Cited by 215Metabolism, Diabetes, and CancerDiabetes, Cardiovascular Risks, and LipoproteinsGrowth Hormone and Insulin-like Growth Factors

The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.

Studies on the mechanism of insulin resistance in the liver from humans with noninsulin-dependent diabetes. Insulin action and binding in isolated hepatocytes, insulin receptor structure, and kinase activity.

Open access

Caro, J F, Ittoop, O, Pories, W J, Meelheim, D, Flickinger, E G, Thomas, F, Jenquin, M, Silverman, J F, Khazanie, P G, Sinha, M K·1986·Journal of Clinical Investigation

DOI 10.1172/jci112558PMC PMC329556

Open this paper in CoChat — free account Open PDF

Abstract

We have developed a method to isolate insulin-responsive human hepatocytes from an intraoperative liver biopsy to study insulin action and resistance in man.Hepatocytes from obese patients with noninsulin-dependent diabetes were resistant to maximal insulin concentration, and those from obese controls to submax- imal insulin concentration in comparison to nonobese controls.Insulin binding per cell number was similar in all groups.How- ever, insulin binding per surface area was decreased in the two obese groups because their hepatocytes were larger.In addition, the pool of detergent-extractable receptor was further decreased in diabetics.Insulin receptors in all groups were unaltered as determined by affinity-labeling methods.However, insulin-stim- ulated insulin receptor kinase activity was decreased in diabetics.Thus, in obesity, decreased surface binding could explain re- sistance to submaximal insulin concentrations.In diabetes, di- minished insulin-stimulated protein kinase activity and decreased intracellular pool of receptors could provide an explanation for postinsulin-binding defect(s) of insulin action in human liver. Methods Materials. a-[ I 14C]Aminoisobutyric acid (51.6 mCi/mmol), carrier-freeNa 125I, [methoxyl-3H]inulin (186.4 mCi/g), 3-0-['4C] methyl-D-glucose (58.0 mCi/mmol), L-[U-_4C]leucine (300 mCi/mmol), and [I-_4C]acetic acid, sodium salt (56.0 mCi/mmol) were obtained from New England Nuclear, Boston, MA.Crude collagenase (type IV, lots 124F-6807, 25F-6806, 25F-68 17, 44F-68 12) and deoxyribonuclease were obtained from Sigma Chemical Co., St. Louis, MO; dispase was purchased from Boeh- ringer Mannheim Biochemicals, Indianapolis, IN; and soybean trypsin inhibitor from Worthington Biomedical Corp., Freehold, NJ.Fraction V bovine serum albumin (BSA) was obtained from Armour Pharma- ceutical, Co., Kankakee, IL, and it was further purified by charcoal treat- ment (23).Crystalline porcine insulin was kindly provided by Dr. Ronald Chance of Eli Lilly & Co., Indianapolis, IN.All other chemicals were reagent grade.Human subjects.11 morbidly obese patients with NIDDM and an equal number of morbidly obese patients without diabetes were studied.The clinical and biochemical data ofthese patients are presented in Table I.These patients were admitted to the hospital to undergo gastric bypass for the treatment of morbid obesity.We also studied a nonobese non- diabetic group composed of four subjects who had uncomplicated gallstone disease and were admitted for elective cholecystectomy, and five brain-dead organ donors.The biochemical data on the liver ofthese two clinically different subgroups of nonobese subjects were identical.Thus, they have been combined and referred to as the nonobese comparison group.The value ofthe organ donor's liver should be underscored because we have the entire liver from the donors.This tissue has been fundamentalInsulin Resistance in Liverfrom Noninsulin-dependent Diabetes 249

