GHRH receptor-targeted botulinum neurotoxin selectively inhibits pulsatile GH secretion in male rats

Endocrinology

Volumn 154, Issue 9, 2013, Pages 3305-3318

  Leggett, James ^a   Harper, Elaine ^b   Waite, Eleanor ^a   Marks, Philip ^b   Martinez, Alberto ^b   Lightman, Stafford ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

^b SYNTAXIN LTD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN; BOTULINUM TOXIN D; CELLUBREVIN; GROWTH HORMONE RELEASING FACTOR; GROWTH HORMONE RELEASING FACTOR RECEPTOR; N ETHYLMALEIMIDE SENSITIVE FACTOR; OCTREOTIDE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEINASE; RECEPTOR PROTEIN; SYNAPTOBREVIN; UNCLASSIFIED DRUG;

ACTH SECRETING CELL; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CELL CULTURE; CONTROLLED STUDY; DOSE RESPONSE; DRUG MECHANISM; GONADOTROPIN SECRETING CELL; GROWTH HORMONE RELEASE; GROWTH HORMONE SECRETING CELL; HYPOPHYSIS CELL; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEPLETION; PROTEIN DOMAIN; RAT; TSH SECRETING CELL; WEIGHT GAIN;

ANIMALS; BIOLOGICAL TRANSPORT; BOTULINUM TOXINS; CELLS, CULTURED; DOSE-RESPONSE RELATIONSHIP, DRUG; DOWN-REGULATION; GROWTH HORMONE; GROWTH HORMONE-RELEASING HORMONE; MALE; ORGAN SPECIFICITY; PEPTIDE FRAGMENTS; PERIODICITY; PITUITARY GLAND, ANTERIOR; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEOLYSIS; RATS; RATS, SPRAGUE-DAWLEY; RECEPTORS, NEUROPEPTIDE; RECEPTORS, PITUITARY HORMONE-REGULATING HORMONE; RECOMBINANT FUSION PROTEINS; SOMATOTROPHS; VESICLE-ASSOCIATED MEMBRANE PROTEIN 3;

EID: 84883142608     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2012-2175     Document Type: Article

References (49)

