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Статті в журналах з теми "Insulin carrier"

Автор: Grafiati

Опубліковано: 10 січня 2023

Оновлено: 28 січня 2023

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1

Mohsin, Mahmoud A., Yousef Haik, and Tahir Abdulrehman. "Glucose-Mediated Insulin Release Carrier." Polymer Science, Series A 60, no. 5 (September 2018): 618–27. http://dx.doi.org/10.1134/s0965545x18050097.

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2

Ostróżka-Cieślik, Aneta, and Barbara Dolińska. "Hydrogel as a Transdermal Insulin Carrier." Metabolism 116 (March 2021): 154604. http://dx.doi.org/10.1016/j.metabol.2020.154604.

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3

Wei, Wei, Lian-Yan Wang, Jie Wu, and Guang-Hui Ma. "Quaternized chitosan microspheres as insulin carrier." Journal of Biotechnology 136 (October 2008): S452. http://dx.doi.org/10.1016/j.jbiotec.2008.07.1050.

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4

Rušavý, Zdenek, Vladimir Sramek, Renata Sucha, Silvie Lacigova, and Ondrej Topolcan. "Effects of Carrier Solution on Insulin Bioavailability." Journal of Parenteral and Enteral Nutrition 28, no. 6 (November 2004): 439–41. http://dx.doi.org/10.1177/0148607104028006439.

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5

Nguyen, Vu Viet Linh, and Dai Phu Huynh. "THE ELECTROSPRAYED INSULIN-LOADED POLYCAPROLACTONE MICROPARTICLES AS A DRUG CARRIER." ASEAN Engineering Journal 12, no. 2 (June 1, 2022): 63–68. http://dx.doi.org/10.11113/aej.v12.16910.

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Drug and protein encapsulated polymeric microparticles have been considered as the most effective delivery in pharmaceutical biotechnology. In this work, we report the fabrication of polycaprolactone microparticles (PCL MPs) containing insulin via an electrospraying method. The morphology, chemical composition, physicochemical properties, insulin encapsulation and release efficiency, degradation of PCL MPs, and cytotoxicity are systematically characterized and analyzed. The results indicate that insulin do not incorporate with PCL matrix leading to the deformation of PCL MPs’ structure. In addition, insulin can be loaded into the PCL MPs with high concentration up to 25 % while it remains chemical properties when releasing from the PCL MPs. Moreover, insulin demonstrates high burst release within the first day, subsequently the release become more stable during 2-7 days. The 80% viability of the cell suggests that PCL MPs are biocompartible to cells. As a consequence, the above mentioned material is proved to be has high potential for insulin carrier in controlled release application

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6

Obermaier-Kusser, B., C. Mühlbacher, J. Mushack, E. Seffer, B. Ermel, F. Machicao, F. Schmidt, and H. U. Häring. "Further evidence for a two-step model of glucose-transport regulation. Inositol phosphate-oligosaccharides regulate glucose-carrier activity." Biochemical Journal 261, no. 3 (August 1, 1989): 699–705. http://dx.doi.org/10.1042/bj2610699.

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The insulin effect on glucose uptake is not sufficiently explained by a simple glucose-carrier translocation model. Recent studies rather suggest a two-step model of carrier translocation and carrier activation. We used several pharmacological tools to characterize the proposed model further. We found that inositol phosphate (IP)-oligosaccharides isolated from the drug Actovegin, as well as the alkaloid vinblastine, show a partial insulin-like effect on glucose-transport activity of fat-cells (3-O-methylglucose uptake, expressed as % of equilibrium value per 4 s: basal 5.8%, insulin 59%, IP-oligosaccharides 30%, vinblastine 29%) without inducing carrier translocation. On the other hand, two newly developed anti-diabetic compounds (alpha-activated carbonic acids, BM 130795 and BM 13907) induced carrier translocation to the same extent as insulin and phorbol esters [cytochalasin-B-binding sites in plasma membranes: basal 5 pmol/mg of protein, insulin 13 pmol/mg of protein, TPA (12-O-tetradecanoylphorbol 13-acetate) 11.8 pmol/mg of protein, BM 130795 10.8 pmol/mg of protein], but produce also only 40-50% of the insulin effect on glucose-transport activity (basal 5.8%, insulin 59%, TPA 23%, BM 130795 35%). Almost the full insulin effect was mimicked by a combination of phorbol esters and IP-oligosaccharides (basal 7%, insulin 50%, IP-oligosaccharides 30%, TPA 23%, IP-oligosaccharides + TPA 45%). None of these substances stimulated insulin-receptor kinase in vitro or in vivo, suggesting a post-kinase site of action. The data confirm the following aspects of the proposed model: (1) carrier translocation and carrier activation are two independently regulated processes; (2) the full insulin effect is mimicked only by a simultaneous stimulation of carrier translocation and intrinsic carrier activity, suggesting that insulin acts through a synergism of both mechanisms; (3) IP-oligosaccharides might be involved in the transmission of a stimulatory signal on carrier activity.

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7

Valuev, L. I., I. L. Valuev, L. V. Vanchugova, and I. V. Obydennova. "Modified Hydrogel as a Carrier of Oral Insulin." Applied Biochemistry and Microbiology 57, no. 3 (May 2021): 373–76. http://dx.doi.org/10.1134/s0003683821020186.

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8

Rusavý, Z., V. Srámek, R. Suchá, E. Langhamerová, R. Rokyta, and O. Topolcan. "Impact of carrier solution on biological insulin availability." Critical Care 4, Suppl 1 (2000): P166. http://dx.doi.org/10.1186/cc886.

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9

Wang, Yuanpeng, Mian Fu, Zuwei Wang, X. X. Zhu, Ying Guan, and Yongjun Zhang. "A sustained zero-order release carrier for long-acting, peakless basal insulin therapy." Journal of Materials Chemistry B 8, no. 9 (2020): 1952–59. http://dx.doi.org/10.1039/c9tb02728a.