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1172/jci112558

Cites

74 of 74 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

Insulin Sensitivity and Insulin Binding to Monocytes in Maturity-Onset Diabetes
Defronzo, R., Deibert, D., Hendler, R., Felig, P., & Soman, V. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109394 · Cited by 188
Retracted
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
Assay of proteins in the presence of interfering materials
Bensadoun, A., & Weinstein, D. (1976) · Analytical Biochemistry · doi:10.1016/s0003-2697(76)80064-4 · Cited by 3,191
Immunoassay of endogenous plasma insulin in man
Yalow, R. S., & Berson, S. A. (1960) · Journal of Clinical Investigation · doi:10.1172/jci104130 · Cited by 3,041
Removal of Fatty Acids from Serum Albumin by Charcoal Treatment
Chen, R. F. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81445-x · Cited by 2,093
Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus.
DeFronzo, R. A., Gunnarsson, R., Björkman, O., Olsson, M., & Wahren, J. (1985) · Journal of Clinical Investigation · doi:10.1172/jci111938 · Cited by 1,167
Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own Receptor
Kasuga, M., Karlsson, F. A., & Kahn, C. R. (1982) · Science · doi:10.1126/science.7031900 · Cited by 1,132
Plasma Insulin Responses to Oral and Intravenous Glucose: Studies in Normal and Diabetic Subjects*
Perley, M. J., & Kipnis, D. M. (1967) · Journal of Clinical Investigation · doi:10.1172/jci105685 · Cited by 917
Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system
Kasuga, M., Zick, Y., Blithe, D., Crettaz, M., & Kahn, C. R. (1982) · Nature · doi:10.1038/298667a0 · Cited by 680

