with high and one with low insulin concentration were immunohistologically negative, while the islets of the adjacent panceas of all six cases showed a strong reaction. Thus the immunohistilogic reaction of insulin in B-cell tumours but not in normal islets depends on the time elapsed between the paraffin embedding and the examination. Only tumours fixed in Bouin's fluid but not in Karnovsky's solution gave a positive immunohistologie reaction, while the islets of the adjacent pancreas reacted positively also after fixation in Karnovsky's solution. These findings suggest differences between the normal and the tumour insulin. A correlation between aldehyde-thionin stain and immunohistology indicates the superiority of immunohistology in identifying insulin producing tumour cells.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-0428
    Keywords: Insulinoma ; IRI content of insulinoma ; ultrastructural categorization of insulinomas ; proinsulin content of insulinomas ; functional defect in insulinomas reduced storage capacity of insulinoma cells ; non-granular insulin release ; proinsulin content of human pancreas ; diazoxide response of insulinomas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Thirty human insulinomas have been investigated histologically and their immunoreactive insulin (IRI) content estimated. In most cases immunohistological and ultrastructural studies were also performed and the percentage of proinsulin-like components (PLC) in the tumour determined. Except for 1 case the IRI concentration in the tumours was lower (0.01–89.0 U/g) than in the islet tissue. Histologically, immunohistologically and ultrastructurally a variable number of tumour cells contained few and often no beta-granules, indicating a decreased storage capacity for insulin. This defective storage capacity seems to be the major functional abnormality of insulinoma cells. Ultrastructurally four types of insulinoma can be distinguished. The ultra-structural diagnosis of an insulinoma can only be made in type I (typical beta-granules, 13 cases) and type II (typical and atypical granules, 7 cases) but not in type III (atypical granules only, 4 cases) and type IV (virtually agranular, 4 cases). The type IV tumours had the lowest IRI concentration and did not respond to diazoxide treatment. The IRI concentration of the uninvolved pancreas of 19 patients was 2.0±0.2 U/g and in the range of non-diabetic adults. — The percentage PLC in 19 insulinomas was higher (5.3–22%) than in the pancreas of human adults with and without insulinoma (1.7–4.8%). The percentage of PLC in the serum of patients with insulinoma was always higher than in their tumours (33–61%). It is suggested that the higher PLC levels found in the tumour and serum of insulinoma patients are the consequence of the reduced storage capacity of the tumour cells resulting in a rapid passage through the granular route or even a non-granular release of newly synthesized insulin.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0428
    Keywords: GIP ; gastrin ; insulin ; incretin ; chronic pancreatitis ; test meal ; malassimilation of fat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Twenty-nine patients with chronic pancreatitis had a significantly greater IR-GIP response to a test meal than 15 controls. This increased response was not related to the degree of steatorrhoea or glucose intolerance. It was most marked in a group of patients with moderately impaired IRI release and medium steatorrhoea. From this is concluded that the IR-GIP response to a test meal is determined by at least two factors: 1. feedback control via insulin secretion, 2. assimilation of fat. In chronic pancreatitis endocrine insufficiency may induce an exaggerated GIP response and severe exocrine insufficiency may prevent fat induced GIP release. Gastrin is not involved in the different GIP response in patients with chronic pancreatitis.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0428
    Keywords: GIP ; gastrin ; insulin ; incretin ; coeliac disease ; duodeno-pancreatectomy ; chronic pancreatitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The response of serum immunoreactive gastric inhibitory polypeptide (IR-GIP), gastrin (IRG) and insulin (IRI) to a mixed standard meal was measured in 15 controls, 6 patients with coeliac disease, 26 patients with chronic pancreatitis and 6 patients with chronic pancreatitis and partial duodenopancreatectomy (Whipple's procedure). Serum levels of IR-GIP, IRG and IRI were significantly reduced in patients with coeliac disease. The serum glucose increase was significantly smaller only during the first hour after the meal. Since small intestinal GIP- and G-cells are situated mainly in the glands of duodenal and jejunal mucosa their absolute number is not significantly reduced in coeliac disease. It is suggested that the release of IR-GIP and duodenal IRG is influenced by the rate of absorption of nutrients. In patients with chronic pancreatitis the IR-GIP release is significantly greater than in controls, the IRG release normal and the IRI response delayed. After Whipple's procedure the IR-GIP response is increased significantly while the IRG secretion is abolished. This demonstrates that the duodenum is not necessary for GIP release and that pancreatic and jejunal gastrin are without clinical significance.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: α-Macroglobulins derived from plasma or secreted by macrophages are plateletderived growth factor (PDGF) binding proteins that compete with cell-surface receptors on fibroblasts for PDGF binding. α2-Macroglobulin (α2M) derived from bovine plasma was tested for its ability to modulate the PDGF-induced proliferation of primary passage rat lung fibroblasts (RLFs) and a human skin fibroblast cell line (CRL 1508). Fibroblasts were grown in 10% fetal bovine serum (FBS) for 24 hr, then washed with serum-free medium before adding serum-free defined medium (SFDM) containing insulin and transferrin. To this medium were added varying concentrations of human plasma-derived AB-PDGF and α2M, alone or in combination. Receptor-recognized α2M was prepared by treatment with methylamine. Both native α2M and the α2M-methylamine (α2M-MA) were tested for growth promoting activity in the absence or presence of PDGF. After 3 days, a concentration-dependent growth curve of fibroblast proliferation was demonstrated for PDGF alone, with near maximal stimulation reached at 15-20 ng/ml PDGF. α2M and α2M-MA alone had no effect on cell proliferation. However, α2M-MA concentrations above 32 μg/ml synergistically enhanced PDGF-stimulated proliferation 〉100% in the presence of 15 ng/ml PDGF. Native α2M enhanced PDGF-stimulated growth 80-100% above PDGF controls only at low concentrations (32-64 μg/ml α2M). High concentrations of native α2M (128-256 μg/ml) either had no effect on growth or were inhibitory to PDGF-stimulated growth, depending on the cell type tested. Rat lung fibroblasts were shown to secrete a factor(s) that inhibited the trypsin-binding capacity of native α2M. We further demonstrated that early passage RLFs possess specific cell-surface receptors for [125I]-PDGF and [125I]-α2M-MA, and preincubation of RLFs with α2M-MA increased the specific binding of [125I]-PDGF to the cell surface of these fibroblasts. Considered together, these data support the view that receptor-recognized α2M synergistically enhances the proliferative capacity of PDGF. We postulate that receptor-recognized αMs enhance PDGF-stimulated growth by increasing the local concentration of PDGF at the cell surface, where the PDGF could be released in close proximity to its own receptors.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Electron Microscopy Technique 5 (1987), S. 223-226 
    ISSN: 0741-0581
    Keywords: Galvalume ; Hot dip coatings ; Coatings ; Thickness measurement ; Thin sheet ; Analytical electron microscopy ; Transmission electron microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: A method of preparing thinned cross sections of coated sheet steel (Galvalume) for observation in an analytical electron microscope (AEM) was developed. Steel panels dipped for 4 sec in baths of 55% by weight (wt pct) Al-1.7 wt pct Si-balance Zn, and 55 wt pct Al-6.88 wt pct Si-balance Zn at 610°C were examined. The ratio of the intensity of the K and L x-ray lines from the same element was used in determining the foil thickness. The AEM results compared favorably to results obtained using electron microprobe analysis (EMPA).
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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