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Identification of ChIP-seq mapped targets of HP1β due to bombesin/GRP receptor activation.

Clinical epigenetics

Tell R, Wang QT, Blunier A, Benya RV.
PMID: 22704345
Clin Epigenetics. 2011 Aug;2(2):331-8. doi: 10.1007/s13148-011-0027-5. Epub 2011 Mar 29.

Epithelial cells lining the adult colon do not normally express gastrin-releasing peptide (GRP) or its receptor (GRPR). In contrast, GRP/GRPR can be aberrantly expressed in human colorectal cancer (CRC) including Caco-2 cells. We have previously shown that GRPR activation...

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Tell R, Wang QT, Blunier A, et al. Identification of ChIP-seq mapped targets of HP1β due to bombesin/GRP receptor activation. Clin Epigenetics. 2011;2(2):331-8doi: 10.1007/s13148-011-0027-5.
Tell, R., Wang, Q. T., Blunier, A., & Benya, R. V. (2011). Identification of ChIP-seq mapped targets of HP1β due to bombesin/GRP receptor activation. Clinical epigenetics, 2(2), 331-8. https://doi.org/10.1007/s13148-011-0027-5
Tell, Robert, et al. "Identification of ChIP-seq mapped targets of HP1β due to bombesin/GRP receptor activation." Clinical epigenetics vol. 2,2 (2011): 331-8. doi: https://doi.org/10.1007/s13148-011-0027-5
Tell R, Wang QT, Blunier A, Benya RV. Identification of ChIP-seq mapped targets of HP1β due to bombesin/GRP receptor activation. Clin Epigenetics. 2011 Aug;2(2):331-8. doi: 10.1007/s13148-011-0027-5. Epub 2011 Mar 29. PMID: 22704345; PMCID: PMC3365384.
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Sulfakinins reduce food intake in the desert locust, Schistocerca gregaria.

Journal of insect physiology

Wei Z, Baggerman G, J Nachman R, Goldsworthy G, Verhaert P, De Loof A, Schoofs L.
PMID: 10844144
J Insect Physiol. 2000 Sep 01;46(9):1259-1265. doi: 10.1016/s0022-1910(00)00046-9.

In vertebrates, the peptides cholecystokinin (CCK), neuropeptide Y, galanin, and bombesin are known to be involved in the control of food intake. We report here that insect sulfakinins, peptides which display substantial sequence similarities with the vertebrate gastrin/CCK peptide...

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Wei Z, Baggerman G, J Nachman R, et al. Sulfakinins reduce food intake in the desert locust, Schistocerca gregaria. J Insect Physiol. 2000;46(9):1259-1265doi: 10.1016/s0022-1910(00)00046-9.
Wei, Z., Baggerman, G., J Nachman R, Goldsworthy, G., Verhaert, P., De Loof A, & Schoofs, L. (2000). Sulfakinins reduce food intake in the desert locust, Schistocerca gregaria. Journal of insect physiology, 46(9), 1259-1265. https://doi.org/10.1016/s0022-1910(00)00046-9
Wei, et al. "Sulfakinins reduce food intake in the desert locust, Schistocerca gregaria." Journal of insect physiology vol. 46,9 (2000): 1259-1265. doi: https://doi.org/10.1016/s0022-1910(00)00046-9
Wei Z, Baggerman G, J Nachman R, Goldsworthy G, Verhaert P, De Loof A, Schoofs L. Sulfakinins reduce food intake in the desert locust, Schistocerca gregaria. J Insect Physiol. 2000 Sep 01;46(9):1259-1265. doi: 10.1016/s0022-1910(00)00046-9. PMID: 10844144.
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Localization of putative biochemical messengers during Eisenia foetida (Annelida, Oligochaeta) development.

Tissue & cell

Falugi C, Davoli C.
PMID: 18621234
Tissue Cell. 1993 Jun;25(3):311-23. doi: 10.1016/0040-8166(93)90073-t.