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10

Bahar, Adeleh, Zahra Kashi, Mehrnoush Sohrab, Mehrnoush Kowsarian, Ghasem Janbabaei, and Ardeshir Ghavamzadeh. "Relationship of Being a Beta Globin Gene Carrier with Insulin Resistance." Blood 118, no. 21 (November 18, 2011): 5305. http://dx.doi.org/10.1182/blood.v118.21.5305.5305.

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Анотація:

Abstract Abstract 5305 Objective: There was a paper in favor of beta-globin gene carrier and insulin resistance. Considering the high prevalence of these individuals in north of Iran, the present study was designed to assess the relationship between a beta-globin gene carrier and developing insulin resistance. Methods: This historical cohort study was conducted on 164 people, including 82 healthy controls and 82 individuals with thalassemia minor. The two study groups were matched for age, body mass index(BMI) and family history of diabetes mellitus. Blood samples were taken for; CBC, fasting blood sugar(FBS), liver enzymes (AST, ALT), high sensitive C- reactive protein(CRP), serum insulin and a standard OGTT were performed in all. Insulin resistance was diagnosed based on homeostasis model assessment method(HOMA). TM was diagnosed if microcytic(MCV<80 fl) hypochromia(MCH<25 pg) was detected on CBC and HbA2 ≥3.5% using HPLC method. Controls had negative past medical history and normal CBC. Student T- Test and and Chi-Square test were used to compare demographic data. Relative Risk was measured to test the hypothesis. P<0.05 was considered as significant. Results: Age, gender, BMI, were similar. CRP, and AST were significantly higher in case group. (p value <0.05). The Relative Risk for diabetes mellitus and insulin resistance in the cases with minor thalassemia was 2 (CI % 95:1.8–2.5) and 2.02 (CI % 95:1.7–2.4), respectively. Conclusion: The risk of developing diabetes and insulin resistance in patients with thalassemia minor is two times greater than the general population. Considering the high serum levels of CRP in these cases, the inflammation noted in liver cells could be considered as the underlying cause of insulin resistance, impaired glucose tolerance and diabetes in these patients. Disclosures: No relevant conflicts of interest to declare.

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11

Reis, Catarina Pinto, António J. Ribeiro, Ronald J. Neufeld, and Francisco Veiga. "Alginate microparticles as novel carrier for oral insulin delivery." Biotechnology and Bioengineering 96, no. 5 (2007): 977–89. http://dx.doi.org/10.1002/bit.21164.

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12

Diedrichsen, Ragna Guldsmed, Stine Harloff-Helleberg, Ulrich Werner, Melissa Besenius, Ekkehard Leberer, Mie Kristensen, and Hanne Mørck Nielsen. "Revealing the importance of carrier-cargo association in delivery of insulin and lipidated insulin." Journal of Controlled Release 338 (October 2021): 8–21. http://dx.doi.org/10.1016/j.jconrel.2021.07.030.

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13

Obermaier-Kusser, B., C. Mühlbacher, J. Mushack, E. Rattenhuber, M. Fehlmann, and H. U. Haring. "Regulation of glucose carrier activity by AlCl3 and phospholipase C in fat-cells." Biochemical Journal 256, no. 2 (December 1, 1988): 515–20. http://dx.doi.org/10.1042/bj2560515.

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Анотація:

Recently it was speculated that activation of GTP-binding proteins and of phospholipase is involved in the transmission of a signal from the insulin-receptor kinase to effector systems in the cell. To confirm this hypothesis, we have tested the effect of AlCl3, which has been recently used as an experimental tool to activate GTP-binding proteins, on glucose transport in fat-cells. We found that AlCl3 has a partial insulin-like effect on glucose transport activity (3-O-methylglucose uptake, expressed as % of equilibrium value per 4 s: basal 9.6 +/- 2, AlCl3 29.6 +/- 4, insulin 74.0 +/- 3). The AlCl3 effect is totally blocked by pertussis toxin, whereas the insulin effect was not altered. The effect starts at [AlCl3] greater than 1 fM and reaches its maximum at 0.1 nM. Addition of phospholipase C (PLC; 50 munits/ml) also stimulated glucose transport (maximal 53.0 +/- 5%). Both substances acted faster than insulin itself (maximal values within 1 min for PLC, 2 min for AlCl3 and 5-10 min for insulin). Using the cytochalasin-B-binding assay to determine the effects of AlCl3 and PLC on the distribution of glucose carrier sites in subcellular fractions, we found that their glucose-transport-stimulating effect does not occur through an increase in glucose carrier sites in the plasma-membrane fraction. When PLC was combined with the phorbol ester TPA (12-O-tetradecanoylphorbol 13-acetate), which increases glucose carrier sites in the plasma membrane, an additive effect on glucose transport was found [PLC (50 munits/ml), 53.0 +/- 5%, TPA (1 nM), 17.3 +/- 2%; PLC + TPA, 68.0 +/- 3%]. In conclusion: (1) the data show that AlCl3, probably through activation of a pertussis-toxin-inhibitable G protein, and PLC are able to modulate the intrinsic glucose carrier activity; (2) as pertussis toxin did not modify the effect of insulin, it seems unlikely that the insulin signal on glucose transport involves activation of this specific G protein.

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14

Dahan, Wasmia Mohammed, Faruq Mohammad, AbdelRahman O. Ezzat, Ayman M. Atta, Hissah Hamad Al-Tilasi, and Hamad A. Al-Lohedan. "Enhanced Delivery of Insulin through Acrylamide-Modified Chitosan Containing Smart Carrier System." Gels 8, no. 11 (October 30, 2022): 701. http://dx.doi.org/10.3390/gels8110701.