Flagged first, then by citations

Show all 74 references

Sorted by citations

Items 101–200 of 215

Metabolic Aspects of Bariatric Surgery
Folli, F. B., Pontiroli, A. E., & Schwesinger, W. H. (2007) · Medical Clinics of North America · doi:10.1016/j.mcna.2007.01.005 · Cited by 33
Insulin binding and receptor tyrosine kinase activity in rat liver and skeletal muscle: Effect of starvation
Balage, M., Grizard, J., Sornet, C., Simon, J., Dardevet, D. P., & Manin, M. (1990) · Metabolism · doi:10.1016/0026-0495(90)90250-g · Cited by 34
Angiotensin II Inhibits Insulin Receptor Signaling in Adipose Cells
Gutiérrez-Rodelo, C., Arellano-Plancarte, A., Hernández-Aranda, J., Landa-Galván, H. V., Parra-Mercado, G. K., Moreno-Licona, N. J., Hernández-González, K. D., Catt, K. J., Villalobos‐Molina, R., & Olivares-Reyes, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116048 · Cited by 33
Pathogenesis of Hyperglycemia in Genetically Obese-Hyperglycemic Rats, Wistar Fatty: Presence of Hepatic Insulin Resistance.
Sugiyama, Y., SHIMURA, Y., & Ikeda, H. (1989) · Endocrinologia Japonica · doi:10.1507/endocrj1954.36.65 · Cited by 33
Regulation of the Insulin Receptor Kinase by Hyperinsulinism
Treadway, J. L., Whittaker, J., & Pessin, J. E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63822-0 · Cited by 32
Insulin Resistance and the Pathogenesis of Non-Insulin Dependent Diabetes Mellitus: Cellular and Molecular Mechanisms
Olefsky, J. M. (1993) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-2910-1_10 · Cited by 30
Insulin receptor kinase defects in insulin‐resistant tissues and their role in the pathogenesis of NIDDM
Häring, H.-U., & Obermaier-Kusser, B. (1989) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610050502 · Cited by 29
Treatment of streptozotocin-diabetic rats with metformin restores the ability of insulin to inhibit adenylate cyclase activity and demonstrates that insulin does not exert this action through the inhibitory guanine nucleotide regulatory protein Gi
Gawler, D. J., Milligan, G., & Houslay, M. D. (1988) · Biochemical Journal · doi:10.1042/bj2490537 · Cited by 30
Intrinsic kinase activity of the insulin receptor
O'Hare, T., & Pilch, P. F. (1990) · International Journal of Biochemistry · doi:10.1016/0020-711x(90)90132-m · Cited by 29
Alterations in the Hepatic Insulin Receptor Kinase in Genetic and Acquired Obesity in Rats*
Hurrell, D. G., Pedersen, O. B., & Kahn, C. R. (1989) · Endocrinology · doi:10.1210/endo-125-5-2454 · Cited by 29
Effect ofin VivoVanadate Treatment on Insulin Receptor Tyrosine Kinase Activity in Partially Pancreatectomized Diabetic Rats*
Cordera, R., Andraghetti, G., DeFronzo, R. A., & Rossetti, L. (1990) · Endocrinology · doi:10.1210/endo-126-4-2177 · Cited by 29
Defects of insulin's signal transduction in old rat livers
Nadiv, O., Cohen, O., & Zick, Y. (1992) · Endocrinology · doi:10.1210/endo.130.3.1311243 · Cited by 28
Insulin receptor tyrosine-kinase activity is altered in both muscle and adipose tissue from non-obese normoglycaemic insulin-resistant subjects
Grasso, G., Frittitta, L., Anello, M., Russo, P., Sesti, G., & Trischitta, V. (1995) · Diabetologia · doi:10.1007/bf02369353 · Cited by 27
Topiramate-Induced Modulation of Hepatic Molecular Mechanisms: An Aspect for Its Anti-Insulin Resistant Effect
El-Abhar, H. S., & Schaalan, M. F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037757 · Cited by 27
A Microtiter Well Assay System to Measure Insulin Activation of Insulin Receptor Kinase in Intact Human Mononuclear Cells: Decreased Insulin Effect in Cells From Patients With NIDDM
Klein, H. H., Kowalewski, B., Drenckhan, M., Neugebauer, S., Matthaei, S., & Kotzke, G. (1993) · Diabetes · doi:10.2337/diab.42.6.883 · Cited by 27
Methods for studying protein synthesis and degradation in liver and skeletal muscle
Hasselgren, P.-O., Pedersen, P., Sax, H. C., Warner, B. W., & Fischer, J. E. (1988) · Journal of Surgical Research · doi:10.1016/0022-4804(88)90136-9 · Cited by 27
Heterogeneity of human liver, muscle, and adipose tissue insulin receptor
Caro, J., Raju, S. M., Sinha, M. K., Goldfine, I. D., & Dohm, G. L. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(88)90567-0 · Cited by 26
Self-citation
Insulin resistance in non-insulin-dependent diabetes mellitus
Alzaid, A. (1996) · Acta Diabetologica · doi:10.1007/bf00569416 · Cited by 25
Guanine nucleotide binding regulatory proteins in liver from obese humans with and without type II diabetes: Evidence for altered “cross‐talk” between the insulin receptor and Gi‐proteins
Caro, J. F., Raju, M. S., Caro, M., Lynch, C. J., Poulos, J., Exton, J. H., & Thakkar, J. K. (1994) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240540307 · Cited by 25
Self-citation