This histochemical-immunohistochemical study was performed on the earthworm Eisenia foetida at different developmental stages, to investigate the presence and distribution of cholinergic molecules (AChE, BuChE, alpha-bungarotoxin-binding sites), several biogenic amines (5HT and catecholamines), and some immunologically-related peptides (somatostatin. FMRF-amide,...

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Falugi C, Davoli C. Localization of putative biochemical messengers during Eisenia foetida (Annelida, Oligochaeta) development. Tissue Cell. 1993;25(3):311-23doi: 10.1016/0040-8166(93)90073-t.
Falugi, C., & Davoli, C. (1993). Localization of putative biochemical messengers during Eisenia foetida (Annelida, Oligochaeta) development. Tissue & cell, 25(3), 311-23. https://doi.org/10.1016/0040-8166(93)90073-t
Falugi, C, and Davoli, C. "Localization of putative biochemical messengers during Eisenia foetida (Annelida, Oligochaeta) development." Tissue & cell vol. 25,3 (1993): 311-23. doi: https://doi.org/10.1016/0040-8166(93)90073-t
Falugi C, Davoli C. Localization of putative biochemical messengers during Eisenia foetida (Annelida, Oligochaeta) development. Tissue Cell. 1993 Jun;25(3):311-23. doi: 10.1016/0040-8166(93)90073-t. PMID: 18621234.
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Neuromedin: An insight into its types, receptors and therapeutic opportunities.

Pharmacological reports : PR

Gajjar S, Patel BM.
PMID: 31994106
Pharmacol Rep. 2017 May;69(3):438-447. doi: 10.1016/j.pharep.2017.01.009. Epub 2017 Jan 22.

Neuropeptides are small protein used by neurons in signal communications. Neuromedin U was the first neuropeptide discovered from the porcine spinal and showed its potent constricting activities on uterus hence was entitled with neuromedin U. Following neuromedin U another...

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Gajjar S, Patel BM. Neuromedin: An insight into its types, receptors and therapeutic opportunities. Pharmacol Rep. 2017;69(3):438-447doi: 10.1016/j.pharep.2017.01.009.
Gajjar, S., & Patel, B. M. (2017). Neuromedin: An insight into its types, receptors and therapeutic opportunities. Pharmacological reports : PR, 69(3), 438-447. https://doi.org/10.1016/j.pharep.2017.01.009
Gajjar, Saumitra, and Patel, Bhoomika M. "Neuromedin: An insight into its types, receptors and therapeutic opportunities." Pharmacological reports : PR vol. 69,3 (2017): 438-447. doi: https://doi.org/10.1016/j.pharep.2017.01.009
Gajjar S, Patel BM. Neuromedin: An insight into its types, receptors and therapeutic opportunities. Pharmacol Rep. 2017 May;69(3):438-447. doi: 10.1016/j.pharep.2017.01.009. Epub 2017 Jan 22. PMID: 31994106.
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Autoradiographic localization of neuromedin B binding sites in rat brain.

Molecular and cellular neurosciences

Lee MC, Jensen RT, Coy DH, Moody TW.
PMID: 19912767
Mol Cell Neurosci. 1990 Oct;1(2):161-7. doi: 10.1016/1044-7431(90)90021-u.

The binding properties and autoradiographic distribution of radiolabeled neuromedin B (NMB) to rat brain sections were investigated. (125)I-NMB bound with high affinity (K(d) = 1 nM) to a single class of sites (B(max) = 80 fmol/mg protein) in coronal...

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Lee MC, Jensen RT, Coy DH, et al. Autoradiographic localization of neuromedin B binding sites in rat brain. Mol Cell Neurosci. 1990;1(2):161-7doi: 10.1016/1044-7431(90)90021-u.
Lee, M. C., Jensen, R. T., Coy, D. H., & Moody, T. W. (1990). Autoradiographic localization of neuromedin B binding sites in rat brain. Molecular and cellular neurosciences, 1(2), 161-7. https://doi.org/10.1016/1044-7431(90)90021-u
Lee, M C, et al. "Autoradiographic localization of neuromedin B binding sites in rat brain." Molecular and cellular neurosciences vol. 1,2 (1990): 161-7. doi: https://doi.org/10.1016/1044-7431(90)90021-u
Lee MC, Jensen RT, Coy DH, Moody TW. Autoradiographic localization of neuromedin B binding sites in rat brain. Mol Cell Neurosci. 1990 Oct;1(2):161-7. doi: 10.1016/1044-7431(90)90021-u. PMID: 19912767.
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Targeting the gastrin-releasing peptide receptor pathway to treat cognitive dysfunctionassociated with Alzheimer's Disease.