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The present study develops on insulin-release studies from the chitosan-amide-modified stimuli-responsive polymers formed from various fatty acids including stearic acid, oleic acid, linoleic acid, and linolenic acid. This is the continuation of an earlier reported study that investigates the insulin-release profiles of chitosan-modified fatty acid amides (without stimuli responsive polymers). Following the synthesis and characterization of many different fatty acid amides with a varying amount of unsaturation, the insulin drug loading and release effects were compared among N-isopropylacrylamide (NIPAm), a thermo-responsive polymer, and 2-acrylamide-2-methylpropane sulfonic acid (AMPS), a pH-responsive polymer-modified hydrogel that is expected to enhance environmental response and the controllability of release. Finally, drug release effects were studied to investigate the drug release mechanisms with the help of five different pharmacokinetic models including the zero-order, first-order, Higuchi, Korsmeyers–Peppas, and Hixson models. The results indicate that the Higuchi and Hixson models are valid in terms of the operation of the NIPAm and AMPS matrices during the delivery of insulin.

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15

Kristensen, Mie, Ragna Guldsmed Diedrichsen, Valeria Vetri, Vito Foderà, and Hanne Mørck Nielsen. "Increased Carrier Peptide Stability through pH Adjustment Improves Insulin and PTH(1-34) Delivery In Vitro and In Vivo Rather than by Enforced Carrier Peptide-Cargo Complexation." Pharmaceutics 12, no. 10 (October 20, 2020): 993. http://dx.doi.org/10.3390/pharmaceutics12100993.

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Oral delivery of therapeutic peptides is hampered by their large molecular size and labile nature, thus limiting their permeation across the intestinal epithelium. Promising approaches to overcome the latter include co-administration with carrier peptides. In this study, the cell-penetrating peptide penetratin was employed to investigate effects of co-administration with insulin and the pharmacologically active part of parathyroid hormone (PTH(1-34)) at pH 5, 6.5, and 7.4 with respect to complexation, enzymatic stability, and transepithelial permeation of the therapeutic peptide in vitro and in vivo. Complex formation between insulin or PTH(1-34) and penetratin was pH-dependent. Micron-sized complexes dominated in the samples prepared at pH-values at which penetratin interacts electrostatically with the therapeutic peptide. The association efficiency was more pronounced between insulin and penetratin than between PTH(1-34) and penetratin. Despite the high degree of complexation, penetratin retained its membrane activity when applied to liposomal structures. The enzymatic stability of penetratin during incubation on polarized Caco-2 cell monolayers was pH-dependent with a prolonged half-live determined at pH 5 when compared to pH 6.5 and 7.4. Also, the penetratin-mediated transepithelial permeation of insulin and PTH(1-34) was increased in vitro and in vivo upon lowering the sample pH from 7.4 or 6.5 to 5. Thus, the formation of penetratin-cargo complexes with several molecular entities is not prerequisite for penetratin-mediated transepithelial permeation a therapeutic peptide. Rather, a sample pH, which improves the penetratin stability, appears to optimize the penetratin-mediated transepithelial permeation of insulin and PTH(1-34).

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16

Reis, Catarina Pinto, António J. Ribeiro, Francisco Veiga, Ronald J. Neufeld, and Christiane Damgé. "Polyelectrolyte Biomaterial Interactions Provide Nanoparticulate Carrier for Oral Insulin Delivery." Drug Delivery 15, no. 2 (January 2008): 127–39. http://dx.doi.org/10.1080/10717540801905165.

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17

JI, Ying, Chen LIU, and Yuan-ying PEI. "Artificial pulmonary surfactant as a carrier for intratracheally instilled insulin." Acta Pharmacologica Sinica 28, no. 5 (May 2007): 744–50. http://dx.doi.org/10.1111/j.1745-7254.2007.00513.x.

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18

Chung, H., J. Kim, J. Y. Um, I. C. Kwon, and S. Y. Jeong. "Self-assembled “nanocubicle” as a carrier for peroral insulin delivery." Diabetologia 45, no. 3 (March 2002): 448–51. http://dx.doi.org/10.1007/s00125-001-0751-z.

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19

Lin, Chuen-Chang, and Cheng-Wei Lin. "Preparation ofN,O-carboxymethyl chitosan nanoparticles as an insulin carrier." Drug Delivery 16, no. 8 (October 20, 2009): 458–64. http://dx.doi.org/10.3109/10717540903353090.

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20

Mühlbacher, C., E. Karnieli, P. Schaff, B. Obermaier, J. Mushack, E. Rattenhuber, and H. U. Häring. "Phorbol esters imitate in rat fat-cells the full effect of insulin on glucose-carrier translocation, but not on 3-O-methylglucose-transport activity." Biochemical Journal 249, no. 3 (February 1, 1988): 865–70. http://dx.doi.org/10.1042/bj2490865.

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Анотація:

Tumour-promoting phorbol esters have insulin-like effects on glucose transport and lipogenesis in adipocytes and myocytes. It is believed that insulin activates the glucose-transport system through translocation of glucose transporters from subcellular membranes to the plasma membrane. The aim of the present study was to investigate if phorbol esters act through the same mechanism as insulin on glucose-transport activity of rat adipocytes. We compared the effects of the tumour-promoting phorbol ester tetradecanoylphorbol acetate (TPA) and of insulin on 3-O-methylglucose transport and on the distribution of D-glucose-inhibitable cytochalasin-B binding sites in isolated rat adipocytes. Insulin (100 mu units/ml) stimulated 3-O-methylglucose uptake 9-fold, whereas TPA (1 nM) stimulated the uptake only 3-fold (mean values of five experiments, given as percentage of equilibrium reached after 4 s: basal 7 +/- 1.3%, insulin 60 +/- 3.1%, TPA 22 +/- 2.3%). In contrast, both agents stimulated glucose-transporter translocation to the same extent [cytochalasin B-binding sites (pmol/mg of protein; n = 7): plasma membranes, basal 6.2 +/- 1.0, insulin 13.4 +/- 2.0, TPA 12.7 +/- 2.7; low-density membranes, basal 12.8 +/- 2.1, insulin 6.3 +/- 0.9, TPA 8.9 +/- 0.7; high-density membranes, 6.9 +/- 1.1; insulin 12.5 +/- 1.0, TPA 8.1 +/- 0.9]. We conclude from these data: (1) TPA stimulates glucose transport in fat-cells by stimulation of glucose-carrier translocation; (2) insulin and TPA stimulate the carrier translocation to the same extent, whereas the stimulation of glucose uptake is 3-fold higher with insulin, suggesting that the stimulatory effect of insulin on glucose-transport activity involves other mechanisms in addition to carrier translocation.

