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Stempniak В. and Guzek J. W.: Intracerebroventricular insulin affects the neurohypophysial vasopressin content in euhydrated and dehydrated rats. Acta Physiol. Pol., Rats euhydrated or dehydrated for four days were given intracerebroventricular insulin once daily in a dose of 100 ng (not affecting blood sugar level). In euhydrated rats, insulin decreased significantly the neurohypophysial vasopressin content. In dehydrated animals the neurohypophysial content depleted by deprivation of water could be further reduced by intracerebroventricular treatment with insulin. These results may suggest a possible regulatory role of brain insulin in the mechanisms of vasopressin release.
The insulin receptor (IR) and the insulin-like growth factor receptor I (IGF-IR) have different functions in cell growth, apoptosis, differentation, and transformation. Although some of these differences may be explained by the relative level of receptor expression and receptor structure (a and b subunits), they may also be attributed to differences in intracellular signals generated by insulin and IGF-I. The presence of hybrid receptors (IR ab subunits and IGF-IR ab subunits) making up the heterotetramers has added a new dimension to our understanding of the functional roles of these receptors. However, to date the results of efforts to understand the differences between these two closely related receptors have indicated mostly similarities. For example, both receptors utilize IRS-1/IRS-2 and Shc as immediate downstream adaptors, leading to activation of the Ras, Raf, ERK kinases and PI-3 kinase pathways. We have used the yeast two hybrid system to identify proteins which bind to the activated IGF-IR but not to the IR. The cytoplasmic domain of the IGF-IR was used to screen a human fetal brain library and two isoforms of the 14-3-3 family were identified. 14-3-3 proteins are a highly conserved family of proteins which have recently been shown to interact with other components of the mitogenic and apoptotic signaling pathways, including Raf, BAD, Bcr/Bcr-Abl, middle-T antigen, Ksr, PKC, PI-3 kinase, ASK1 kinase, and cdc25C phosphatase. We also identified human Grb10, an adaptor protein with SH2 domain associated with the IGF-IR b subunit. Smith's laboratory showed that Grb10 preferentially binds to the IR in intact cells. Using the interaction trap screen (active cytoplasmic domain of the IGF-IR) 55PIK and SOCS-2 proteins were also identified. However, 55PIK and SOCS-2 also interact with the IR in the yeast two hybrid system. These studies raise the possibility that 14-3-3 and Grb10 may play a role in insulin and IGF-I signal transduction and may underlie the observed differences.
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Inhaled insulin - does it become reality?

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Healthy, and insulin-deficient (streptozotocin-induced diabetic, STZ) Sprague-Dawley rats were used to investigate the effects of different doses of ß-endorphin (25 and 50 µg/kg) on plasma ß-endorphin, insulin, glucagon, and glucose levels at 15- and 30-min time points. In experimental groups, plasma ß-endorphin levels were higher at the 15-min than at the 30-min time point in healthy rats; however, in STZ-diabetic rats, ß-endorphin levels were lower at 15 min than at 30 min, indicating that intraperitoneal absorption of ß-endorphin differed between healthy and insulin-deficient rats, ß-endorphin did not affect plasma glucose, insulin, or glucagon at either dose in the healthy group. In the insulin-deficient rats, ß-endorphin at 50 µg/kg reduced plasma glucose levels at the 30-min time point compared to the 25 µg/kg dose, without affecting plasma insulin. Moreover, ß-endorphin at 50 µg/kg decreased plasma glucagon levels at the 15-min time point in comparison to the 25 µg/kg dose in insulin-deficient rats. Plasma glucose levels may be reduced in insulin-deficient rats at high ß-endorphin levels regardless of insulin status.
Maćkowiak P.: Amino acid-induced insulin release from the perfused irat pancreas. The influence of phenylalanine and tyrosine. Acta physiol, pol. The effects of L or D phenylalanine and L tyrosine on insulin release from the perfused rat pancreas were investigated. It was found that in the presence of D-glucose, all three amino-acids stimulate insulin secretion. After L-Phe had been removed from perfusate in the presence or absence of L-Tyr, the secondary rise of insulin release (an “off response”) was noticed. This phenomenon did not follow to either D-Phe or L-Tyr.
Diabetes mellitus is the world’s largest endocrine disorder resulting in multiple aetiologies, involving metabolic disorders of carbohydrate, fat and protein. All forms of diabetes are due to a decrease in the circulating concentration of insulin (insulin deficiency) and a decrease in the response of peripheral tissues to insulin i.e., insulin resistance. According to the World Health Organization projections, the prevalence of diabetes is likely to increase by 35% by the year 2025. In this study, the streptozotocin (STZ)-induced diabetic rats, the activities of membrane-bound adenosine triphosphatases (ATPases) are altered in erythrocytes and in tissues such as liver and kidney. Albino Wistar rats were rendered diabetic by a single intraperitoneal injection of STZ (40 mg/kg body weight). Diabetic rats exhibited significantly (p<0.05) increased levels of plasma glucose and decreased levels of plasma insulin. The activities of total ATPases, (Na++K+)-ATPase, Ca2+-ATPase and Mg2+-ATPase were significantly (p<0.05) decreased in diabetic control rats. Control and diabetic rats were treated with camel milk (250 mL/day) for a period of 45 days. A group of diabetic rats were also treated with glibenclamide (600 μg/kg body weight). After the treatment period, a significant (p<0.05) decrease in the levels of glucose and increase in the levels of plasma insulin and the activities of ATPases in erythrocytes and tissues were observed in diabetic rats treated with camel milk. A similar effect is also observed in the glibenclamide treated rats. But, control rats treated with camel milk did not show any significant (p<0.05) effect in any of the parameters studied. Our study shows that camel milk has the potential to restore the deranged activities of membrane-bound ATPases in STZ-diabetic rats. Further detailed investigation is necessary to find out its mechanism of action.
The fraction of free fatty acids (FFA) is present in skeletal muscles. However, there is almost no data regarding regulation in the content of this intramuscular lipid pool. We took advantage of the isolated muscle preparation to examine whether: a) increasing exogenous concentration of FFA (500µM or 700µM, 30min) b) insulin (10.00 I.U./L, 30min), c) adrenalin (4.4 nM, 30min), or d) contractions (200ms, tetani, 1Hz, 30min), affect the FFA content inside myocytes. Incubation of soleus (S) and extensor digitorum longus (EDL) with increasing concentrations of exogenous FFA (from 500µM to 700µM) resulted in an increase in the total FFA fraction in both muscles studied (by 280.2% and 259.1%, respectively). In contracting muscles FFA pool was significantly reduced both in S (by 73.1%) and in EDL (by 31.1%). Neither stimulation by adrenalin nor insulin affected the total content of FFA fraction in the muscles examined. We conclude that a) increased availability of exogenous FFA at the sarcolemma level results in an increase in the size of intramuscular FFA fraction b) the intracellular FFA fraction is utilized by contracting muscles with regard to the fiber composition and to a greater extent in more oxidative muscles, c) FFA fraction remains stable upon stimulation by insulin or adrenalin.
Insulin-like growth factor I (IGF-I) stimulates multiplication of the human osteosarcoma cell line, MG-63, by acting through IGF-I receptor. We have characterized IGF-I stimulated phosphorylation of IRS-1, activation of Ras cycle and phosphorylation of c-Jun in this cell line. Serum starved MG-63 cells were (1) IGF-I stimulated and lysates were immunoprecipitated with polyclonal IRS-1 antibody or (2) metabolically labeled with [32P]orthophosphoric acid and then cells were treated with IGF-I. Cell lysates were immunoprecipitated with p21Ras antibody(Y13-259) and bound nucleotides were analysed by thin layer chromatography. We demonstrated tyrosine phosphorylation of IRS-1/2 immunoprecipitated from MG-63 cells stimulated with IGF-I. We also showed an increased level of GTP in p21Ras immunoprecipitates from IGF-I treated cells. Nuclear extracts prepared from 32P-labeled cells before and after addition of IGF-I were immunoprecipitated with c-Jun antibody. After electrophoresis and autoradiography, phosphorylation of the c-Jun band was seen to be IGF-I independent. Phosphoamino acid analysis of the c-Jun band showed that phosphoserine was the major species.
In this study, the effects of xylazine on serum levels of triiodothyronine (T3), tetraiodothyronine (T4), insulin (INS), and glucagon (GN) in dogs were investigated. The dogs before injection were used as control group (0 h). The dogs were injected with xylazine at 3 mg/kg, then blood was collected from the peripheral veins at 0.5, 2, 8, 24, 48, 72, and 120 h after the injection. Serum T3, T4, INS, and GN were measured by ELISA. The results revealed that the T3 level decreased in serum 0.5 h after the injection (P<0.05), while the change in T4 was not significant. The secretion of INS increased 8 h after the injection (P<0.05). The GN level increased 2 h and 8 h after the injection (P<0.05). However, all of these changes returned to the norm after 24 h.
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