TY - JOUR AB - Exercise improves the insulin sensitivity of glucose uptake in skeletal muscle. Due to that, exercise has become a cornerstone treatment for type 2 diabetes mellitus (T2DM). The mechanisms by which exercise improves skeletal muscle insulin sensitivity are, however, incompletely understood. We conducted a systematic review to identify all genes whose gain or loss of function alters skeletal muscle glucose uptake. We subsequently cross-referenced these genes with recently generated data sets on exercise-induced gene expression and signaling. Our search revealed 176 muscle glucose-uptake genes, meaning that their genetic manipulation altered glucose uptake in skeletal muscle. Notably, exercise regulates the expression or phosphorylation of more than 50% of the glucose-uptake genes or their protein products. This included many genes that previously have not been associated with exercise-induced insulin sensitivity. Interestingly, endurance and resistance exercise triggered some common but mostly unique changes in expression and phosphorylation of glucose-uptake genes or their protein products. Collectively, our work provides a resource of potentially new molecular effectors that play a role in the incompletely understood regulation of muscle insulin sensitivity by exercise. AU - Verbrugge, S. AU - Alhusen, J.A. AU - Kempin, S.* AU - Pillon, N.J.* AU - Rozman, J.* AU - Wackerhage, H.* AU - Kleinert, M.* C1 - 63616 C2 - 51604 CY - 111 River St, Hoboken 07030-5774, Nj Usa TI - Genes controlling skeletal muscle glucose uptake and their regulation by endurance and resistance exercise. JO - J. Cell. Biochem. PB - Wiley PY - 2021 SN - 0730-2312 ER - TY - JOUR AB - Cytokines are important regulators or cell fates with high clinical and commercial relevance. However, despite decades of intense academic and industrial research, it proved surprisingly difficult to describe the biological functions of cytokines in a precise and comprehensive manner. The exact analysis of cytokine biology is complicated by the fact that. individual cytokines control many different cell fates and activate a multitude of intracellular signaling pathways. Moreover, although activating different molecular programs, different cytokines can be redundant in their biological effects. In addition, cytokines with different biological effects can activate overlapping signaling pathways. This prospect article will outline the necessity of continuous single cell biochemistry to unravel the biological functions of molecular cytokine signaling. It focuses on potentials and limitations of recent technical developments in fluorescent time-lapse imaging and single cell tracking allowing constant long-term observation of molecules and behavior of single cells. AU - Rieger, M. AU - Schroeder, T. C1 - 23470 C2 - 26552 SP - 343-352 TI - Analyzing cell fate control by cytokines through continuous single cell biochemistry. JO - J. Cell. Biochem. VL - 108 IS - 2 PB - Wiley-Blackwell PY - 2009 SN - 0730-2312 ER - TY - JOUR AU - Hughes-Fulford, M.* AU - Rodenacker, K. AU - Jütting, U. C1 - 4189 C2 - 23759 SP - 435-449 TI - Reduction of anabolic signals and alteration of osteoblast nuclear morphology in microgravity. JO - J. Cell. Biochem. VL - 99 PB - Wiley PY - 2006 SN - 0730-2312 ER - TY - JOUR AU - Siggelkow, H.* AU - Schenck, M.* AU - Rohde, M.* AU - Viereck, V.* AU - Tauber, S.* AU - Atkinson, M.J. AU - Hüfner, M.* C1 - 22038 C2 - 20635 SP - 279-294 TI - Prolonged Culture of HOS 58 Human Osteosarcoma Cells with 1,25-(OH)2-D3, TGF-Beta and Dexamethasone Reveals Physiological Regulation of Alkaline Phosphatase, Dissociated Osteocalcin Gene Expression and Protein Synthesis and Lack of Mineralization. JO - J. Cell. Biochem. VL - 85 PB - Wiley PY - 2002 SN - 0730-2312 ER - TY - JOUR AU - Dittmann, K.H. AU - Petrides, P.E. C1 - 17774 C2 - 10683 SP - 122 TI - HL-60 Cells Constitutively Relase a Polypeptide which Disturbs the Interaction of Various Target Cells with their Extracellular Matrix. JO - J. Cell. Biochem. VL - 13 PY - 1989 SN - 0730-2312 ER - TY - JOUR AB - In this report, we have examined whether (6R)-tetrahydrobiopterin (H4biopterin) modulates the binding of interleukin 2 to high-affinity sites of the cloned mouse cytotoxic T-lymphocyte clone CTLL-2. Scatchard plot analysis of the equilibrium binding data reveals increased affinity when the cells are exposed simultaneously to interleukin 2 and to the pterin. The K(d) values are statistically significantly reduced from 1.4 x 10-11M to 0.78 x 10-11M interleukin 2. The dissociation kinetics of the ligand were followed at 4°C after equilibrium binding under high-affinity conditions (1.2 x 10-10M interleukin 2). In the presence of H4 biopterin, the dissociation rate constant (k-1) decreases from 6.2 x 10-3 min-1 to 3.0 x 10-3 min-1 and the half-time for dissociation increases from 106.8 min to 218.0 min. As a third approach interleukin 2 was bound to the surface of cells under high-affinity conditions by incubation in the cold and the internalization kinetics upon warming were determined. Sigmoidal-shaped kinetics of endocytosis in control cells indicate that the internalization rates increase only gradually. The presence of H4 biopterin causes an apparent immediate transition from higher-order kinetics to a linear response so that maximum internalization rates are reached immediately upon warming. The data show that lymphocyte-derived H4 biopterin in vitro at concentrations ranging from 2-8 x 10-7M modulates interleukin 2 high-affinity binding and that H4 biopterin potentially participates in the control of interleukin 2 receptor assembly. AU - Ziegler, I. AU - Schwulera, U. C1 - 42086 C2 - 0 SP - 103-112 TI - Modulation of interleukin 2 high-affinity binding by lymphocyte-derived tetrahydrobiopterin: Pterins as potential participants in the control of interleukin 2 receptor assembly. JO - J. Cell. Biochem. VL - 41 IS - 2 PY - 1989 SN - 0730-2312 ER - TY - JOUR AB - After iodine oxidation, biopterin, 6-hydroxymethylpterin, and 6-formylpterin were identified in mouse spleen lymphocytes by means of reverse-phase HPLC, Crithidia assay, and oxidative degradation. Concanavalin A activation induces a 30-fold increase in the pteridine amounts; biopterin as well as the sum of the carbinol and the aldehyde attain levels of 6-8 X 10(-12) mol/10(6) cells. The most rapid increase occurs during the first 24 hr. Thus, pteridine accumulation precedes the period of lymphocyte proliferation; maximum DNA synthesis was found after 72 hr. Biopterin remains largely inside the cells, whereas 6-hydroxymethylpterin and 6-formylpterin were found in the supernatant if the stimulated cells were subsequently incubated in a phosphate buffered salt solution (PBS). Isoxanthopterin was found in the PBS supernatant of control cells that previously were kept in medium alone rather than subjected to lectin stimulation. Only minimal amounts were found inside these cells, and this pterin was absent from the stimulated lymphocytes. The early increase in cellular pteridines and their differential release may well provide the basis for their modulating effect on interleukin-2 activity (Ziegler I, et al: Lymphokine Research 3:284, 1984). AU - Ziegler, I. C1 - 41566 C2 - 38233 SP - 197-206 TI - Pteridine formation during lectin-induced lymphocyte activation. JO - J. Cell. Biochem. VL - 28 IS - 3 PY - 1985 SN - 0730-2312 ER -