Dementia & neuropsychologia

Roesler R, Luft T, Schwartsmann G.
PMID: 29213377
Dement Neuropsychol. 2007 Apr-Jun;1(2):118-123. doi: 10.1590/s1980-57642008dn10200002.

Increasing evidence indicates that bombesin (BB)-like peptides (BLPs), such as the gastrin-releasing peptide (GRP) and its receptor (GRPR), might play a role in neurological and psychiatric disorders. The present study reviews findings from animal and human studies suggesting that...

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Roesler R, Luft T, Schwartsmann G. Targeting the gastrin-releasing peptide receptor pathway to treat cognitive dysfunctionassociated with Alzheimer's Disease. Dement Neuropsychol. 2007;1(2):118-123doi: 10.1590/s1980-57642008dn10200002.
Roesler, R., Luft, T., & Schwartsmann, G. (2007). Targeting the gastrin-releasing peptide receptor pathway to treat cognitive dysfunctionassociated with Alzheimer's Disease. Dementia & neuropsychologia, 1(2), 118-123. https://doi.org/10.1590/s1980-57642008dn10200002
Roesler, Rafael, et al. "Targeting the gastrin-releasing peptide receptor pathway to treat cognitive dysfunctionassociated with Alzheimer's Disease." Dementia & neuropsychologia vol. 1,2 (2007): 118-123. doi: https://doi.org/10.1590/s1980-57642008dn10200002
Roesler R, Luft T, Schwartsmann G. Targeting the gastrin-releasing peptide receptor pathway to treat cognitive dysfunctionassociated with Alzheimer's Disease. Dement Neuropsychol. 2007 Apr-Jun;1(2):118-123. doi: 10.1590/s1980-57642008dn10200002. PMID: 29213377; PMCID: PMC5619558.
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Dexamethasone treatment after adrenalectomy increases bombesin content in the rat spinal cord.

Acta physiologica Scandinavica

Westermark T, Isaksson T, Holmberg P, Kjörell U, Rantapää-Dahlqvist S, Forsgren S.
PMID: 10571562
Acta Physiol Scand. 1999 Oct;167(2):A8. doi: 10.1046/j.1365-201x.1999.0600h.x.

No abstract available.

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Westermark T, Isaksson T, Holmberg P, et al. Dexamethasone treatment after adrenalectomy increases bombesin content in the rat spinal cord. Acta Physiol Scand. 1999;167(2):A8doi: 10.1046/j.1365-201x.1999.0600h.x.
Westermark, T., Isaksson, T., Holmberg, P., Kjörell, U., Rantapää-Dahlqvist, S., & Forsgren, S. (1999). Dexamethasone treatment after adrenalectomy increases bombesin content in the rat spinal cord. Acta physiologica Scandinavica, 167(2), A8. https://doi.org/10.1046/j.1365-201x.1999.0600h.x
Westermark, et al. "Dexamethasone treatment after adrenalectomy increases bombesin content in the rat spinal cord." Acta physiologica Scandinavica vol. 167,2 (1999): A8. doi: https://doi.org/10.1046/j.1365-201x.1999.0600h.x
Westermark T, Isaksson T, Holmberg P, Kjörell U, Rantapää-Dahlqvist S, Forsgren S. Dexamethasone treatment after adrenalectomy increases bombesin content in the rat spinal cord. Acta Physiol Scand. 1999 Oct;167(2):A8. doi: 10.1046/j.1365-201x.1999.0600h.x. PMID: 10571562.
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Gut hormones in cyclostomes.