Insulin receptor tyrosine kinase activity is reduced in monocytes from non-obese normoglycaemic insulin-resistant subjects
Frittitta, L., Grasso, G., Munguira, M. E., Vigneri, R., & Trischitta, V. (1993) · Diabetologia · doi:10.1007/bf00401061 · Cited by 25
Characterisation of insulin-like growth factor I receptor in skeletal muscles of normal and insulin resistant subjects
Livingston, N., Pollare, T., Lithell, H., & Arner, P. (1988) · Diabetologia · doi:10.1007/bf00265369 · Cited by 25
Glucose-induced stimulation of human insulin-receptor mRNA and tyrosine kinase activity in cultured cells
Mouzon, S. H., Mrejen, C., Alengrin, F., & OBBERGHEN, E. V. (1995) · Biochemical Journal · doi:10.1042/bj3050119 · Cited by 24
Effect of chlorpropamide on glucose transport in rat adipocytes in the absence of changes in insulin binding and receptor-associated tyrosine kinase activity
Jacobs, D. B., Hayes, G. R., & Lockwood, D. H. (1987) · Metabolism · doi:10.1016/0026-0495(87)90165-x · Cited by 24
The impact of obesity on the pathogenesis of non‐insulin‐dependent diabetes mellitus: A review of current hypotheses
Pedersen, O. B. (1989) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610050603 · Cited by 23
Mechanisms of Insulin Resistance Leading to Hypertension: What We Can Learn from Experimental Models
Sechi, L. A., & Bartoli, E. (1997) · Journal of Investigative Medicine · doi:10.1177/108155899704500503 · Cited by 22
Normal insulin receptor tyrosine kinase activity and glucose transporter (GLUT 4) levels in the skeletal muscle of hyperinsulinaemic hypertensive rats
Bader, S. A., Scholz, R., Kellerer, M., Tippmer, S., Kristian, R. E. T. T., Mathaei, S., Freund, P., & Häring, H.-U. (1992) · Diabetologia · doi:10.1007/bf00429089 · Cited by 22
Tissue Specific Differences in the Insulin Receptor Kinase Activated in Vitro and in Vivo*
Burant, C., Treutelaar, M. K., & Buse, M. G. (1988) · Endocrinology · doi:10.1210/endo-122-2-427 · Cited by 21
Insulin resistance in a case of coexisting insulinoma and type 2 diabetes
Grunberger, G. (1993) · Acta Diabetologica · doi:10.1007/bf00569936 · Cited by 20
Lipid-induced insulin resistance in cultured hepatoma cells is associated with a decreased insulin receptor tyrosine kinase activity.
Hubert, P., Bruneau, C., Crémel, G., MARCHAND‐BRUSTEL, Y. L., & Staedel, C. (1991) · Cell Regulation · doi:10.1091/mbc.2.1.65 · Cited by 20
The case for metabolic hypertension: Is it time to restructure the hypertension paradigm?
Pool, P. E. (1993) · Progress in Cardiovascular Diseases · doi:10.1016/0033-0620(93)90020-e · Cited by 20
Effects of exercise training on the relationship between insulin binding and insulin-stimulated tyrosine kinase activity in rat skeletal muscle
dos Santos, R. F., Mondon, C. E., Reaven, G. M., & Azhar, S. (1989) · Metabolism · doi:10.1016/0026-0495(89)90128-5 · Cited by 20
Protein-tyrosine Phosphatase-1B acts as a negative regulator of insulin signal transduction
Byon, J. C. H., Kusari, A. B., & Kusari, J. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5647-3_11 · Cited by 19
Does the insulin-mimetic action of vanadate involve insulin receptor kinase?
Pugazhenthi, S., & Khandelwal, R. L. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076772 · Cited by 19
Insulin receptor and postbinding defects in KK mouse adipocytes and improvement by ciglitazone
Taketomi, S., Fujita, T., & Yokono, K. (1988) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(88)80051-2 · Cited by 18
Insulin Resistance: A Look at the Role of Insulin Receptor Kinase
Reddy, S. S. ‐., & Kahn, C. R. (1988) · Diabetic Medicine · doi:10.1111/j.1464-5491.1988.tb01069.x · Cited by 18
Polyunsaturated fatty acid regulation of lipogenic enzyme gene expression in liver of genetically obese rat
Iritani, N., Hosomi, H., Fukuda, H., & Ikeda, H. (1995) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(94)00203-b · Cited by 18
Atorvastatin alters gene expression and cholesterol synthesis in primary rainbow trout (Oncorhynchus mykiss) hepatocytes
Al-Habsi, A. A., Massarsky, A., & Moon, T. W. (2017) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2017.08.007 · Cited by 16
Lipoprotein metabolism in non-insulin-dependent diabetes mellitus
BARAKAT, H., Vadlamudi, S., MacLean, P. S., MACDONALD, K., & Pories, W. J. (1996) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(96)00117-9 · Cited by 16
Self-citation
Investigation of FcRn‐Mediated Transepithelial Mechanisms for Oral Nanoparticle Delivery Systems
Yu, Y., Wu, Z., Wu, J., Shen, X., Wu, R., Zhou, M., Li, L., & Huang, Y. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202100145 · Cited by 15
Individuals with only one allele for a functional insulin receptor have a tendency to hyperinsulinaemia but not to hyperglycaemia
