Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Transmembrane Ca2+ currents were investigated by means of a whole-cell clamp technique in a hamster glucagon-secreting tumor cell line (ITC-1). Two types of Ca2+ current were identified in ITC-1 cells. The low-threshold and transient (T-type) current became detectable above the potential level around -60 mV and decayed rapidly with an inactivation time constant of 95 ms (at -40 mV and 23 degrees C), while the high-threshold and long-lasting (L-type) one was activated by depolarization more positive to -30 mV with non-inactivating kinetics. The voltage dependence and kinetics of these currents were identical to those reported in guinea-pig pancreatic alpha 2 cells. Both currents were augmented by equimolar substitution of Ca2+ with Ba2+ and completely abolished by adding 1 microM La3+. Phenytoin, a well known anti-epileptic drug and a postulated T-type specific Ca2+ current antagonist, surprisingly blocked the L-type current without affecting the T-type current in ITC-1 cells. While phenytoin antagonized the L-type Ba2+ current selectively, 60% of the current remained even in supramaximal concentration range over 500 microM. The residual component of the L-type current was completely abolished by adding nifedipine.
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PMID:Phenytoin partially antagonized L-type Ca2+ current in glucagon-secreting tumor cells (ITC-1). 131 28

Nucleic acids were extracted from the tumor (IT-1) and purified to give poly (A)-containing RNA, which was subjected to protein synthesis in vitro with a wheat germ extract. Gel-filtration (Bio Gel P-30) profiles of the translated product showed the presence of glucagon-like substance, and the results of treatment of fractions with glucagon antibodies (30K or K4023) showed the possibility that translated products contained true-glucagon. This confirms glucagon synthesis in IT-1. The molecular weight of the translated glucagon was estimated to be 3,000 from the K-value. The time courses of the glucagon synthesis were examined in cultured tumor cells (ITC-1) using 3H-leucine as a tracer. A large molecular weight protein was already detected after pulse labeling for 1 h. The amount of labeled glucagon in the cells was shown to be maximum at 1 h. True-glucagon was converted at 3 h to smaller molecular weight peptides which reacted with the C-terminal antibody of glucagon. In vitro protein synthesis, peptides with molecular weights of around 10,000 were major products in 15-30 min.
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PMID:Glucagon synthesis with mRNA preparation of a glucagon-producing tumor (IT-1). 255 41