1. Miller M. Syndromes of excess antidiuretic hormone release. Crit Care Clin. 2003;17:11-23.
2. Cooper DS. Hyperthyroidism. Lancet. 2003;362:459-468.
3. Silverberg SJ, Bilezikian JP. Clinical presentation of primary hyperparathyroidism in the United States. In: Bilezikian JP, Marcus R Levine MA, eds. The Parathyroids. 2nd Edition Basic and Clinical Concepts. Waltham, Massachusetts: Elsevier; 2001:349-360.
4. Miyachi Y. Pathophysiology and diagnosis of Cushing's syndrome. Biomed Pharmacother. 2000;54:113-117.
5. Melmed S. Acromegaly pathogenesis and treatment. J Clin Invest. 2009;119:3189-3202.
6. Foster KA, Hambleton P, Shone CC. Introduction and historical perspectives. In: Foster KA, Hambleton P, Shone C, eds. Treatments from Toxins: The Therapeutic Potential of Clostridial Neurotoxins. Boca Raton, FL: CRC Press; 2006:1-17.
7. Dolly JO, Lawrence GW, Meng J, Wang J, Ovsepian SV. Neuroexocytosis: botulinum toxins as inhibitory probes and versatile therapeutics. Curr Opin Pharmacol. 2009;9:326-335.
8. Davletov B, Bajohrs M, Binz T. Beyond BOTOX: advantages and limitations of individual botulinum neurotoxins. Trends Neurosci. 2005;28:446-452.
9. Chaddock J, Purkiss JR, Alexander FCG, et al.Retargeted clostridial endopeptidases: inhibition of nociceptive neurotransmitter release in vitro, and antinociceptive activity in in vivo models of pain. Move Disord. 2004;19(suppl 8):S42-S47.
10. Foster KA, Chaddock JA. Development of therapeutics based upon clostridial endopeptidase activity. In: Foster KA, Hambleton P, Shone C, eds. Treatments from Toxins: The Therapeutic Potential of Clostridial Neurotoxins. Boca Raton, FL: CRC Press; 2006;195-212.
11. Foster KA, Adams EJ, Durose L, et al. Re-engineering the target specificity of clostridial neurotoxins - a route to novel therapeutics. Neurotox Res. 2006;9:101-107.
12. Jahn R, Scheller RH. SNAREs - engines for membrane fusion. Nat Rev Mol Cell Biol. 2006;7:631-643.
13. Montal M. Botulinum neurotoxin: a marvel of protein design. Annu Rev Biochem. 2010;79:591-617.
14. Foster K, Chaddock J. Targeted secretion inhibitors - innovative protein therapeutics. Toxins. 2010;2:2795-2815.
15. Fedele M, Battista S, Kenyon. L, et al. Overexpression of the HMGA2 gene in transgenic mice leads to the onset of pituitary adenomas. Oncogene. 2002;21:3190-3198.
16. Fedele M, De Martino I, Pivonello R, et al. SOM230, a new somatostatin analogue, is highly effective in the therapy of growth hormone/prolactin- secreting pituitary adenomas. Clin Cancer Res. 2007;13:2738-2744.
17. Somm E, Bonnet N, Martinez A, Marks PM, et al. A botulinum toxin-derived targeted secretion inhibitor downregulates the GH/IGF1 axis. J Clin Invest. 2012;122:3295-3306.
18. Chapman IM, Helfgott A, Willoughby JO. Disappearance half-life times of exogenous and growth hormone-releasing factor-stimulated endogenous growth hormone in normal rats. J Endocrinol. 1991;128:369-374.
19. Clark RG, Chambers G, Lewin J, Robinson IC. Automated repetitive microsampling of blood: growth hormone profiles in conscious male rats. J Endocrinol. 1986;111:27-35.
20. Windle RJ, Wood S, Shanks N, et al. Endocrine and behavioural responses to noise stress: comparison of virgin and lactating female rats during non-disrupted maternal activity. J Neuroendocrinol. 1997;9:407-414.
21. Atkinson HC, Leggett JD, Wood SA, Castrique ES, Kershaw YM, Lightman SL. Regulation of the hypothalamic-pituitary-adrenal axis circadian rhythm by endocannabinoids is sexually diergic. Endocrinology. 2010;151:3720-3727.
22. Lebeda FJ, Cer RZ, Stephens RM, Mudunuri U. Temporal characteristics of botulinum neurotoxin therapy. Expert Rev Neurother. 2010;10:93-103.
23. Johnson ML, Virostko A, Veldhuis JD, Evans WS. Deconvolution analysis as a hormone pulse-detection algorithm. Methods Enzymol. 2004;384:40-54.
24. Evans WS, Farhy LS, Johnson ML. Biomathematical modeling of pulsatile hormone secretion: a historical perspective. Methods Enzymol. 2009;454:345-366.
25. Johnson ML, Pipes L, Veldhuis PP, et al. AutoDecon: a robust numerical method for the quantification of pulsatile events. Methods Enzymol. 2009;454:367-404.
26. Varga J, Schally AV, Csernus VJ, et al. Synthesis and biological evaluation of antagonists of growth hormone-releasing hormone with high and protracted in vivo activities. Proc Natl Acad Sci USA. 1999;96:692-697.
