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Amylin fasting plasma levels are decreased in patients with osteoporosis

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Abstract

Amylin is a polypeptide hormone produced in pancreatic beta-cells that belongs to the family of calcitonin gene-related peptides. There is a 20% sequence homology between amylin and calcitonin and 44% homology with calcitonin gene-related peptide. Amylin and its fragments stimulate the proliferation of osteoblasts, inhibit bone resorption, and increase bone density and the amount of bone mass. We measured amylin total and unreduced amylin fasting plasma levels in patients with osteoporosis (n=28; 3 men, 25 women; mean age 65 years), type 2 diabetes mellitus (n=10; 5 men, 5 women; 64 years), and in the control group (n=24; 11 men, 13 women; 53 years) using an ELISA kit with immunofluorescent detection (Linco). Amylin total plasma levels in patients with osteoporosis were 3.33±0.46 pmol/l (mean±SEM), in patients with type 2 diabetes 6.29±1.47 pmol/l (mean±SEM), and in the control group 8.48±3.12 pmol/l (mean±SEM). Mean plasma levels were lower in patients with osteoporosis than in patients with type 2 diabetes and in the control group. Unreduced amylin plasma levels in patients with osteoporosis (n=28) were 2.51±0.87 pmol/l (mean±SEM), in patients with type 2 diabetes (n=10) 4.15±0.95 pmol/l (mean±SEM) and in the control group (n=5) 13.50±3.94 pmol/l (mean±SEM). Plasma levels were significantly lower in patients with osteoporosis than in patients with type 2 diabetes (P<0.01) and in the control group (P<0.001). Amylin plasma levels are decreased in patients with osteoporosis. Amylin deficiency in these patients may contribute to the development of osteoporosis. Amylin should be investigated in relation to the pharmacological treatment of osteoporosis.

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References

  1. Cooper GJ, Willis AC, Clark A et al. (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA 84:8628–8632

    CAS  PubMed  Google Scholar 

  2. Young A (1997) Amylin’s physiology and its role in diabetes. Curr Opin Endocrinol Diab 4:282–290

    CAS  Google Scholar 

  3. Percy AJ, Trainor DA, Rittenhouse J et al. (1996) Development of sensitive immunoassays to detect amylin and amylin-like peptides in unextracted plasma. Clin Chem 42:4:576–585

    Google Scholar 

  4. Wimalawansa SJ (1997) Amylin, calcitonin gene-related peptide, calcitonin, and adrenomedullin: a peptide superfamily. Crit Rev Neurobiol 11:167–239

    CAS  PubMed  Google Scholar 

  5. Gedulin BR, Rink TJ, Young AA (1997) Dose-response for glucagonostatic effect of amylin in rats. Metabolism 46:67–70

    CAS  PubMed  Google Scholar 

  6. Guidobono F (1998) Amylin and gastrointestinal activity. Gen Pharm 31:173–177

    Article  CAS  Google Scholar 

  7. Wookey PJ, Cao Z, van Geenen RCI et al. (1997) Increased density of renal amylin binding sites in experimental hypertension. Hypertension 30:455–460

    CAS  PubMed  Google Scholar 

  8. Chin SY, Hall JM, Brain SD, Morton IK (1994) Vasodilator responses to calcitonin gene-related peptide (CGRP) and amylin in the rat isolated perfused kidney are mediated via CGRP1 receptors. J Pharmacol Exp Ther 269:989–992

    CAS  PubMed  Google Scholar 

  9. Higham CE, Hull RL, Lawrie L et al. (2000) Processing of synthetic pro-islet amyloid polypeptide (proIAPP) “amylin” by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro. Eur J Biochem 267:4998–5004

    Article  CAS  PubMed  Google Scholar 

  10. Dechenes CJ, Verchere CB, Andrikopoulos S, Kahn SE (1998) Human aging is associated with parallel reductions in insulin and amylin release. Am J Physiol Endocrinol Metab 275:E785–E791

    CAS  Google Scholar 

  11. Cornish J, Callon KE, Lin CQX et al. (1998) Dissociation of the effects of amylin on osteoblast proliferation and bone resorption. Am J Physiol Endocrinol Metab 274:E827–E833

    CAS  Google Scholar 

  12. Cornish J, Callon KE, King AR et al. (1998) Systemic administration of amylin increases bone mass, linear growth, and adiposity in adult male mice. Am J Physiol Endocrinol Metab 275:E694–E699

    CAS  Google Scholar 

  13. Cornish J, Callon KE, Gasser JA et al. (2000) Systemic administration of a novel octapeptide, amylin-(1–8), increases bone volume in male mice. Am J Physiol Endocrinol Metab 279:E730–E735

    CAS  PubMed  Google Scholar 

  14. Cornish J, Callon KE, Coy DH et al. (1997) Adrenomedullin is a potent stimulator of osteoblastic activity in vitro and in vivo. Am J Physiol Endocrinol Metab 273:E1113–E1120

    CAS  Google Scholar 

  15. Cornish J, Callon KE, Reid IR (1996) Insulin increases histomorphometric indices of bone formation in vivo. Calcif Tissue Int 59:492–495

    Article  CAS  PubMed  Google Scholar 

  16. Livshitz G, Pantsulaia I, Trofimov S, Kobyliansky E (2003) Genetic variation of circulating leptin is involved in genetic variation of hand bone size and geometry. Osteoporos Int 14:476–483

    PubMed  Google Scholar 

  17. Samsom M, Szarka LA, Camilleri M et al. (2000) Pramlintide, an amylin analog, selectively delays gastric emptying: potential role of vagal inhibition. Am J Physiol Gastrointest Liver Physiol 278:G946–G951

    CAS  PubMed  Google Scholar 

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Acknowledgements

This work was supported by research grants IGA MZ NK/6447-3, GAUK 46/2003C and by DANONE Institute.

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Correspondence to J. Bronský.

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Bronský, J., Průša, R. Amylin fasting plasma levels are decreased in patients with osteoporosis. Osteoporos Int 15, 243–247 (2004). https://doi.org/10.1007/s00198-003-1538-5

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