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Article ; Online: Peptide receptors as cancer drug targets.

Moody, Terry W

Annals of the New York Academy of Sciences

2019 Volume 1455, Issue 1, Page(s) 141–148

Abstract: Neuropeptides function as neuromodulators in the brain, whereby they are released in a paracrine manner and activate G protein-coupled receptors (GPCRs) in adjacent cells. Because neuropeptides are made in, and secreted from, cancer cells, then bind to ... ...

Abstract	Neuropeptides function as neuromodulators in the brain, whereby they are released in a paracrine manner and activate G protein-coupled receptors (GPCRs) in adjacent cells. Because neuropeptides are made in, and secreted from, cancer cells, then bind to cell surface receptors, they function in an autocrine manner. Bombesin (BB)-like peptides synthesized by neuroendocrine tumor small cell lung cancer (SCLC) bind to BB receptors (BBRs), causing phosphatidylinositol turnover and phosphorylation of extracellular signal-regulated kinase (ERK). Phosphorylated ERK enters the nucleus and alters gene expression of SCLC cells, stimulating growth. Vasoactive intestinal peptide (VIP) addition to SCLC cells increases their release rate of BB-like peptides via activation of VIP receptors (VIPR), leading to activation of adenylyl cyclase and subsequent elevation of cAMP. Protein kinase A is then stimulated, leading to phosphorylation of cyclic AMP response element binding protein (CREB), which alters gene expression and stimulates proliferation. The growth of SCLC is inhibited by BBR and VIPR antagonists. This review will focus on how GPCRs for VIP and BB are molecular targets for early detection and treatment of cancer.
MeSH term(s)	Animals ; Humans ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Phosphorylation ; Receptors, Peptide/metabolism
Chemical Substances	Receptors, Peptide
Language	English
Publishing date	2019-05-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	211003-9
ISSN	1749-6632 ; 0077-8923
ISSN (online)	1749-6632
ISSN	0077-8923
DOI	10.1111/nyas.14100
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Peptide G-Protein-Coupled Receptors and ErbB Receptor Tyrosine Kinases in Cancer.

Moody, Terry W / Ramos-Alvarez, Irene / Jensen, Robert T

Biology

2023 Volume 12, Issue 7

Abstract: The ErbB RTKs (EGFR, HER2, HER3, and HER4) have been well-studied in cancer. EGFR, HER2, and HER3 stimulate cancer proliferation, principally by activating the phosphatidylinositol-3-kinase and extracellular signal-regulated kinase (ERK) pathways, ... ...

Abstract	The ErbB RTKs (EGFR, HER2, HER3, and HER4) have been well-studied in cancer. EGFR, HER2, and HER3 stimulate cancer proliferation, principally by activating the phosphatidylinositol-3-kinase and extracellular signal-regulated kinase (ERK) pathways, resulting in increased cancer cell survival and proliferation. Cancer cells have high densities of the EGFR, HER2, and HER3 causing phosphorylation of tyrosine amino acids on protein substrates and tyrosine amino acids near the C-terminal of the RTKs. After transforming growth factor (TGF) α binds to the EGFR, homodimers or EGFR heterodimers form. HER2 forms heterodimers with the EGFR, HER3, and HER4. The EGFR, HER2, and HER3 are overexpressed in lung cancer patient tumors, and monoclonal antibodies (mAbs), such as Herceptin against HER2, are used to treat breast cancer patients. Patients with EGFR mutations are treated with tyrosine kinase inhibitors, such as gefitinib or osimertinib. Peptide GPCRs, such as NTSR1, are present in many cancers, and neurotensin (NTS) stimulates the growth of cancer cells. Lung cancer proliferation is impaired by SR48692, an NTSR1 antagonist. SR48692 is synergistic with gefitinib at inhibiting lung cancer growth. Adding NTS to lung cancer cells increases the shedding of TGFα, which activates the EGFR, or neuregulin-1, which activates HER3. The transactivation process is impaired by SRC, matrix metalloprotease, and reactive oxygen species inhibitors. While the transactivation process is complicated, it is fast and occurs within minutes after adding NTS to cancer cells. This review emphasizes the use of tyrosine kinase inhibitors and SR48692 to impair transactivation and cancer growth.
Language	English
Publishing date	2023-07-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology12070957
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Article ; Online: Pituitary adenylate cyclase-activating polypeptide/vasoactive intestinal peptide (Part 2): biology and clinical importance in central nervous system and inflammatory disorders.