Deprez, R. H. L., van Loon, B. J. P., van der Zon, G. C. M., Möller, W. J., Lindhout, D., Klinkhamer, M. P., Krans, H. M. J., & Maassen, J. A. (1989) · Diabetologia · doi:10.1007/bf00274534 · Cited by 15
Effect Of Altered Nutritional States On Insulin Receptors
Adamo, M. L., LeRoith, D., Simon, J., & Roth, J. (1988) · Annual Review of Nutrition · doi:10.1146/annurev.nu.08.070188.001053 · Cited by 15
Metabolic and Molecular Pathogenesis of Type 2 Diabetes Mellitus
DeFronzo, R. A., Mandarino, L. J., & Ferrannini, E. (2003) · Wiley eBooks · doi:10.1002/0470862092.d0310 · Cited by 15
Insulin resistance and noninsulin‐dependent diabetes mellitus: Which horse is pulling the cart?
Garvey, W. T. (1989) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610050807 · Cited by 15
Tyrosine kinase activity of insulin receptors from an insulin-resistant patient with leprechaunism
Cama, A., & Taylor, S. I. (1987) · Diabetologia · doi:10.1007/bf00277320 · Cited by 15
Pathogenesis of Type 2 Diabetes Mellitus
DeFronzo, R. A. (2018) · Endocrinology · doi:10.1007/978-3-319-45015-5_8 · Cited by 14
Parent-of-origin specific linkage and association of the IGF2 gene region with birth weight and adult metabolic risk factors
Souren, N. Y., Paulussen, A. D. C., Steyls, A., Loos, R. J. F., Brandão, R. D., Gielen, M., Smeets, H. J. M., Beunen, G. P., Fagard, R. H., Derom, C. A., et al. (2009) · International Journal of Obesity · doi:10.1038/ijo.2009.126 · Cited by 14
Liver Insulin Receptor Tyrosine Kinase Activity in a Rat Model of Type II Diabetes Mellitus and Obesity
Adamo, M. L., Shemer, J., Aridor, M., Dixon, J., Carswell, N., Bhathena, S. J., Michaelis, O. E., & LeRoith, D. (1989) · Journal of Nutrition · doi:10.1093/jn/119.3.484 · Cited by 14
What is the role of the insulin receptor tyrosine kinase?
Espinal, J. (1988) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(88)90170-3 · Cited by 14
Pathogenesis of type 2 diabetes mellitus
DeFronzo, R. A. (2015) · Wiley eBooks · doi:10.1002/9781118387658.ch25 · Cited by 17
Studies on the mechanism of action of sulphonylureas in type II diabetic subjects: gliquidone
Bonora, E., Moghetti, P., Querena, M., Zenere, M. B., Cacciatori, V., Tosi, F., Travia, D., Zoppini, G., & Muggeo, M. (1992) · Journal of Endocrinological Investigation · doi:10.1007/bf03348644 · Cited by 14
Insulin Resistance in Polycystic Ovarian Disease
Bhatia, V. (2005) · Southern Medical Journal · doi:10.1097/01.smj.0000177251.15366.85 · Cited by 13
[3H]myoinositol incorporation into phospholipids in liver microsomes from humans with and without type II diabetes. The lack of synthesis of glycosylphosphatidylinositol, precursor of the insulin mediator inositol phosphate glycan.
Thakkar, J. K., Raju, M. S., Kennington, A. S., Foil, B., & Caro, J. F. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39386-x · Cited by 13
Self-citation
Hepatocyte-secreted FAM3D ameliorates hepatic steatosis by activating FPR1-hnRNP U-GR-SCAD pathway to enhance lipid oxidation
Hu, Y., Li, J., Li, X., Wang, D., Xiang, R., Liu, W., Hou, S., Zhao, Q., Yu, X., Xu, M., et al. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155661 · Cited by 12
Orally active insulin mimics: where do we stand now?
Balasubramanyam, M., & Mohan, V. (2001) · Journal of Biosciences · doi:10.1007/bf02703748 · Cited by 12
Glyburide but not ciglitazone enhances insulin action in the liver independent of insulin receptor kinase activation
Caro, J., Ittoop, O. R. R., & Sinha, M. K. (1989) · Metabolism · doi:10.1016/0026-0495(89)90095-4 · Cited by 12
Self-citation
Insulin stimulated protein phosphorylation in human plasma liver membranes: Detection of endogenous or plasma membrane associated substrates for insulin receptor kinase
Caro, J., Shafer, J. A., Taylor, S. I., Raju, S. M., Perrotti, N., & Sinha, M. K. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90509-2 · Cited by 12
Self-citation
Pathogenesis of Type 2 Diabetes Mellitus
DeFronzo, R. A. (2018) · Endocrinology · doi:10.1007/978-3-319-27317-4_8-1 · Cited by 11
Insulin resistance of glucose metabolism in isolated brown adipocytes of lactating rats. Evidence for a post-receptor defect in insulin action
Burnol, A., Ebner, S., Kandé, J., & Girard, J. R. (1990) · Biochemical Journal · doi:10.1042/bj2650511 · Cited by 11
Derangement in Hepatic Enzymes Caused by Sucrose-Drinking and Its Implication for the Development of Hyperglycemia in Female Wistar Fatty Rats.
Sugiyama, Y., SHIMURA, Y., & Ikeda, H. (1989) · Endocrinologia Japonica · doi:10.1507/endocrj1954.36.245 · Cited by 11
Impaired insulin-like growth factor I-mediated stimulation of glucose incorporation into glycogen in vivo in the ob/ob mouse
