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  • 1
    Electronic Resource
    Electronic Resource
    Effects of biosynthetic human proinsulin on plasma lipids in type 2 diabetes mellitus (1988)
    Springer
    Journal of molecular medicine 66 (1988), S. 1171-1174 
    Details
    ISSN: 1432-1440
    Keywords: Cholesterol ; Diabetes mellitus ; HDL-Cholesterol ; Proinsulin ; Triglycerides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Plasma cholesterol, triglycerides, HDL2-cholesterol, and HDL3-cholesterol were studied in 18 patients with Type 2 diabetes. Prior to entering the clinical trial, the study subjects were in stable control under a fixed mixture of 20% regular and 80% NPH (isophane) biosynthetic human insulin twice daily. The patients were randomized to treatment with either biosynthetic human proinsulin or biosynthetic human NPH insulin (controls) twice daily. Glucose control was kept constant in both groups throughout the study. Of the nine patients treated with proinsulin, eight exhibited a decrease of plasma triglycerides (median decrease by 0.13 mmol/l). In contrast, all nine controls showed a rise (median increase by 0.69 mmol/l) of plasma triglycerides (p〈0.001). In keeping with the fall of plasma triglycerides, HDL2-cholesterol rose in all but one proinsulin-treated patients. Both treatment modalities reduced HDL3-cholesterol with a median decrease of 0.20 mmol/l (p〈0.01) with proinsulin and 0.26 mmol/l with NPH insulin (p〈0.05). We conclude that human proinsulin is able to reduce plasma triglycerides and to increase HDL2-cholesterol in the majority of patients with Type 2 diabetes and thus appears to alter favourably risk factors for coronary heart disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01727664
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    In vitro human polymorphonuclear leukocyte chemokinesis and human monocyte chemotaxis are different activities of aminoterminal and carboxyterminal substance P (1989)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 340 (1989), S. 185-190 
    Details
    ISSN: 1432-1912
    Keywords: Tachykinins ; Calcitonin gene related peptide ; Neutrophils ; Monocytes ; Chemotaxis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Polymorphonuclear leukocytes (PMNL) are a component of the inflammatory response to neurogenic mediators. Using the micropore filter approach, the authors studied the chemoattracting properties of tachykinins, including substance P (SP), neurokinin A (NKA) and neurokinin B (NKB), and that of calcitonin gene-related peptide (CGRP) for human PMNL in vitro and now show that SP in near nanomolar concentrations stimulates locomotion of human PMNL. Locomotion of PMNL is induced by SP, aminoterminal SP (1–9) and the SP receptor antagonist [d-pro2, d-trp7,9]-SP (DPDT) but not by carboxyterminal SP (3–11), NKA, NKB, or CGRP suggesting that the aminoterminal amino acids arginine and proline, are essential residues of SP in activation of PMNL locomotion. In contrast, the migratory effect of SP on monocytes resides in the carboxyterminal SP amino acid sequence, which is in agreement with carboxyterminal, SP receptor-mediated chemotaxis of human monocytes previously shown by others. From the known structure-activity relationships for SP receptors it is concluded that induction of PMNL migration by SP does not involve neurokinin-1 (NK-1), NK-2 or NK-3 receptors. “Checkerboard” analysis reveals that PMNL locomotion by SP is not dependent on concentration gradients and thus represents chemokinesis, which is enhancement of speed and/or frequency of locomotion. One cannot exclude that this action of SP on PMNL is mediated by the aminoterminal sequence via yet unknown SP “receptors”. Since structure-activity relationships appear to be similar to the mast cell degranulating actions of tachykinins, which also critically depend on the aminoterminal sequence, it may correspondingly be regarded as non-receptorial mechanism, due to membrane interaction of the basic groups in the N-terminal region of the peptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00168967
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    Paper (German National Licenses)
    Fulltext
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