Moody, Terry W / Jensen, Robert T

Current opinion in endocrinology, diabetes, and obesity

2021 Volume 28, Issue 2, Page(s) 206–213

Abstract: Purpose of review: To discuss recent advances of vasoactive intestinal peptide/pituitary adenylate cyclase-activating polypeptide (VIP/PACAP) receptors in the selected central nervous system (CNS) and inflammatory disorders.: Recent findings: Recent ... ...

Abstract	Purpose of review: To discuss recent advances of vasoactive intestinal peptide/pituitary adenylate cyclase-activating polypeptide (VIP/PACAP) receptors in the selected central nervous system (CNS) and inflammatory disorders. Recent findings: Recent studies provide evidence that PACAP plays an important role in a number of CNS disorders, particularly the pathogenesis of headaches (migraine, etc.) as well as posttraumatic stress disorder and drug/alcohol/smoking addiction. VIP has important therapeutic effects in a number of autoimmune/inflammatory disorder such as rheumatoid arthritis. In some cases, these insights have advanced to therapeutic trials. Summary: Recent insights from studies of VIP/PACAP and their receptors in both CNS disorders (migraine, posttraumatic stress disorder, addiction [drugs, alcohol, smoking]) and inflammatory disorders [such as rheumatoid arthritis] are suggesting new treatment approaches. The elucidation of the importance of VIP/PACAP system in these disorders combined recent development of specific drugs acting on this system (i.e., monoclonal VIP/PACAP antibodies) will likely lead to importance novel treatment approaches in these diseases.
MeSH term(s)	Biology ; Central Nervous System ; Humans ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I ; Receptors, Vasoactive Intestinal Peptide, Type II ; Receptors, Vasoactive Intestinal Polypeptide, Type I ; Vasoactive Intestinal Peptide
Chemical Substances	Pituitary Adenylate Cyclase-Activating Polypeptide ; Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I ; Receptors, Vasoactive Intestinal Peptide, Type II ; Receptors, Vasoactive Intestinal Polypeptide, Type I ; Vasoactive Intestinal Peptide (37221-79-7)
Language	English
Publishing date	2021-01-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2272017-0
ISSN	1752-2978 ; 1752-296X
ISSN (online)	1752-2978
ISSN	1752-296X
DOI	10.1097/MED.0000000000000621
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Article ; Online: Pituitary adenylate cyclase-activating polypeptide/vasoactive intestinal peptide [Part 1]: biology, pharmacology, and new insights into their cellular basis of action/signaling which are providing new therapeutic targets.

Moody, Terry W / Jensen, Robert T

Current opinion in endocrinology, diabetes, and obesity

2021 Volume 28, Issue 2, Page(s) 198–205

Abstract: Purpose of review: To discuss recent advances of vasoactive intestinal peptide (VIP)/pituitary adenylate cyclase-activating polypeptide (PACAP) receptors in pharmacology, cell biology, and intracellular signaling in cancer.: Recent findings: Recent ... ...

Abstract	Purpose of review: To discuss recent advances of vasoactive intestinal peptide (VIP)/pituitary adenylate cyclase-activating polypeptide (PACAP) receptors in pharmacology, cell biology, and intracellular signaling in cancer. Recent findings: Recent studies provide new insights into the pharmacology, cell biology of the VIP/PACAP system and show they play important roles in a number of human cancers, as well as in tumor growth/differentiation and are providing an increased understanding of their signaling cascade that is suggesting new treatment targets/approaches. Summary: Recent insights from studies of VIP/PACAP and their receptors in both central nervous system disorders and inflammatory disorders suggest possible new treatment approaches. Elucidation of the exact roles of VIP/PACAP in these disorders and development of new therapeutic approaches involving these peptides have been limited by lack of specific pharmacological tools, and exact signaling mechanisms involved, mediating their effects. Reviewed here are recent insights from the elucidation of structural basis for VIP/PACAP receptor activation as well as the signaling cascades mediating their cellular effects (using results primarily from the study of their effects in cancer) that will likely lead to novel targets and treatment approaches in these diseases.
MeSH term(s)	Biology ; Humans ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I ; Receptors, Vasoactive Intestinal Peptide ; Receptors, Vasoactive Intestinal Polypeptide, Type I ; Vasoactive Intestinal Peptide
Chemical Substances	Pituitary Adenylate Cyclase-Activating Polypeptide ; Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I ; Receptors, Vasoactive Intestinal Peptide ; Receptors, Vasoactive Intestinal Polypeptide, Type I ; Vasoactive Intestinal Peptide (37221-79-7)
Language	English
Publishing date	2021-01-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2272017-0
ISSN	1752-2978 ; 1752-296X
ISSN (online)	1752-2978
ISSN	1752-296X
DOI	10.1097/MED.0000000000000617
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Article ; Online: Adding of neurotensin to non-small cell lung cancer cells increases tyrosine phosphorylation of HER3.