Cascieri, M. A., Slater, E. E., Vicario, P. P., Green, B. G., BAYNE, M. L., & Saperstein, R. (1989) · Diabetologia · doi:10.1007/bf00277256 · Cited by 11
The 180000 molecular weight plasma membrane insulin receptor substrate is a protein tyrosine phosphatase and is elevated in diabetic plasma membranes
Goren, H. J., & Boland, D. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81087-3 · Cited by 11
Lack of Metabolic Effects of Cholecystokinin on Hepatocytes
Kost, L. J., Gores, G. J., Sayles, J. M., Miller, L. J., Lemasters, J. J., Herman, B., & LaRusso, N. F. (1990) · Hepatology · doi:10.1002/hep.1840120218 · Cited by 10
Insulin receptor binding and kinase activity in liver and skeletal muscles of lactating goats
Balage, M., Sornet, C., & Grizard, J. (1992) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1992.262.5.e561 · Cited by 10
Recent Advances in Noncoding RNAs
Tutar, L. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.98151 · Cited by 9
In vivo and in vitro studies of vanadate in human and rodent diabetes mellitus
Goldfine, A. B., Simonson, D. C., Folli, F. B., Patti, M., & Kahn, C. R. (1995) · Springer eBooks · doi:10.1007/978-1-4613-1251-2_29 · Cited by 9
Insulin receptor gene polymorphisms in Type 2 (non-insulin-dependent) diabetes mellitus
Oelbaum, R. S., Bouloux, P. M., Li, S. R., Baroni, M. G., Stocks, J., & Galton, D. J. (1991) · Diabetologia · doi:10.1007/bf00405085 · Cited by 9
The Genetics and Pathophysiology of Type II and Gestational Diabetes
Csorba, T. R., Edwards, A. L., & Tan, M. H. (1995) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408369509082593 · Cited by 9
Activation of liver and muscle insulin receptor tyrosine kinase activity during in vivo insulin administration in rats
Kruszynska, Y. T., Halban, P. A., Kahn, C. R., & White, M. F. (1990) · Diabetologia · doi:10.1007/bf00401044 · Cited by 9
Dried Bilberry (Vaccinium myrtillus L.) Alleviates the Inflammation and Adverse Metabolic Effects Caused by a High-Fat Diet in a Mouse Model of Obesity
Pemmari, T., Hämäläinen, M., Ryyti, R., Peltola, R., & Moilanen, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911021 · Cited by 8
Isomers of conjugated linoleic acid induce insulin resistance through a mechanism involving activation of protein kinase Cε in liver cells
Roura-Guiberna, A., Hernández-Aranda, J., Ramírez‐Flores, C. J., Mondragón‐Flores, R., Garibay-Nieto, N., Queipo-García, G. E., Laresgoiti‐Servitje, E., Soh, J., & Olivares-Reyes, J. A. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.10.013 · Cited by 8
Insulin-receptor kinase is enhanced in placentas from non-insulin-dependent diabetic women with large-for-gestational-age babies
Takayama-Hasumi, S., Yoshino, H., Shimisu, M., Minei, S., Sanaka, M., & Omori, Y. (1994) · Diabetes Research and Clinical Practice · doi:10.1016/0168-8227(94)90043-4 · Cited by 8
10 Human liver in vitro techniques for metabolic studies
Agius, L. (1987) · Baillière s Clinical Endocrinology and Metabolism · doi:10.1016/s0950-351x(87)80014-9 · Cited by 8
Insulin induces a similar reduction in the concentrations of its own receptor and of an insulin‐sensitive glycosyl‐phosphatidylinositol in isolated rat hepatocytes
Ruiz‐Albusac, J. M., Zueco, J. A., Velázquez, E., Alvarez, J. F., Mato, J. M., & Blázquez, E. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81674-6 · Cited by 8
The insulin receptor endocytosis
Wu, J., Park, S. H., & Choi, E. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.06.020 · Cited by 7
Lipogenic potential of liver from morbidly obese patients with and without non-insulin-dependent diabetes
Barakat, H. A., McLendon, V. D., Carpenter, J. W., Marks, R. H. L., Leggett-Frazier, N., O'Brien, K. F., & Caro, J. F. (1991) · Metabolism · doi:10.1016/0026-0495(91)90110-i · Cited by 7
Self-citation
Multi-layered proteomics identifies insulin-induced upregulation of the EphA2 receptor via the ERK pathway which is dependent on low IGF1R level
Jørgensen, S. H., Emdal, K. B., Pedersen, A.-K., Axelsen, L. N., Kildegaard, H. F., Demozay, D., Pedersen, T. Å., Grønborg, M., Slaaby, R., Nielsen, P. K., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-77817-5 · Cited by 7
Insulin-Sensitive Tyrosine Kinase Activity Changes in Parallel with Plasma Insulin and Glucose Concentrations in Humans*
Nyomba, B. L. G., Swinburn, B. A., Ossowski, V., Boyce, V. L., Bogardus, C., & Mott, D. M. (1991) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-72-6-1212 · Cited by 6
Erythrocyte insulin receptor tyrosine kinase activity is increased in glyburide‐treated patients with type 2 diabetes in good glycaemic control
Santos, R. F., Nomizo, R., de Oliveira, E. M., Ursich, M. J. M., WAJCHENBERG, B. L., Reaven, G. M., & Azhar, S. (2000) · Diabetes Obesity and Metabolism · doi:10.1046/j.1463-1326.2000.00091.x · Cited by 6