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21

Mora, S., P. Kaliman, J. Chillarón, X. Testar, M. Palacín, and A. Zorzano. "Insulin and insulin-like growth factor I (IGF-I) stimulate GLUT4 glucose transporter translocation in Xenopus oocytes." Biochemical Journal 311, no. 1 (October 1, 1995): 59–65. http://dx.doi.org/10.1042/bj3110059.

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1. The heterologous expression of glucose transporters GLUT4 and GLUT1 in Xenopus oocytes has been shown to cause a differential targeting of these glucose-carrier isoforms to cellular membranes and a distinct induction of glucose transport activity. In this study we have evaluated the effect of insulin and insulin-like growth factor I (IGF-I) on glucose uptake and glucose transporter distribution in Xenopus oocytes expressing mammalian GLUT4 and GLUT1 glucose carriers. 2. Insulin and IGF-I stimulated 2-deoxyglucose uptake in GLUT4-expressing oocytes, but not in GLUT1-expressing oocytes or in water-injected oocytes. The stimulatory effect of insulin and IGF-I on 2-deoxyglucose uptake in GLUT4-expressing oocytes occurred via activation of the IGF-I receptor. 3. Subcellular-fractionation studies indicated that insulin and IGF-I stimulated translocation of GLUT4 to the cell surface of the oocyte. 4. Incubation of intact oocytes with insulin stimulated phosphatidylinositol 3-kinase activity, an effect that was blocked by the additional presence of wortmannin. Furthermore, wortmannin totally abolished the insulin-induced stimulation of 2-deoxyglucose uptake in GLUT4-expressing oocytes. 5. In this study, both the insulin-induced GLUT4 carrier translocation and GLUT4-dependent insulin-stimulated glucose transport have been reconstituted in the Xenopus oocyte. These observations, together with the fact that wortmannin, as found in adipocytes, inhibits insulin-stimulated glucose transport in oocytes, suggest that the heterologous expression of GLUT4 in oocytes is a useful experimental model by which to study the cell biology of insulin-induced GLUT4 translocation.

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22

Li, Yu Ping, Li Zhen Sun, Xiang Yuan Xiong, Zi Ling Li, Ting Kang Xing, and Li Hua Yao. "Controlled Release Characteristics of PLA-Pluronic-PLA Nano-Sized Vesicles In Vitro." Advanced Materials Research 785-786 (September 2013): 493–97. http://dx.doi.org/10.4028/www.scientific.net/amr.785-786.493.

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In the present study, controlled release characteristics of new nanosized PLA-Pluronic-PLA block copolymer vesicles comprising of amphiphilic poly (lactic acid) (PLA) and Pluronic block copolymers (PEO-PPO-PEO) have been evaluated as an oral insulin carrier. The mean size of vesicles was 78 nm for PLA-F127-PLA and 165 nm for PLA-P85-PLA copolymer. The mean insulin entrapment efficiency was 59.6% for PLA-P85-PLA and 26.4% for PLA-F127-PLA. The in vitro release characteristics of insulin from vesicles exhibited an initial burst in the range of pH 1.2-7.4 dissolution mediums. The presence of PLA-Pluronic-PLA vesicles improved the stability of insulin in the gastrointestinal fluids than that of the phosphate buffer solution (PBS) of insulin. More importantly, the released insulin from the vesicles maintained their biological activity. The results from this studies demonstrated that biodegradable PLA-Pluronic-PLA can self-assemble with insulin, form insulin-encapsulated vesicles, and is good carrier materials for oral insulin/protein delivery.

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23

Picone, Pasquale, Maria Antonietta Sabatino, Lorena Anna Ditta, Antonella Amato, Pier Luigi San Biagio, Flavia Mulè, Daniela Giacomazza, Clelia Dispenza, and Marta Di Carlo. "Nose-to-brain delivery of insulin enhanced by a nanogel carrier." Journal of Controlled Release 270 (January 2018): 23–36. http://dx.doi.org/10.1016/j.jconrel.2017.11.040.

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24

Wiessner, John H., Henderseon Mar, Denis G. Baskin, and Karl J. Hwang. "Peptide—Carrier Interaction: Induction of Liposome Fusion and Aggregation by Insulin." Journal of Pharmaceutical Sciences 75, no. 3 (March 1986): 259–63. http://dx.doi.org/10.1002/jps.2600750311.

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25

Petrus, Amanda K, Anthony R Vortherms, Timothy J Fairchild, and Robert P Doyle. "Vitamin B12 as a Carrier for the Oral Delivery of Insulin." ChemMedChem 2, no. 12 (December 10, 2007): 1717–21. http://dx.doi.org/10.1002/cmdc.200700239.

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26

Sultan, Muhammad H., Wael A. Mahdi, and Young M. Kwon. "Insulin Release from NPH Insulin-Loaded Pluronic® F127 Hydrogel in the Presence of Simulated Tissue Enzyme Activity." Processes 8, no. 10 (October 21, 2020): 1320. http://dx.doi.org/10.3390/pr8101320.