Moody, Terry W / Ramos-Alvarez, Irene / Jensen, Robert T

Peptides

2022 Volume 156, Page(s) 170858

Abstract: Neurotensin (NTS) receptor 1 regulates the growth non-small cell lung cancer (NSCLC) cells. NTS binds with high affinity to NTSR1, leading to increased tyrosine phosphorylation of the EGFR and HER2. Using Calu3, NCI-H358, or NCI-H441 cells, the effects ... ...

Abstract	Neurotensin (NTS) receptor 1 regulates the growth non-small cell lung cancer (NSCLC) cells. NTS binds with high affinity to NTSR1, leading to increased tyrosine phosphorylation of the EGFR and HER2. Using Calu3, NCI-H358, or NCI-H441 cells, the effects of NTS on HER3 transactivation were investigated. HER3 tyrosine phosphorylation was increased by NTS or neuregulin (NRG1) addition to NSCLC cells. NCI-H358, NCI-H441, and Calu-3 cells have HER3, NTSR1 and neuregulin (NRG)1 protein. NTSR1 regulation of HER3 transactivation was impaired by SR48692 (NTSR1 antagonist) or monoclonal antibody (mAb)3481 (HER3 blocker). Immunoprecipitation experiments indicated that NTS addition to NCI-H441cells resulted in the formation of EGFR/HER3 and HER2/HER3 heterodimers. The ability of NTS to increase HER3 tyrosine phosphorylation was impaired by GM6001 (MMP inhibitor), PP2 (Src inhibitor), Tiron (superoxide scavenger), or N-acetylcysteine (antioxidant). Adding NTS to NSCLC cells increased phosphorylation of ERK, HER3, and AKT. NTS or NRG1 increased colony formation of NSCLC cells which was strongly inhibited by SR48692 and mAb3481. The results indicate that NTSR1 regulates HER3 transactivation in NSCLC cells leading to increased proliferation.
MeSH term(s)	1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt/pharmacology ; Acetylcysteine/metabolism ; Acetylcysteine/pharmacology ; Antibodies, Monoclonal/pharmacology ; Antioxidants/pharmacology ; Carcinoma, Non-Small-Cell Lung/genetics ; Cell Line, Tumor ; Cell Proliferation ; ErbB Receptors/genetics ; ErbB Receptors/metabolism ; Humans ; Lung Neoplasms/genetics ; Lung Neoplasms/metabolism ; Matrix Metalloproteinase Inhibitors/pharmacology ; Neuregulins/metabolism ; Neurotensin/metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-akt/metabolism ; Receptor, ErbB-3 ; Receptors, Neurotensin/genetics ; Receptors, Neurotensin/metabolism ; Superoxides ; Tyrosine
Chemical Substances	Antibodies, Monoclonal ; Antioxidants ; Matrix Metalloproteinase Inhibitors ; Neuregulins ; Receptors, Neurotensin ; neurotensin type 1 receptor ; Superoxides (11062-77-4) ; Neurotensin (39379-15-2) ; Tyrosine (42HK56048U) ; 1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium Salt (4X87R5T106) ; ERBB3 protein, human (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1) ; Receptor, ErbB-3 (EC 2.7.10.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Acetylcysteine (WYQ7N0BPYC)
Language	English
Publishing date	2022-08-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	769028-9
ISSN	1873-5169 ; 0196-9781
ISSN (online)	1873-5169
ISSN	0196-9781
DOI	10.1016/j.peptides.2022.170858
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Book ; Conference proceedings: Growth factors, peptides and receptors

Moody, Terry W.

proceedings of the Twelfth Washington International Spring Symposium at The George Washington University held in June 1 - 5, 1992, in Washington, D.C

(GWUMC Department of Biochemistry Annual Spring Symposia)