Pathogenesis of Type 2 Diabetes
Cusi, K. J., & DeFronzo, R. A. (2001) · Comprehensive physiology · doi:10.1002/cphy.cp070237 · Cited by 5
High Sucrose Low Magnesium Diet Modulates the Expression of PI3K and ERK2 in Different Tissues of Weanling Rats
Garg, M., Kiran, R., & Bansal, D. D. (2011) · American Journal of Biomedical Sciences · doi:10.5099/aj110100011 · Cited by 4
Age-Dependent Onset of Insulin Resistance in Insulin-Resistant Mice
Ide, N., Arisawa, K., Ogura, K., Kagawa, Y., & Maeda, T. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00602 · Cited by 4
Decreased autophosphorylation and kinase activity of insulin receptors in diabetic Chinese hamsters
Oshima, E., Watanabe, K., & Makino, I. (1990) · Diabetes Research and Clinical Practice · doi:10.1016/0168-8227(90)90079-9 · Cited by 4
Insulin binding in non-insulin-dependent diabetes mellitus (NIDDM) is correlated with glycemic control: Clinical evidence for abnormal receptor regulation in NIDDM
Kelly, C. M., & Fantus, I. G. (1995) · Metabolism · doi:10.1016/0026-0495(95)90059-4 · Cited by 4
The Influence of Obesity on the Development of Non-Insulin-Dependent Diabetes Mellitus
Kolaczynski, J. W., & Goldstein, B. J. (2000) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-59651-3_4 · Cited by 4
Analysis of the insulin receptor gene in noninsulin-dependent diabetes mellitus by denaturing gradient gel blots: a clinical research center study
Magré, J., Goldfine, A. B., Warram, J. H., Królewski, A. S., & Kahn, C. R. (1995) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.80.6.1882 · Cited by 4
Relationship between insulin receptor tyrosine kinase activity and internalization in monocytes of non-insulin-dependent diabetes mellitus patients
Trischitta, V., Giorgino, F., Frittitta, L., Scalisi, R., & Vigneri, R. (1993) · Metabolism · doi:10.1016/0026-0495(93)90064-u · Cited by 4
A microphysiological model of human MASLD reveals paradoxical response to resmetirom
Hellen, D. J., Ungerleider, J. L., Tevonian, E. N., Sphabmixay, P., Roy, P., Meimetis, N., Presutti, F., Williams, A. M., Ogi, R., Lewis, C. A., et al. (2026) · Communications Biology · doi:10.1038/s42003-025-09484-9 · Cited by 4
Does glibenclamide influence the clearance of insulin and glucose uptake in patients with type 2 diabetes mellitus?
Widén, E. (1993) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365519309086632 · Cited by 3
Autophosphorylation of Insulin Receptor in a Patient with Werner's Syndrome Associated with Insulin Resistant Diabetes Mellitus.
Shima, F., Ishida, Y., HOTTA, K., Hagino, H., Hozumi, T., Shii, K., Baba, S., & Kazumi, T. (1995) · Endocrine Journal · doi:10.1507/endocrj.42.107 · Cited by 3
Chapter 15 Structure and function of the receptor for insulin
Houslay, M. D., & Wakelam, M. J. O. (1988) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60670-5 · Cited by 2
Purification and characterization of a feline hepatic insulin receptor
Paxton, R., & Ye, L. X. (2000) · American Journal of Veterinary Research · doi:10.2460/ajvr.2000.61.1625 · Cited by 2
Molecular effects of Vitamin-D and PUFAs metabolism in skeletal muscle combating Type-II diabetes mellitus
Logesh, R., Hari, B., Chidambaram, K., & Das, N. (2024) · Gene · doi:10.1016/j.gene.2024.148216 · Cited by 1
Insulin binding to circulating monocytes in children with insulin-dependent and non-insulin-dependent diabetes mellitus
Kida, K., Goto, Y., Watanabe, N., Kaino, Y., Miyagawa, T., Inoue, T., Ikeuchi, M., Matsuda, H., & Kuwajima, K. (1988) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(88)80013-5 · Cited by 1
Insulin: Biochemical and Physiological Aspects
Gruppuso, P. A. (1991) · Springer eBooks · doi:10.1007/978-1-4684-0400-5_5 · Cited by 1
The Role of Covalent and Non-Covalent Mechanisms in Insulin Receptor Action
Rothenberg, P., & Kahn, C. R. (1990) · Springer eBooks · doi:10.1007/978-1-4613-0559-0_4
Protein Phosphorylation and Insulin Action
Perrotti, N., Accili, D., Phillips, S. A., & Taylor, S. I. (1988) · Springer eBooks · doi:10.1007/978-1-4684-9042-8_42
Discovery of small molecule insulin mimetics as potential novel antidiabetic agents
Zhang, B. B. (2002) · Pharmacochemistry library · doi:10.1016/s0165-7208(02)80023-x
Genetic analyses of type 2 diabetes related metabolic risk factors : a twin study
Souren, N. Y. (2009) · Research Publications (Maastricht University) · doi:10.26481/dis.20090123ns
Insulin Action and Insulin Resistance in Noninsulin-Dependent Diabetes Mellitus
Nolan, J. J., & Olefsky, J. M. (1997) · Humana Press eBooks · doi:10.1007/978-1-4757-3906-0_8
BIOACTIVE FATTY ACID SUPPLEMENTATION AND RISK FACTORS FOR THE METABOLIC SYNDROME
Mitchell, P. L. (2010) · Library and Archives Canada (Government of Canada)