Fish physiology and biochemistry

Van Noorden S.
PMID: 24220989
Fish Physiol Biochem. 1990 Sep;8(5):399-408. doi: 10.1007/BF00003371.

The current state of knowledge about regulatory peptides in endocrine cells and nerves of the alimentary canal of lampreys and hagfishes is reviewed. Cyclostomes have a wide range of peptides similar immunochemically to those of higher vertebrates. They include,...

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Van Noorden S. Gut hormones in cyclostomes. Fish Physiol Biochem. 1990;8(5):399-408doi: 10.1007/BF00003371.
Van Noorden, S. (1990). Gut hormones in cyclostomes. Fish physiology and biochemistry, 8(5), 399-408. https://doi.org/10.1007/BF00003371
Van Noorden, S. "Gut hormones in cyclostomes." Fish physiology and biochemistry vol. 8,5 (1990): 399-408. doi: https://doi.org/10.1007/BF00003371
Van Noorden S. Gut hormones in cyclostomes. Fish Physiol Biochem. 1990 Sep;8(5):399-408. doi: 10.1007/BF00003371. PMID: 24220989.
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Radiolabeled peptides: valuable tools for the detection and treatment of cancer.

Theranostics

Fani M, Maecke HR, Okarvi SM.
PMID: 22737187
Theranostics. 2012;2(5):481-501. doi: 10.7150/thno.4024. Epub 2012 May 16.

Human cancer cells overexpress many peptide receptors as molecular targets. Radiolabeled peptides that bind with high affinity and specificity to the receptors on tumor cells hold great potential for both diagnostic imaging and targeted radionuclide therapy. The advantage of...

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Fani M, Maecke HR, Okarvi SM. Radiolabeled peptides: valuable tools for the detection and treatment of cancer. Theranostics. 2012;2(5):481-501doi: 10.7150/thno.4024.
Fani, M., Maecke, H. R., & Okarvi, S. M. (2012). Radiolabeled peptides: valuable tools for the detection and treatment of cancer. Theranostics, 2(5), 481-501. https://doi.org/10.7150/thno.4024
Fani, M, et al. "Radiolabeled peptides: valuable tools for the detection and treatment of cancer." Theranostics vol. 2,5 (2012): 481-501. doi: https://doi.org/10.7150/thno.4024
Fani M, Maecke HR, Okarvi SM. Radiolabeled peptides: valuable tools for the detection and treatment of cancer. Theranostics. 2012;2(5):481-501. doi: 10.7150/thno.4024. Epub 2012 May 16. PMID: 22737187; PMCID: PMC3364555.
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Interactions of gastrointestinal peptides: ghrelin and its anorexigenic antagonists.

International journal of peptides

Wisser AS, Habbel P, Wiedenmann B, Klapp BF, Mönnikes H, Kobelt P.
PMID: 20798884
Int J Pept. 2010;2010. doi: 10.1155/2010/817457. Epub 2010 Jan 06.

Food intake behaviour and energy homeostasis are strongly regulated by a complex system of humoral factors and nerval structures constituting the brain-gut-axis. To date the only known peripherally produced and centrally acting peptide that stimulates food intake is ghrelin,...

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Wisser AS, Habbel P, Wiedenmann B, et al. Interactions of gastrointestinal peptides: ghrelin and its anorexigenic antagonists. Int J Pept. 2010;2010doi: 10.1155/2010/817457.
Wisser, A. S., Habbel, P., Wiedenmann, B., Klapp, B. F., Mönnikes, H., & Kobelt, P. (2010). Interactions of gastrointestinal peptides: ghrelin and its anorexigenic antagonists. International journal of peptides, 2010. https://doi.org/10.1155/2010/817457
Wisser, Anna-Sophia, et al. "Interactions of gastrointestinal peptides: ghrelin and its anorexigenic antagonists." International journal of peptides vol. 2010 (2010). doi: https://doi.org/10.1155/2010/817457
Wisser AS, Habbel P, Wiedenmann B, Klapp BF, Mönnikes H, Kobelt P. Interactions of gastrointestinal peptides: ghrelin and its anorexigenic antagonists. Int J Pept. 2010;2010. doi: 10.1155/2010/817457. Epub 2010 Jan 06. PMID: 20798884; PMCID: PMC2925274.
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Endocrine cells and nerves in the stomach of the lizard Podarcis hispanica detected by immunocytochemistry.