1993

Institution	Washington Spring Symposium on Health Sciences
Author's details	ed. by Terry W. Moody
Series title	GWUMC Department of Biochemistry Annual Spring Symposia
Keywords	Growth Substances / congresses ; Hormones / congresses ; Peptides / congresses ; Receptors, Cell Surface / congresses ; Second Messenger Systems / congresses ; Neuropeptide ; Rezeptor ; Wachstumsfaktor ; Peptide
Subject	Neuromodulator
Language	English
Size	X, 467 S. : Ill., graph. Darst.
Publisher	Plenum Press
Publishing place	New York u.a.
Publishing country	United States
Document type	Book ; Conference proceedings
HBZ-ID	HT005041342
ISBN	0-306-44484-4 ; 978-0-306-44484-5
Database	Catalogue ZB MED Medicine, Health

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1993 A 3775	order for loan	Magazin

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Article ; Online: Peptide G-Protein-Coupled Receptors and ErbB Receptor Tyrosine Kinases in Cancer

Moody, Terry W. / Ramos-Alvarez, Irene / Jensen, R. T.

Biology (Basel). 2023 July 04, v. 12, no. 7

2023

Abstract	The ErbB RTKs (EGFR, HER2, HER3, and HER4) have been well-studied in cancer. EGFR, HER2, and HER3 stimulate cancer proliferation, principally by activating the phosphatidylinositol-3-kinase and extracellular signal-regulated kinase (ERK) pathways, resulting in increased cancer cell survival and proliferation. Cancer cells have high densities of the EGFR, HER2, and HER3 causing phosphorylation of tyrosine amino acids on protein substrates and tyrosine amino acids near the C-terminal of the RTKs. After transforming growth factor (TGF) α binds to the EGFR, homodimers or EGFR heterodimers form. HER2 forms heterodimers with the EGFR, HER3, and HER4. The EGFR, HER2, and HER3 are overexpressed in lung cancer patient tumors, and monoclonal antibodies (mAbs), such as Herceptin against HER2, are used to treat breast cancer patients. Patients with EGFR mutations are treated with tyrosine kinase inhibitors, such as gefitinib or osimertinib. Peptide GPCRs, such as NTSR1, are present in many cancers, and neurotensin (NTS) stimulates the growth of cancer cells. Lung cancer proliferation is impaired by SR48692, an NTSR1 antagonist. SR48692 is synergistic with gefitinib at inhibiting lung cancer growth. Adding NTS to lung cancer cells increases the shedding of TGFα, which activates the EGFR, or neuregulin-1, which activates HER3. The transactivation process is impaired by SRC, matrix metalloprotease, and reactive oxygen species inhibitors. While the transactivation process is complicated, it is fast and occurs within minutes after adding NTS to cancer cells. This review emphasizes the use of tyrosine kinase inhibitors and SR48692 to impair transactivation and cancer growth.
Keywords	antagonists ; breast neoplasms ; cell viability ; lung neoplasms ; metalloproteinases ; mitogen-activated protein kinase ; neoplasm cells ; neurotensin ; patients ; phosphatidylinositol 3-kinase ; phosphorylation ; reactive oxygen species ; receptor protein-tyrosine kinase ; transcriptional activation ; tyrosine
Language	English
Dates of publication	2023-0704
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article ; Online
ZDB-ID	2661517-4
ISSN	2079-7737
ISSN	2079-7737
DOI	10.3390/biology12070957
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Chronic Exposure to Nitric Oxide Induces P53 Mutations and Malignant-like Features in Human Breast Epithelial Cells.

Cheng, Robert Y S / Burkett, Sandra / Ambs, Stefan / Moody, Terry / Wink, David A / Ridnour, Lisa A

Biomolecules

2023 Volume 13, Issue 2

Abstract: The small endogenous signaling molecule nitric oxide (NO) has been linked with chronic inflammation and cancer. The effects of NO are both concentration and temporally dependent; under some conditions, NO protects against damage caused by reactive oxygen ...