Authors: Caro, J. F., Ittoop, O., Pories, W. J., Meelheim, D., Flickinger, E. G., Thomas, F., Jenquin, M., Silverman, J. F., Khazanie, P. G., & Sinha, M. K.
Affiliations: East Carolina University (US)
ORCID: Pories, W J
Silverman, J F
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 1986-07-01
Volume: 78
Issue: 1
Pages: 249-258
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci112558
PMC: PMC329556
OpenAlex: W2062299625
Cited by: 215
References: 74
Citations by year: 2026: 2 · 2024: 4 · 2023: 4 · 2022: 7 · 2021: 2 · 2020: 2 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 1 · 2015: 5 · 2013: 1 · 2012: 2
FWCI: 8.05
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (R01-AM3285-04)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Growth Hormone and Insulin-like Growth Factors
Keywords: insulin resistance, type 2 diabetes, liver, hepatocytes, insulin receptor, insulin receptor kinase, insulin binding, obesity, insulin action, receptor internalization, insulin-stimulated glucose transport
MeSH terms: Biopsy, Cell Separation, Diabetes Mellitus, Electrophoresis, Polyacrylamide Gel, Humans, Insulin, Insulin Resistance, Kinetics, Liver, Obesity, Protein Kinases, Receptor, Insulin, Structure-Activity Relationship

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Studies on the mechanism of insulin resistance in the liver from humans with noninsulin-dependent diabetes. Insulin action and binding in isolated hepatocytes, insulin receptor structure, and kinase activity.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks