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1.
Photochem Photobiol ; 62(1): 144-50, 1995 Jul.
Article in English | MEDLINE | ID: mdl-7638258

ABSTRACT

The inhibition of cytokine and monoclonal antibody binding cell surfaces caused by an extract of Psychotria acuminata, a medicinal plant used in the traditional medicine of the people of Belize (Central Africa), was attributed to the presence of pheophorbide a and pyropheophorbide a. Since the binding of tumor necrosis factor-alpha, interleukin-8, complement factor 5a as well as epidermal growth factor to target cells was dramatically reduced, the inhibition was not receptor or cytokine specific. In addition, the respective binding of radiolabeled monoclonal antibodies CL203 and R15.7 to the cell surface antigens intracellular cell adhesion molecule-1 and lymphocyte function-associated antigen-1 beta-chain was decreased by pretreatment of cells with pheophorbide a as well. In all cases, the inhibition by pheophorbides was dependent on the simultaneous presence of light, indicating causative involvement of a photodynamic process. These observations are not unique to pheophorbides and can be extended to porphyrins as well as to other photodynamic agents. Cytotoxicity resulting from photodynamic therapy (PDT) has been documented by many studies. Our investigations suggest that the inactivation of cell surface receptors contributes not only to an antitumor effect of PDT but also to the systemic immunosuppression, a serious side effect of PDT.


Subject(s)
Chlorophyll/analogs & derivatives , Plants, Medicinal/chemistry , Porphyrins/pharmacology , Receptors, Cell Surface/drug effects , Belize , Chlorophyll/pharmacology , Complement C5a/antagonists & inhibitors , Complement C5a/metabolism , Humans , Interleukin-8/antagonists & inhibitors , Interleukin-8/metabolism , Photosensitizing Agents/pharmacology , Tumor Cells, Cultured , Tumor Necrosis Factor-alpha/antagonists & inhibitors , Tumor Necrosis Factor-alpha/metabolism
3.
Dtsch Zahnarztl Z ; 34(11): 830-2, 1979 Nov.
Article in German | MEDLINE | ID: mdl-296717

ABSTRACT

Failure analysis reveals, that using different materials for expansion screws and fixing elements may cause severe galvanic corrosion or pitting corrosion. Such failures can easily be avoided by using only one alloy with good passivation characteristics instead of different alloys.


Subject(s)
Dental Alloys , Electrogalvanism, Intraoral , Corrosion , Dental Materials , Humans
4.
Biochemistry ; 15(26): 5721-9, 1976 Dec 28.
Article in English | MEDLINE | ID: mdl-1009085

ABSTRACT

Determination of the mechanism of intramolecular nuclear Overhauser effects (NOE) in peptides and depsipeptides is essential to the use of this technique in conformational analysis of these and related biomolecules. Towards this end, 1H NMR double-resonance studies were conducted on valinomycin in (CD3)2SO at 90 MGZ (FT mode) and 250 MGZ (correlation mode). The NOE's are positive at the lower frequency and negative at the higher frequency. Consideration of the theoretical dependence of the NOE on the proton-proton internuclear correlation time and on the resonance frequency indicates that these results are explained by a predominantly dipolar relaxation mechanism. It is demonstrated that exchange modulation of scalar coupling does not contribute significantly to the NOE. A formalism for the NOE's of loosely coupled spin systems is presented which takes into account the effects of high magnetic-field strengths and long correlation times. An approximate analysis of the NOE data assuming a single correlation time for the entire molecule and ignoring cross-relaxation effects was used to evaluate various models that have been proposed for the conformation of valinomycin. The III-1 model of Patel and Tonelli (Patel, D.J., and Tonelli, A.E. (1973), Biochemistry 12, 486) fits the NOE and peptide NHCalphaH coupling constant data and is probably a preferred orientation in dimethyl sulfoxide. These experiments illustrate how intramolecular NOE data provide a valuable auxiliary method to other techniques for delineating the preferred solution conformation of peptides, depsipeptides, and other biomolecules.


Subject(s)
Valinomycin , Binding Sites , Dimethyl Sulfoxide , Magnetic Resonance Spectroscopy , Mathematics , Models, Theoretical , Protein Binding , Protein Conformation
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