Tissue & cell

De Rada OD, Burrell MA, García C, Barrenechea MA, Sesma P.
PMID: 18621220
Tissue Cell. 1992;24(5):705-13. doi: 10.1016/0040-8166(92)90041-5.

The general identification of endocrine cells in the stomach of the lizard Podarcis hispanica was carried out by their response to the Grimelius and Masson-Fontana techniques. 11 immunoreactive cell-types, positive for chromogranin-, serotonin-, caerulein/gastrin/ cholecystokinin (CAER/G/CCK)-, glucagon-like-peptide-1 (GLP-1)-. glucagon-,...

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De Rada OD, Burrell MA, García C, et al. Endocrine cells and nerves in the stomach of the lizard Podarcis hispanica detected by immunocytochemistry. Tissue Cell. 1992;24(5):705-13doi: 10.1016/0040-8166(92)90041-5.
De Rada, O. D., Burrell, M. A., García, C., Barrenechea, M. A., & Sesma, P. (1992). Endocrine cells and nerves in the stomach of the lizard Podarcis hispanica detected by immunocytochemistry. Tissue & cell, 24(5), 705-13. https://doi.org/10.1016/0040-8166(92)90041-5
De Rada, O D, et al. "Endocrine cells and nerves in the stomach of the lizard Podarcis hispanica detected by immunocytochemistry." Tissue & cell vol. 24,5 (1992): 705-13. doi: https://doi.org/10.1016/0040-8166(92)90041-5
De Rada OD, Burrell MA, García C, Barrenechea MA, Sesma P. Endocrine cells and nerves in the stomach of the lizard Podarcis hispanica detected by immunocytochemistry. Tissue Cell. 1992;24(5):705-13. doi: 10.1016/0040-8166(92)90041-5. PMID: 18621220.
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AM-37 and ST-36 Are Small Molecule Bombesin Receptor Antagonists.

Frontiers in endocrinology

Moody TW, Tashakkori N, Mantey SA, Moreno P, Ramos-Alvarez I, Leopoldo M, Jensen RT.
PMID: 28785244
Front Endocrinol (Lausanne). 2017 Jul 21;8:176. doi: 10.3389/fendo.2017.00176. eCollection 2017.

While peptide antagonists for the gastrin-releasing peptide receptor (BB

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Moody TW, Tashakkori N, Mantey SA, et al. AM-37 and ST-36 Are Small Molecule Bombesin Receptor Antagonists. Front Endocrinol (Lausanne). 2017;8:176doi: 10.3389/fendo.2017.00176.
Moody, T. W., Tashakkori, N., Mantey, S. A., Moreno, P., Ramos-Alvarez, I., Leopoldo, M., & Jensen, R. T. (2017). AM-37 and ST-36 Are Small Molecule Bombesin Receptor Antagonists. Frontiers in endocrinology, 8176. https://doi.org/10.3389/fendo.2017.00176
Moody, Terry W, et al. "AM-37 and ST-36 Are Small Molecule Bombesin Receptor Antagonists." Frontiers in endocrinology vol. 8 (2017): 176. doi: https://doi.org/10.3389/fendo.2017.00176
Moody TW, Tashakkori N, Mantey SA, Moreno P, Ramos-Alvarez I, Leopoldo M, Jensen RT. AM-37 and ST-36 Are Small Molecule Bombesin Receptor Antagonists. Front Endocrinol (Lausanne). 2017 Jul 21;8:176. doi: 10.3389/fendo.2017.00176. eCollection 2017. PMID: 28785244; PMCID: PMC5519534.
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