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Clinical Chemistry, Vol 42, 576-585, Copyright © 1996 by American Association for Clinical Chemistry
AJ Percy, DA Trainor, J Rittenhouse, J Phelps and JE Koda
Amylin Pharmaceuticals, Inc., San Diego, CA 92121, USA.
Amylin is a 37-amino-acid polypeptide synthesized in and secreted from pancreatic beta cells along with insulin. Its biological actions include the slowing and reduction of postmeal increases in plasma glucose concentrations. Studies of the basic amylin biology in humans have been hampered by the lack of a rapid, sensitive assay capable of measuring physiological concentrations of amylin in small volumes of plasma. We report here two sandwich-type immunoassays that use pairs of monoclonal antibodies, the fluorescent substrate 4-methylumbelliferyl phosphate, and the enzyme alkaline phosphatase. The minimum detectable concentration of amylin in 50 microL of plasma was 0.5 to 2 pmol/L, and the dynamic range was 2 to 100 pmol/L. The assays had average intraassay CVs of <10%, average interassay CVs of <15%, and good linearity on dilution and recovery of added amylin. The two assays use the same detection antibody, which binds to the carboxyl terminus of the molecule, but different capture antibodies. One of the assays measures only human amylin; the other also detects amylin-like peptides. Examples of measurements in human plasma are provided in subjects with impaired glucose tolerance and in nondiabetic controls.
The following articles in journals at HighWire Press have cited this article:
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  V R Kairamkonda, A Deorukhkar, C Bruce, R Coombs, R Fraser, and A-P T Mayer Amylin peptide is increased in preterm neonates with feed intolerance Arch. Dis. Child. Fetal Neonatal Ed., July 1, 2008; 93(4): F265 - F270. [Abstract] [Full Text] [PDF]
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 C. Mack, J. Wilson, J. Athanacio, J. Reynolds, K. Laugero, S. Guss, C. Vu, J. Roth, and D. Parkes Pharmacological actions of the peptide hormone amylin in the long-term regulation of food intake, food preference, and body weight Am J Physiol Regulatory Integrative Comp Physiol, November 1, 2007; 293(5): R1855 - R1863. [Abstract] [Full Text] [PDF]
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 V Kairamkonda, A Deorukhkar, R Coombs, R Fraser, and T Mayer Amylin peptide levels are raised in infants of diabetic mothers Arch. Dis. Child., December 1, 2005; 90(12): 1279 - 1282. [Abstract] [Full Text] [PDF]
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 R. L. Hull, M. R. Watts, K. Kodama, Z.-p. Shen, K. M. Utzschneider, D. B. Carr, J. Vidal, and S. E. Kahn Genetic background determines the extent of islet amyloid formation in human islet amyloid polypeptide transgenic mice Am J Physiol Endocrinol Metab, October 1, 2005; 289(4): E703 - E709. [Abstract] [Full Text] [PDF]
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 R. A. Heptulla, L. M. Rodriguez, L. Bomgaars, and M. W. Haymond The Role of Amylin and Glucagon in the Dampening of Glycemic Excursions in Children With Type 1 Diabetes Diabetes, April 1, 2005; 54(4): 1100 - 1107. [Abstract] [Full Text] [PDF]
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 L. Marzban, G. Soukhatcheva, and C. B. Verchere Role of Carboxypeptidase E in Processing of Pro-Islet Amyloid Polypeptide in {beta}-Cells Endocrinology, April 1, 2005; 146(4): 1808 - 1817. [Abstract] [Full Text] [PDF]
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S. Andrikopoulos, R. L. Hull, C. B. Verchere, F. Wang, S. M. Wilbur, T. N. Wight, L. Marzban, and S. E. Kahn Extended life span is associated with insulin resistance in a transgenic mouse model of insulinoma secreting human islet amyloid polypeptide Am J Physiol Endocrinol Metab, March 1, 2004; 286(3): E418 - E424. [Abstract] [Full Text]
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R. L. Hull, S. Andrikopoulos, C. B. Verchere, J. Vidal, F. Wang, M. Cnop, R. L. Prigeon, and S. E. Kahn Increased Dietary Fat Promotes Islet Amyloid Formation and {beta}-Cell Secretory Dysfunction in a Transgenic Mouse Model of Islet Amyloid Diabetes, February 1, 2003; 52(2): 372 - 379. [Abstract] [Full Text] [PDF]
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 N. G. Knowles, M. A. Landchild, W. Y. Fujimoto, and S. E. Kahn Insulin and Amylin Release Are Both Diminished in First-Degree Relatives of Subjects With Type 2 Diabetes Diabetes Care, February 1, 2002; 25(2): 292 - 297. [Abstract] [Full Text] [PDF]
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 K. Tateishi, E. P. DiMagno, and G. G. Klee Plasma Islet Amyloid Polypeptide Is Not an Effective Tumor Marker for Pancreatic Cancer Even When Protease Inhibitors and Rapid Freezing of Specimens Are Utilized Clin. Chem., November 1, 2001; 47(11): 2071 - 2073. [Full Text] [PDF]
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R. A. Silvestre, J. Rodriguez-Gallardo, C. Jodka, D. G. Parkes, R. A. Pittner, A. A. Young, and J. Marco Selective amylin inhibition of the glucagon response to arginine is extrinsic to the pancreas Am J Physiol Endocrinol Metab, March 1, 2001; 280(3): E443 - E449. [Abstract] [Full Text] [PDF]
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 S. Mäkimattila, M. S. Fineman, and H. Yki-Järvinen Deficiency of Total and Nonglycosylated Amylin in Plasma Characterizes Subjects with Impaired Glucose Tolerance and Type 2 Diabetes J. Clin. Endocrinol. Metab., August 1, 2000; 85(8): 2822 - 2827. [Abstract] [Full Text]
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C. B. Juhl, N. Porksen, J. Sturis, A. P. Hansen, J. D. Veldhuis, S. Pincus, M. Fineman, and O. Schmitz High-frequency oscillations in circulating amylin concentrations in healthy humans Am J Physiol Endocrinol Metab, March 1, 2000; 278(3): E484 - E490. [Abstract] [Full Text] [PDF]
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C. J. Dechenes, C. B. Verchere, S. Andrikopoulos, and S. E. Kahn Human aging is associated with parallel reductions in insulin and amylin release Am J Physiol Endocrinol Metab, November 1, 1998; 275(5): E785 - E791. [Abstract] [Full Text] [PDF]
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M. Clodi, K. Thomaseth, G. Pacini, K. Hermann, A. Kautzky-Willer, W. Waldhausl, R. Prager, and B. Ludvik Distribution and kinetics of amylin in humans Am J Physiol Endocrinol Metab, May 1, 1998; 274(5): E903 - E908. [Abstract] [Full Text] [PDF]
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