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Анотація:

Background: Despite the widespread use of newer basal insulins, Natural Protamine Hagedorn (NPH) insulin still represents a well-established basal formulation with its long history of use, featuring the native form of human insulin. However, NPH insulin exhibits an undesirable peak within hours after a single subcutaneous (s.c.) injection, which may lead to hypoglycemia followed by insufficient basal insulin delivery. This may be attributed to the s.c. enzyme activities degrading the protamine in NPH microcrystals. Methods: A thermogelling block copolymer Pluronic® F127 (PF127) was utilized as a protective carrier for NPH microcrystals and as a modulator for insulin release from NPH. NPH insulin-loaded PF127 gel was prepared with varying concentrations of the polymer (15–25%) under mild conditions. The formulations were characterized for their gelling temperature, morphology, gel erosion, and in vitro insulin release, with trypsin concentrations up to 5 U/mL. Results: Scanning electron microscopy (SEM) showed that the integrity of NPH microcrystals was maintained after preparation. The burst release of insulin from NPH was significantly attenuated over the course of ~16h in the presence of PF127 with or without enzyme activity. Conclusion: NPH-PF127 successfully resisted the acceleration of NPH crystal dissolution and insulin release in vitro in the presence of protamine-degrading enzyme activity, warranting further testing.

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27

Huang, Juan, Jian Wei Wang, Tao Gong, and Zhi Rong Zhang. "Synthesis and characterization of insulin-5-Fu conjugate, enabling insulin as multi-drug carrier via dendritic approach." Chinese Chemical Letters 18, no. 3 (March 2007): 247–50. http://dx.doi.org/10.1016/j.cclet.2006.12.026.

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28

Cappello, Anna R., Carmela Guido, Antonella Santoro, Marta Santoro, Loredana Capobianco, Daniela Montanaro, Marianna Madeo, Sebastiano Andò, Vincenza Dolce, and Saveria Aquila. "The Mitochondrial Citrate Carrier (CIC) Is Present and Regulates Insulin Secretion by Human Male Gamete." Endocrinology 153, no. 4 (February 21, 2012): 1743–54. http://dx.doi.org/10.1210/en.2011-1562.

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The mechanisms through which sperm manage their energy metabolism are poorly understood. The present study provides biochemical and morphological evidence that mitochondrial citrate carrier (CIC) is present in ejaculated human sperm and is restricted to the midpiece. The inhibition of CIC with the specific substrate analog 1,2,3-benzenetricarboxylate resulted in the reduction of cholesterol efflux, protein tyrosine phosphorylation, phospho-AKT, phospho-p60src, hyperactivated motility and acrosome reaction, suggesting a role for this mitochondrial carrier in sperm physiology. Furthermore, inhibition of CIC by 1,2,3-benzenetricarboxylate resulted in a reduction of glucose-stimulated insulin secretion and autocrine insulin secretion by sperm. Remarkably, blocking CIC also reduced glucose-6-phosphate dehydrogenase activity, probably in accordance with its regulation on insulin secretion. Capacitation and glucose metabolism were stimulated by glucose as well as citrate, the specific substrate of CIC, implying a similar action because glucose and citrate both induced insulin secretion by sperm. In the present finding, we discovered a new site of action for CIC in the regulation of metabolism, and it may be assumed that CIC works with other factors in the regulation of sperm energy metabolism to sustain capacitation process and acrosome reaction.

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29

Duan, Yan, Fanggui Ye, Yuanlin Huang, Yuemei Qin, Caimei He, and Shulin Zhao. "One-pot synthesis of a metal–organic framework-based drug carrier for intelligent glucose-responsive insulin delivery." Chemical Communications 54, no. 42 (2018): 5377–80. http://dx.doi.org/10.1039/c8cc02708k.

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A glucose-responsive metal–organic framework (MOF)-based insulin delivery nanosystem was developed via a one-pot process. The system relies on the MOF response to glucose stimulation and this can promote insulin delivery.

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30

Kaliman, P., F. Viñals, X. Testar, M. Palacín, and A. Zorzano. "Disruption of GLUT1 glucose carrier trafficking in L6E9 and Sol8 myoblasts by the phosphatidylinositol 3-kinase inhibitor wortmannin." Biochemical Journal 312, no. 2 (December 1, 1995): 471–77. http://dx.doi.org/10.1042/bj3120471.

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In this study we have used wortmannin, a highly specific inhibitor of phosphatidylinositol (PI) 3-kinase, to assess the role of this enzyme on GLUT1 glucose carrier distribution and glucose transport activity in myoblasts from two skeletal-muscle cell lines, L6E9 and Sol8. As detected in L6E9 cells, myoblasts exhibited basal and insulin-stimulated PI 3-kinase activities. Incubation of intact myoblasts with wortmannin resulted in a marked inhibition of both basal and insulin-stimulated PI 3-kinase activities. L6E9 and Sol8 myoblasts showed basal and insulin-stimulated glucose transport activities, both of them inhibited by wortmannin in a dose-dependent manner (IC50 approximately 10-20 nM). Concomitantly, immunofluorescence analysis revealed that 1 h treatment with wortmannin led to a dramatic intracellular accumulation of GLUT1 carriers (the main glucose transporter expressed in L6E9 and Sol8 myoblasts) in both cell systems. The effect of wortmannin on GLUT1 cellular redistribution was independent of the presence of insulin. The cellular distribution of two structural plasma-membrane components such as beta 1-integrin or the alpha 1 subunit of the Na(+)-K(+)-ATPase were unaffected by wortmannin in both the absence and the presence of insulin. As a whole, our results indicate that PI 3-kinase is necessary to basal and insulin-stimulated glucose transport in L6E9 and Sol8 myoblasts. Moreover, immunofluorescence assays suggest that in both cellular models there is a constitutive GLUT 1 trafficking pathway (independent of insulin) that involves PI 3-kinase and which, when blocked, locks GLUT1 in a perinuclear compartment.