Abstract	The small endogenous signaling molecule nitric oxide (NO) has been linked with chronic inflammation and cancer. The effects of NO are both concentration and temporally dependent; under some conditions, NO protects against damage caused by reactive oxygen species and activates P53 signaling. During chronic inflammation, NO causes DNA damage and inhibits repair proteins. To extend our understanding of the roles of NO during carcinogenesis, we investigated the possible effects of chronic NO exposure on MCF10A breast epithelial cells, as defined by changes in cellular morphology, chromosome/genomic stability, RNA, and protein expression, and altered cell phenotypes. Human MCF10A cells were maintained in varying doses of the NO donor DETANO for three weeks. Distinct patterns of genomic modifications in TP53 and KRAS target genes were detected in NO-treated cells when compared to background mutations. In addition, quantitative real-time PCR demonstrated an increase in the expression of cancer stem cell (CSC) marker CD44 after prolonged exposure to 300 μM DETANO. While similar changes in cell morphology were found in cells exposed to 300-500 μM DETANO, cells cultured in 100 μM DETANO exhibited enhanced motility. In addition, 100 μM NO-treated cells proliferated in serum-free media and selected clonal populations and pooled cells formed colonies in soft agar that were clustered and disorganized. These findings show that chronic exposure to NO generates altered breast epithelial cell phenotypes with malignant characteristics.
MeSH term(s)	Humans ; Female ; Nitric Oxide/metabolism ; Tumor Suppressor Protein p53/metabolism ; Epithelial Cells/metabolism ; Mutation ; Inflammation/metabolism ; Breast Neoplasms/metabolism
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; Tumor Suppressor Protein p53
Language	English
Publishing date	2023-02-07
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13020311
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Adding of neurotensin to non-small cell lung cancer cells increases tyrosine phosphorylation of HER3

Moody, Terry W. / Ramos-Alvarez, Irene / Jensen, Robert T.

Peptides. 2022 Oct., v. 156

2022

Abstract	Neurotensin (NTS) receptor 1 regulates the growth non-small cell lung cancer (NSCLC) cells. NTS binds with high affinity to NTSR1, leading to increased tyrosine phosphorylation of the EGFR and HER2. Using Calu3, NCI-H358, or NCI-H441 cells, the effects of NTS on HER3 transactivation were investigated. HER3 tyrosine phosphorylation was increased by NTS or neuregulin (NRG1) addition to NSCLC cells. NCI-H358, NCI-H441, and Calu-3 cells have HER3, NTSR1 and neuregulin (NRG)1 protein. NTSR1 regulation of HER3 transactivation was impaired by SR48692 (NTSR1 antagonist) or monoclonal antibody (mAb)3481 (HER3 blocker). Immunoprecipitation experiments indicated that NTS addition to NCI-H441cells resulted in the formation of EGFR/HER3 and HER2/HER3 heterodimers. The ability of NTS to increase HER3 tyrosine phosphorylation was impaired by GM6001 (MMP inhibitor), PP2 (Src inhibitor), Tiron (superoxide scavenger), or N-acetylcysteine (antioxidant). Adding NTS to NSCLC cells increased phosphorylation of ERK, HER3, and AKT. NTS or NRG1 increased colony formation of NSCLC cells which was strongly inhibited by SR48692 and mAb3481. The results indicate that NTSR1 regulates HER3 transactivation in NSCLC cells leading to increased proliferation.
Keywords	acetylcysteine ; antagonists ; antioxidants ; lung neoplasms ; monoclonal antibodies ; neurotensin ; neurotrophins ; phosphorylation ; precipitin tests ; transcriptional activation ; tyrosine
Language	English
Dates of publication	2022-10
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	769028-9
ISSN	1873-5169 ; 0196-9781
ISSN (online)	1873-5169
ISSN	0196-9781
DOI	10.1016/j.peptides.2022.170858
Database	NAL-Catalogue (AGRICOLA)

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Book ; Conference proceedings: Neural and endocrine peptides and receptors

Moody, Terry W.

(GWUMC Department of Biochemistry annual spring symposia)

1986

Event/congress	Washington Spring Symposium on Health Sciences (5, 1985)
Author's details	Fifth Annual Washington Spring Symposium on Health Sciences. Ed. by Terry W. Moody
Series title	GWUMC Department of Biochemistry annual spring symposia
Keywords	Neuropeptides / congresses ; Receptors, Cell Surface / congresses ; Neuropeptide ; Neurotransmitter-Rezeptor ; Neuropeptid ; Peptidhormon ; Hormonrezeptor ; Rezeptor
Subject	Neuromodulator ; Proteohormon ; Peptidhormone ; Polypeptidhormone ; Neurorezeptor
Language	English
Size	XI, 722 S. : Ill., graph. Darst.
Publisher	Plenum Pr
Publishing place	New York u.a.
Publishing country	United States
Document type	Book ; Conference proceedings
HBZ-ID	HT003022455
ISBN	0-306-42300-6 ; 978-0-306-42300-0
Database	Catalogue ZB MED Medicine, Health

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1987 A 3213	order for loan	Magazin

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