27. Clark RG, Carlsson LM, Rafferty B, Robinson IC. The rebound release of growth hormone (GH) following somatostatin infusion in rats involves hypothalamic GH-releasing factor release. J Endocrinol. 1988;119:397-404.
28. Rigamonti AE, Bonomo SM, Cella SG, Muller EE. GH and cortisol rebound rise during and following a somatostatin infusion: studies in dogs with the use of a GH-releasing peptide. J Endocrinol. 2002; 174:387-394.
29. Boisvert C, Pare C, Veyrat-Durebex C, et al. Localisation and regulation of a functional GHRH receptor in rat renal medulla. Endocrinology. 2002;143:1475-1484.
30. Gallego R, Pintos E, Garcia-Caballero T, et al. Cellular distribution of growth hormone-releasing hormone receptor in human reproductive system and breast and prostate cancers. Histol Histopathol. 2005;20:697-706.
31. Hattori N, Ikekubo K, Ishihara T, Moridera K, Hino M, Kurahachi H. Spontaneous growth hormone (GH) secretion by unstimulated human lymphocytes and the effects of GH releasing hormone and somatostatin. Clin Endocrinol Metab. 1994;79:1678-1680.
32. Guarcello V, Weigent DA, Blalock JE. Growth hormone releasing hormone receptors on thymocytes and splenocytes from rats. Cell Immunol. 1991;136:291-302.
33. Granata R, Trovato L, Gallo MP, et al. Growth hormone-releasing hormone promotes survival of cardiac mycocytes in vitro and protects against ischaemia-reperfusion injury in rat heart. Cardiovasc Res. 2009;83:303-312.
34. Kanashiro-Takeuchi RM, Tziomalos K, Takeuchi LM, et al. Cardioprotective effects of growth hormone-releasing hormone agonist after myocardial infarction. Proc Natl Acad Sci USA. 2010;10: 2604-2609.
35. Motomura T, Hashimoto K, Koga M, et al. Inhibition of signal transduction by a splice variant of the growth hormone-releasing hormone receptor expressed in human pituitary adenomas. Metabolism. 1998;47:804-808.
36. McElvaine AT,MayoKE.Adominant-negative human growth hormone-releasing hormone (GHRH) receptor splice variant inhibits GHRH binding. Endocrinology. 2006;147:1884-1894.
37. Kiaris H, Schally AV, Busto R, Halmos G, Artavanis-Tsakonas S, Varga JL. Expression of a splice variant of the receptor for GHRH in 3T3 fibroblasts activates cell proliferation responses to GHRH analogs. Proc Natl Acad Sci USA. 2002;99:196-200.
38. Peters CG, Miller DF, Giovannucci DR. Identification, localisation and interaction of SNARE proteins in atrial cardiac myocytes. J Mol Cell Cardiol. 2006;40:361-374.
39. Chao CC, Mihic A, Tsushima RG, Gaisano HY. SNARE protein regulation of cardiac potassium channels and atrial natriuretic factor secretion. J Mol Cell Cardiol. 2011;50:401-407.
40. Jahn R, Sudhof TC. Membrane fusion and exocytosis. Annu Rev Biochem. 1999;68:863-911.
41. Ferraro F, Eipper BA, Mains RE. Retrieval and reuse of pituitary secretory granule proteins. J Biol Chem. 2005;280:25424-25435.
42. Ji J, Yang SN, Huang X, et al. Modulation of L-type Ca(2+) channels by distinct domains within SNAP-25. Diabetes. 2002;51:1425-1436.
43. Condliffe SB, Zhang H, Frizzell RA. Syntaxin 1A regulates ENac channel activity. J Biol Chem. 2004;279:10085-10092.
44. Brij B. Singh BB, Lockwich BC, et al. VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to agonist-stimulated Ca2+influx. Mol Cell. 2004;15:635-646.
45. Nielsen S, Marples D, Birn H, Mohtashami M, Dalby NO, Trimble M, Knepper M. Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles. Colocalization with Aquaporin-2 water channels. J Clin Invest. 1995;96:1834-1844.
46. Tang BL, Gee HY, Lee MG. The cystic fibrosis transmembrane conductance regulator's expanding SNARE interactome. Traffic. 2011;12:364-371.
47. Naren AP, Di A, Cormet-Boyaka E, et al. Syntaxin 1A is expressed in airway epithelial cells, where it modulates CFTR Cl(-) currents. J Clin Invest. 2000;105:377-386.
48. Wang L, Kotachala V, Walia B, Balasubramanian S, Hall RA, Merlin D, Sitaraman SV. Agonist-induced polarised trafficking and surface expression of the adenosine 2b receptor in intestinal epithelial cells: role of SNARE proteins. Am J Physiol Gastrointest Live Physiol. 2004;267:G1100-G1107.
49. Skalski M, Coppolino MG. SNARE-mediated trafficking of α5β1 integrin is required for spreading in CHO cells. Biochem Biophys Res Commun. 2005;335:1199-1210.