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1.
Neuroscience ; 53(4): 919-25, 1993 Apr.
Article in English | MEDLINE | ID: mdl-8506026

ABSTRACT

The S-100 protein-PC12 cell interaction has been studied as a model system of the possible physiological role played by S-100 protein in the nervous system. The data reported demonstrate that S-100 exerts a cytotoxic action which eventually leads to PC12 cell death, regardless of the cell cycle phase. The effect is specific for the S-100 isoforms, which are made up of two identical subunits and is abolished by a monoclonal antibody directed against the same isoforms. Other isoforms and/or calcium-binding proteins, such as troponin or calmodulin, do not induce the same effects. The action of S-100 on cell viability is not detectable in other cell lines of different embryological origin, such as 3T3, L1210, GH3. S-100 causes a rapid and considerable increase (two- to three-fold) of intracellular Ca2+ concentration in PC12 cells accompanied by cytostatic and cytotoxic action. It is postulated that this action also occurs in vivo, as part of the physiological action of this protein.


Subject(s)
Calcium/metabolism , Neurons/metabolism , S100 Proteins/toxicity , Animals , Antibodies, Monoclonal/immunology , Calcium Radioisotopes , Calcium-Binding Proteins/metabolism , Cell Death/drug effects , Nerve Growth Factors/pharmacology , Neurons/drug effects , PC12 Cells , Protein Binding , Rats
2.
FEBS Lett ; 255(2): 381-4, 1989 Sep 25.
Article in English | MEDLINE | ID: mdl-2477281

ABSTRACT

S-100a0 protein, the alpha alpha-isoform of the S-100 family, stimulates Ca2+-induced Ca2+ release from terminal cisternae isolated from rat skeletal muscle cells. The stimulatory effect of S-100a0 is maximal at approximately 5 microM S-100a0 and half maximal at approximately 0.1 microM S-100a0, at 1.8 microM free Ca2+ in the presence of 5 mM Mg2+ plus 0.1 M KCl. The effect of the protein on Ca2+-induced Ca2+ release is completely inhibited by the calcium release blocker, ruthenium red.


Subject(s)
Calcium/metabolism , S100 Proteins/pharmacology , Sarcoplasmic Reticulum/metabolism , Animals , Calcium/pharmacology , Heart/physiology , Kinetics , Muscles/metabolism , Rats , Ruthenium Red/pharmacology , S100 Proteins/isolation & purification , Sarcoplasmic Reticulum/drug effects , Swine
3.
J Muscle Res Cell Motil ; 10(4): 326-30, 1989 Aug.
Article in English | MEDLINE | ID: mdl-2527869

ABSTRACT

To study the physiological aspects of the excitation-contraction cycle, saponin (10-100 micrograms ml-1) was used as a skinning agent on muscle and sarcotubular vesicles derived from fast muscles (sartorius and tibialis anterior) of Rana esculenta. The vesicles showed similar Ca2+-ATPase activity and similar protein profiles carried out by SDS-PAGE. Calcium transport in untreated vesicles and those treated with different concentrations of saponin seemed to have the same quantitative and qualitative parameters if the saponin was used in a range between 10 and 50 micrograms ml-1. Our results confirm that saponin may be considered to be a valid skinning agent for the external membranes of fast skeletal muscles.


Subject(s)
Calcium/metabolism , Saponins/pharmacology , Sarcoplasmic Reticulum/metabolism , Animals , Biological Transport, Active/drug effects , Calcium-Transporting ATPases/metabolism , Muscle Contraction/drug effects , Rana esculenta , Sarcoplasmic Reticulum/drug effects
4.
FEBS Lett ; 248(1-2): 9-12, 1989 May 08.
Article in English | MEDLINE | ID: mdl-2721682

ABSTRACT

S-100a0 protein, the alpha alpha isoform of the S-100 family, stimulates basal (Mg2+-activated) adenylate cyclase (AC) activity associated with the sarcolemma, longitudinal tubules and terminal cisternae of rat skeletal muscle cells. The stimulatory effect of S-100a0 on AC activity is maximal around 5 microM S-100a0 and half-maximal around 0.2 microM S-100a0. Also, the stimulatory effect is greatest on the AC activity associated with the terminal cisternae than on the other membrane fractions studied. These data are discussed in relation to the subcellular localization of S-100a0 in muscle cells.


Subject(s)
Adenylyl Cyclases/metabolism , Magnesium/pharmacology , Muscles/enzymology , S100 Proteins/pharmacology , Animals , Cell Membrane/enzymology , Enzyme Activation/drug effects , Muscles/drug effects , Rats
5.
J Immunol ; 142(8): 2583-9, 1989 Apr 15.
Article in English | MEDLINE | ID: mdl-2564856

ABSTRACT

A study was carried out on cord blood T cell activation via the CD2-mediated pathway. Despite similar percentages of circulating CD3+ and CD2+ cells in adult and cord blood, the proliferation of cord PBMC to the anti-CD3 mAb and cord T cells to anti-CD2 mAb were defective. The T cell CD3-surface structure was normally able to control CD2-mediated activation, as its modulation by a non-mitogenic anti-CD3 mAb blocked cord PBMC proliferation induced by anti-CD2 mAb. CD2-stimulated cord T cells did not proliferate and did not produce a significant amount of IL-2 in culture, although they expressed the IL-2R. This observation was confirmed by the optimal proliferation of CD2-induced cord T cells when rIL-2 was added. Despite the alternative T cell activation pathway is monocyte-independent in adults, the defective cord T cell activation via the CD2 molecule could also be bypassed by the addition of PMA, small amounts of either autologous or allogeneic adult and cord AC or simply rIL-1 alone. Our findings provide evidence for an intrinsic functional defect in cord CD2-mediated T cell activation, which is linked to an impaired increase of free cytoplasmic calcium, as confirmed by the effectiveness of calcium ionophore A23187 in restoring a good CD2-induced cord T cell proliferation and by measurement of cellular calcium uptake after activation via the CD2 molecule. The characteristics of cord T cells revealed by this study recall the thymocyte functional pattern and may represent functional expression of the previously described phenotypic immaturity of cord T cells.


Subject(s)
Antigens, Differentiation, T-Lymphocyte/immunology , Lymphocyte Activation , Receptors, Immunologic/immunology , T-Lymphocytes/immunology , Antibodies, Monoclonal/immunology , Antigen-Presenting Cells/physiology , CD2 Antigens , CD3 Complex , Calcium/metabolism , Fetal Blood/cytology , Humans , Interleukin-1/pharmacology , Interleukin-2/biosynthesis , Interleukin-2/pharmacology , Phytohemagglutinins/pharmacology , Receptors, Antigen, T-Cell/immunology , Receptors, Interleukin-2/analysis , T-Lymphocytes/metabolism
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