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Shehata, Tamer M., Anroop B. Nair, Bandar E. Al-Dhubiab, Jigar Shah, Shery Jacob, Ibrahim A. Alhaider, Mahesh Attimarad, Heba S. Elsewedy, and Mahmoud M. Ibrahim. "Vesicular Emulgel Based System for Transdermal Delivery of Insulin: Factorial Design and in Vivo Evaluation." Applied Sciences 10, no. 15 (August 2, 2020): 5341. http://dx.doi.org/10.3390/app10155341.

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Transdermal delivery of insulin is a great challenge due to its poor permeability through the skin. The aim of the current investigation was to evaluate the prospective of insulin loaded niosome emulgel as a noninvasive delivery system for its transdermal therapy. A 23 full-factorial design was used to optimize the insulin niosome emulgel by assessing the effect of independent variables (concentration of paraffin oil, Tween 80 and sodium carboxymethyl cellulose) on dependent variables (in vitro release, viscosity and in vitro permeation). The physical characteristics of the prepared formulations were carried out by determining viscosity, particle size, entrapment efficiency, drug loading, drug release and kinetics. In vitro permeation studies were carried out using rat skin membrane. Hypoglycemic activity of prepared formulations was assessed in diabetic-induced rats. It was observed that the independent variables influenced the dependent variables. A significant difference (p < 0.05) in viscosity was noticed between the prepared gels, which in turn influenced the insulin release. The order of permeation is: insulin niosome emulgel > insulin niosome gel > insulin emulgel > insulin gel > insulin niosomes > insulin solution. The enhancement in transdermal flux in insulin niosome emulgel was 10-fold higher than the control (insulin solution). In vivo data significantly demonstrated reduction (p < 0.05) of plasma glucose level (at six hours) by insulin niosome emulgel than other formulations tested. The results suggest that the developed insulin niosome emulgel could be an efficient carrier for the transdermal delivery of insulin.

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32

Zierath, J. R., L. A. Nolte, E. Wahlström, D. Galuska, P. R. Shepherd, B. B. Kahn, and H. Wallberg-Henriksson. "Carrier-mediated fructose uptake significantly contributes to carbohydrate metabolism in human skeletal muscle." Biochemical Journal 311, no. 2 (October 15, 1995): 517–21. http://dx.doi.org/10.1042/bj3110517.

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To determine whether fructose can be utilized as a metabolic substrate for skeletal muscle in man, we investigated its incorporation into glycogen, its oxidation and lactate production in isolated human skeletal muscle. Rates of fructose oxidation and incorporation into glycogen increased in the presence of increasing fructose concentrations (0.1-1.0 mM). Lactate production increased 3-fold when extracellular fructose was increased from 0.1 to 0.5 mM. Cytochalasin B, a competitive inhibitor of hexose transport mediated by the GLUT1 and GLUT4 facilitative glucose transporters, completely inhibited insulin-stimulated glucose incorporation into glycogen and glucose oxidation (P < 0.01), but did not alter fructose incorporation into glycogen or fructose oxidation. Insulin (1000 mu-units/ml) increased glucose incorporation into glycogen 2.7-fold and glucose oxidation 2.3-fold, whereas no effect on fructose incorporation into glycogen or fructose oxidation was noted. A physiological concentration of glucose (5 mM) decreased the rate of 0.5 mM fructose incorporation into glycogen by 60% (P < 0.001), whereas fructose oxidation was not altered in the presence of 5 mM glucose. Irrespective of fructose concentration, the majority of fructose taken up underwent non-oxidative metabolism. Lactate production accounted for approx. 80% of the fructose metabolism in the basal state and approx. 70% in the insulin (1000 mu-units/ml)-stimulated state. In the presence of 5 mM glucose, physiological concentrations of fructose could account for approximately 10-30% of hexose (glucose + fructose) incorporation into glycogen under non-insulin-stimulated conditions. In conclusion, fructose appears to be transported into human skeletal muscle via a carrier-mediated system that does not involve GLUT4 or GLUT1. Furthermore, under physiological conditions, fructose can significantly contribute to carbohydrate metabolism in human skeletal muscle.

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Schwartz, Gerald P., G. Thompson Burke, Maqsood Sheikh, Lin Zong, and Panayotis G. Katsoyannis. "Synthesis of an insulin-like compound consisting of the B chain of insulin and an A chain corresponding to the A and D domains of human insulin-like growth factor I." Collection of Czechoslovak Chemical Communications 53, no. 11 (1988): 2920–35. http://dx.doi.org/10.1135/cccc19882920.

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We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound in which the A chain amino acid sequence corresponds to that of the A- and D-domains of human insulin-like growth factor I (IGF-I), and the B chain is that of bovine insulin. The compound displays reduced insulin-like activity, but considerably increased growth-promoting activity relative to insulin, and is not recognized by IGF carrier proteins. These data confirm some of our earlier conclusions regarding the role of the A-, B- and D-domains in the expression of the biological profile of IGF-I: The A-domain, but not the B- or D-domain is associated with the growth-promoting activity of IGF-I; the B-domain, but not the A- or D-domain, contains determinants for the recognition of IGF carrier proteins; and the D-domain acts to supress insulin-like activity in IGF-I.

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34

Jacobs, D. B., and C. Y. Jung. "Sulfonylurea potentiates insulin-induced recruitment of glucose transport carrier in rat adipocytes." Journal of Biological Chemistry 260, no. 5 (March 1985): 2593–96. http://dx.doi.org/10.1016/s0021-9258(18)89397-8.

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Lahiri, Susanta, Kamalika Roy, and Souvik Sen. "Complexation study on no-carrier-added astatine with insulin: A candidate radiopharmaceutical." Applied Radiation and Isotopes 66, no. 12 (December 2008): 1901–4. http://dx.doi.org/10.1016/j.apradiso.2008.06.024.

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36

Iacobazzi, Vito, Vittoria Infantino, Faustino Bisaccia, Alessandra Castegna, and Ferdinando Palmieri. "Role of FOXA in mitochondrial citrate carrier gene expression and insulin secretion." Biochemical and Biophysical Research Communications 385, no. 2 (July 2009): 220–24. http://dx.doi.org/10.1016/j.bbrc.2009.05.030.

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37

RYAN, JENNIFER, TIM MANTLE, and D. COLM COSTIGAN. "Association of plasma insulin-like growth factor 1 carrier protein in vivo." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 335–36. http://dx.doi.org/10.1042/bst0180335.

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38

Jain, Akhlesh K., Kishore B. Chalasani, Roop K. Khar, Farhan J. Ahmed, and Prakash V. Diwan. "Muco-adhesive multivesicular liposomes as an effective carrier for transmucosal insulin delivery." Journal of Drug Targeting 15, no. 6 (January 2007): 417–27. http://dx.doi.org/10.1080/10611860701453653.

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39

Pfützner, Andreas, and Thomas Forst. "Pulmonary insulin delivery by means of the Technosphere™ drug carrier mechanism." Expert Opinion on Drug Delivery 2, no. 6 (November 2005): 1097–106. http://dx.doi.org/10.1517/17425247.2.6.1097.

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40

Kettunen, Jarno L. T., Elina Rantala, Om P. Dwivedi, Bo Isomaa, Leena Sarelin, Paula Kokko, Liisa Hakaste, Päivi J. Miettinen, Leif C. Groop, and Tiinamaija Tuomi. "A multigenerational study on phenotypic consequences of the most common causal variant of HNF1A-MODY." Diabetologia 65, no. 4 (December 24, 2021): 632–43. http://dx.doi.org/10.1007/s00125-021-05631-z.

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Abstract Aims/hypothesis Systematic studies on the phenotypic consequences of variants causal of HNF1A-MODY are rare. Our aim was to assess the phenotype of carriers of a single HNF1A variant and genetic and clinical factors affecting the clinical spectrum. Methods We conducted a family-based multigenerational study by comparing heterozygous carriers of the HNF1A p.(Gly292fs) variant with the non-carrier relatives irrespective of diabetes status. During more than two decades, 145 carriers and 131 non-carriers from 12 families participated in the study, and 208 underwent an OGTT at least once. We assessed the polygenic risk score for type 2 diabetes, age at onset of diabetes and measures of body composition, as well as plasma glucose, serum insulin, proinsulin, C-peptide, glucagon and NEFA response during the OGTT. Results Half of the carriers remained free of diabetes at 23 years, one-third at 33 years and 13% even at 50 years. The median age at diagnosis was 21 years (IQR 17–35). We could not identify clinical factors affecting the age at conversion; sex, BMI, insulin sensitivity or parental carrier status had no significant effect. However, for 1 SD unit increase of a polygenic risk score for type 2 diabetes, the predicted age at diagnosis decreased by 3.2 years. During the OGTT, the carriers had higher levels of plasma glucose and lower levels of serum insulin and C-peptide than the non-carriers. The carriers were also leaner than the non-carriers (by 5.0 kg, p=0.012, and by 2.1 kg/m2 units of BMI, p=2.2 × 10−4, using the first adult measurements) and, possibly as a result of insulin deficiency, demonstrated higher lipolytic activity (with medians of NEFA at fasting 621 vs 441 μmol/l, p=0.0039; at 120 min during an OGTT 117 vs 64 μmol/l, p=3.1 × 10−5). Conclusions/interpretation The most common causal variant of HNF1A-MODY, p.(Gly292fs), presents not only with hyperglycaemia and insulin deficiency, but also with increased lipolysis and markedly lower adult BMI. Serum insulin was more discriminative than C-peptide between carriers and non-carriers. A considerable proportion of carriers develop diabetes after young adulthood. Even among individuals with a monogenic form of diabetes, polygenic risk of diabetes modifies the age at onset of diabetes. Graphical abstract

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41

Jimenez-Sánchez, Cecilia, Thierry Brun, and Pierre Maechler. "Mitochondrial Carriers Regulating Insulin Secretion Profiled in Human Islets upon Metabolic Stress." Biomolecules 10, no. 11 (November 12, 2020): 1543. http://dx.doi.org/10.3390/biom10111543.

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Chronic exposure of β-cells to nutrient-rich metabolic stress impairs mitochondrial metabolism and its coupling to insulin secretion. We exposed isolated human islets to different metabolic stresses for 3 days: 0.4 mM oleate or 0.4 mM palmitate at physiological 5.5 mM glucose (lipotoxicity), high 25 mM glucose (glucotoxicity), and high 25 mM glucose combined with 0.4 mM oleate and/or palmitate (glucolipotoxicity). Then, we profiled the mitochondrial carriers and associated genes with RNA-Seq. Diabetogenic conditions, and in particular glucotoxicity, increased expression of several mitochondrial solute carriers in human islets, such as the malate carrier DIC, the α-ketoglutarate-malate exchanger OGC, and the glutamate carrier GC1. Glucotoxicity also induced a general upregulation of the electron transport chain machinery, while palmitate largely counteracted this effect. Expression of different components of the TOM/TIM mitochondrial protein import system was increased by glucotoxicity, whereas glucolipotoxicity strongly upregulated its receptor subunit TOM70. Expression of the mitochondrial calcium uniporter MCU was essentially preserved by metabolic stresses. However, glucotoxicity altered expression of regulatory elements of calcium influx as well as the Na+/Ca2+ exchanger NCLX, which mediates calcium efflux. Overall, the expression profile of mitochondrial carriers and associated genes was modified by the different metabolic stresses exhibiting nutrient-specific signatures.

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Floyd, Suzanne, Cedric Favre, Francesco M. Lasorsa, Madeline Leahy, Giuseppe Trigiante, Philipp Stroebel, Alexander Marx, et al. "The Insulin-like Growth Factor-I–mTOR Signaling Pathway Induces the Mitochondrial Pyrimidine Nucleotide Carrier to Promote Cell Growth." Molecular Biology of the Cell 18, no. 9 (September 2007): 3545–55. http://dx.doi.org/10.1091/mbc.e06-12-1109.

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The insulin/insulin-like growth factor (IGF) signaling pathway to mTOR is essential for the survival and growth of normal cells and also contributes to the genesis and progression of cancer. This signaling pathway is linked with regulation of mitochondrial function, but how is incompletely understood. Here we show that IGF-I and insulin induce rapid transcription of the mitochondrial pyrimidine nucleotide carrier PNC1, which shares significant identity with the essential yeast mitochondrial carrier Rim2p. PNC1 expression is dependent on PI-3 kinase and mTOR activity and is higher in transformed fibroblasts, cancer cell lines, and primary prostate cancers than in normal tissues. Overexpression of PNC1 enhances cell size, whereas suppression of PNC1 expression causes reduced cell size and retarded cell cycle progression and proliferation. Cells with reduced PNC1 expression have reduced mitochondrial UTP levels, but while mitochondrial membrane potential and cellular ATP are not altered, cellular ROS levels are increased. Overall the data indicate that PNC1 is a target of the IGF-I/mTOR pathway that is essential for mitochondrial activity in regulating cell growth and proliferation.

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Casimir, Marina, Blanca Rubi, Francesca Frigerio, Gaelle Chaffard, and Pierre Maechler. "Silencing of the mitochondrial NADH shuttle component aspartate–glutamate carrier AGC1/Aralar1 in INS-1E cells and rat islets." Biochemical Journal 424, no. 3 (December 10, 2009): 459–66. http://dx.doi.org/10.1042/bj20090729.

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Transfer of reducing equivalents between cytosolic compartments and the mitochondrial matrix is mediated by NADH shuttles. Among these, the malate–aspartate shuttle has been proposed to play a major role in β-cells for the control of glucose-stimulated insulin secretion. AGC1 or Aralar1 (aspartate–glutamate carrier 1) is a key component of the malate–aspartate shuttle. Overexpression of AGC1 increases the capacity of the malate–aspartate shuttle, resulting in enhanced metabolism–secretion coupling, both in INS-1E cells and rat islets. In the present study, knockdown of AGC1 was achieved in the same β-cell models, using adenovirus-mediated delivery of shRNA (small-hairpin RNA). Compared with control INS-1E cells, down-regulation of AGC1 blunted NADH formation (−57%; P<0.05), increased lactate production (+16%; P<0.001) and inhibited glucose oxidation (−22%; P<0.01). This correlated with a reduced secretory response at 15 mM glucose (−25%; P<0.05), while insulin release was unchanged at intermediate 7.5 mM and basal 2.5 mM glucose. In isolated rat islets, efficient AGC1 knockdown did not alter insulin exocytosis evoked by 16.7 mM glucose. However, 4 mM amino-oxyacetate, commonly used to block transaminases of the malate–aspartate shuttle, inhibited glucose-stimulated insulin secretion to similar extents in INS-1E cells (−66%; P<0.01) and rat islets (−56%; P<0.01). These results show that down-regulation of the key component of the malate–aspartate shuttle AGC1 reduced glucose-induced oxidative metabolism and insulin secretion in INS-1E cells, whereas similar AGC1 knockdown in rat islets did not affect their secretory response.

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44

Kachko, Ilana, Tamar Traitel, Riki Goldbart, Liron Silbert, Marina Katz, Nava Bashan, Raz Jelinek, Assaf Rudich, and Joseph Kost. "Polymeric carrier-mediated intracellular delivery of phosphatidylinositol-3,4,5-trisphosphate to overcome insulin resistance." Journal of Drug Targeting 23, no. 7-8 (September 14, 2015): 698–709. http://dx.doi.org/10.3109/1061186x.2015.1052076.

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45

Penkov, D. N., Zh A. Akopyan, T. N. Kochegura, and A. D. Egorov. "Transcriptional control of insulin-sensitive glucose carrier Glut4 expression in adipose tissue cells." Doklady Biochemistry and Biophysics 467, no. 1 (March 2016): 145–49. http://dx.doi.org/10.1134/s1607672916020186.

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46

Jianxin Guo, Qineng Ping, Lei Zhang. "Transdermal Delivery of Insulin in Mice by Using Lecithin Vesicles as a Carrier." Drug Delivery 7, no. 2 (January 2000): 113–16. http://dx.doi.org/10.1080/107175400266687.

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47

Damge, C., C. Michel, M. Aprahamian, and P. Couvreur. "New Approach for Oral Administration of Insulin With Polyalkylcyanoacrylate Nanocapsules as Drug Carrier." Diabetes 37, no. 2 (February 1, 1988): 246–51. http://dx.doi.org/10.2337/diab.37.2.246.

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McCommis, Kyle S., Wesley T. Hodges, Daniel K. Bricker, Dona R. Wisidagama, Vincent Compan, Maria S. Remedi, Carl S. Thummel, and Brian N. Finck. "An ancestral role for the mitochondrial pyruvate carrier in glucose-stimulated insulin secretion." Molecular Metabolism 5, no. 8 (August 2016): 602–14. http://dx.doi.org/10.1016/j.molmet.2016.06.016.

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Vilaró, Senen, Manuel Palacín, Paul F. Pilch, Xavier Testar, and Antonio Zorzano. "Expression of an insulin-regulatable glucose carrier in muscle and fat endothelial cells." Nature 342, no. 6251 (December 1989): 798–800. http://dx.doi.org/10.1038/342798a0.

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Kurano, Makoto, Masumi Hara, Koichi Tsuneyama, Hideyuki Sakoda, Tomo Shimizu, Kazuhisa Tsukamoto, Hitoshi Ikeda, and Yutaka Yatomi. "Induction of insulin secretion by apolipoprotein M, a carrier for sphingosine 1-phosphate." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1841, no. 9 (September 2014): 1217–26. http://dx.doi.org/10.1016/j.bbalip.2014.05.002.

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