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1.

001-es BibID:BIBFORM033900
035-os BibID:PMID:8251954 WOS:A1993MB41500002
Első szerző:Halmos Gábor (gyógyszerész, receptorfarmakológus, experimentális onkológus)
Cím:Use of radioreceptor assay and cell superfusion system for in vitro screening of analogs of growth hormone-releasing hormone / Gabor Halmos, Zoltan Rekasi, Balazs Szoke, Andrew V. Schally
Dátum:1993
Megjegyzések:In the search for more active agonists and antagonists of human growth hormone-releasing hormone (hGH-RH), various analogs are being synthesized. In order to follow the binding affinity of these analogs, we have developed a sensitive in vitro radioreceptor assay for GH-RH based on binding of labeled [His1,Nle27]hGH-RH(1-32)NH2 to rat anterior pituitary membrane homogenates by adapting and modifying earlier methods. Scatchard analysis of saturation binding data demonstrated the presence of a single class of specific binding sites for GH-RH in membranes of rat anterior pituitaries with a Bmax of 33.3 +/- 5.2 fmol/mg protein and an apparent Kd of 0.19 +/- 0.02 nM. In displacement analyses, we compared the binding affinity of [His1,Nle27]hGH-RH(1-32)NH2 with its iodinated derivative. No significant differences were detected in IC50 concentrations ranging from 0.97 to 3.4 nM between labeled and nonlabeled hGH-RH analogs. These findings demonstrate the validity of the radioreceptor assay. To evaluate the biological activities of hGH-RH derivatives, we applied a sensitive, dispersed rat pituitary cell superfusion system. This dynamic in vitro system eliminates the drawbacks of the static pituitary cell culture. No differences were observed in biological activities of the iodinated and noniodinated hGH-RH analogs. GH-releasing activity obtained from the superfusion assay correlated well with GH-RH receptor binding affinity for all nonlabeled and labeled hGH-RH analogs examined. These two methods are fast, simple, and relatively inexpensive, and provide quantitative data on receptor affinities, biological activities, and hence structure-affinity and structure-activity relationships. Joint use of these two in vitro systems appears to be suitable for screening newly synthesized GH-RH analogs.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Receptor. - 3 : 2 (1993), p. 87-97. -
További szerzők:Rékási Zoltán Szőke Balázs Schally, Andrew Victor
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2.

001-es BibID:BIBFORM033620
035-os BibID:WOS:000089341400049
Első szerző:Halmos Gábor (gyógyszerész, receptorfarmakológus, experimentális onkológus)
Cím:Human renal cell carcinoma expresses distinct binding sites for growth hormone-releasing hormone / Gabor Halmos, Andrew V. Schally, Jozsef L. Varga, Artur Plonowski, Zoltan Rekasi, Tamas Czompoly
Dátum:2000
Megjegyzések:Antagonists of growth hormone-releasing hormone (GHRH) inhibit the proliferation of various human cancers in vitro and in vivo by mechanisms that include apparent direct effects through specific binding sites expressed on tumors and that differ from pituitary human GHRH (hGHRH) receptors. In this study, GHRH antagonist JV-1-38 (20 mu g/day per animal s.c,) inhibited the growth of orthotopic CAKI-1 human renal cell carcinoma (RCC) by 83% and inhibited the development of metastases to lung and lymph nodes. Using ligand competition assays with I-125-labeled GHRH antagonist JV-1-42. we demonstrated the presence of specific high-affinity (K-d = 0.25 +/- 0.03 nM) binding sites for GHRH with a maximal binding capacity (B-max) Of 70.2 +/- 4.1 fmol/mg of membrane protein in CAKI-1 tumors. These receptors bind GHRH antagonists preferentially and display a lower affinity for hGHRH. The binding of I-125-JV-1-42 is not inhibited by vasoactive intestinal peptide (VIP)-related peptides sharing structural homology with hGHRH. The receptors for GHRH antagonists on CAKI-1 tumors are distinct from binding sites detected with I-125-VIP (K-d = 0.89 +/- 0.14 nM; B-max = 183.5 +/- 2.6 fmol/mg of protein) and also have different characteristics from GHRH receptors on rat pituitary as documented by the insignificant binding of [His(1),I-125-Tyr(10),Nle(27)]hGHRH(1-32)NH2. Reverse transcription-PCR revealed the expression of splice variants of hGHRH receptor in CAKI-1 RCC. Biodistribution studies demonstrate an in vivo uptake of I-125-JV-1-42 by the RCC tumor tissue. The presence of specific receptor proteins that bind GHRH antagonists in CAKI-1 RCC supports the view that distinct binding sites that mediate the inhibitory effect of GHRH antagonists are present on various human cancers.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Proceedings of The National Academy of Sciences of The United States Of America. - 97 : 19 (2000), p. 10555-10560. -
További szerzők:Schally, Andrew Victor Varga József L. Plonowski, Artur Rékási Zoltán Czompoly Tamás
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3.

001-es BibID:BIBFORM033602
035-os BibID:PMID:12364462 WOS:000178649800050
Első szerző:Halmos Gábor (gyógyszerész, receptorfarmakológus, experimentális onkológus)
Cím:Expression of growth hormone-releasing hormone and its receptor splice variants in human prostate cancer / Gabor Halmos, Andrew V. Schally, Tamas Czompoly, Magdalena Krupa, Jozsef L. Varga, Zoltan Rekasi
Dátum:2002
ISSN:0021-972X
Megjegyzések:Antagonists of GHRH inhibit the growth of various human tumors, including prostate cancer, but the tumoral receptors mediating the antiproliferative effect of GHRH antagonists have not been clearly identified. Recently, we demonstrated that human cancer cell lines express splice variants (SVs) of receptors for GHRH, of which SV1 exhibits the greatest similarity to the pituitary GHRH receptors. In this study we investigated the expression of GHRH and SVs of GHRH receptor and the binding characteristics of the GHRH receptor isoform in 20 surgical specimens of organ-confined and locally advanced human prostatic adenocarcinomas. The mRNA expression of GHRH and SVs of GHRH receptor was investigated by RT-PCR. The affinity and density of receptors for GHRH were determined by ligand competition assays based on binding of (125)I-labeled GHRH antagonist JV-1-42 to tumor membranes. Twelve of 20 tumors (60%) exhibited specific, high affinity binding for JV-1-42, with a mean dissociation constant (K(d)) of 0.81 nmol/liter and a mean maximal binding capacity of 185.2 fmol/mg membrane protein. The mRNA of SV1 was detected in 13 of 20 (65%) prostate cancer specimens and was consistent with the presence of GHRH binding. RT-PCR analyses also revealed the expression of mRNA for GHRH in 13 of 15 (86%) prostatic carcinoma specimens examined. The presence of GHRH and its tumoral receptor SVs in prostate cancers suggests the possible existence of an autocrine mitogenic loop. The antitumor effects of GHRH antagonists in prostate cancer could be exerted in part by interference with this local GHRH system.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Journal of Clinical Endocrinology & Metabolism. - 87 : 10 (2002), p. 4707-4714. -
További szerzők:Schally, Andrew Victor Czompoly Tamás Krupa, Magdalena Varga József L. Rékási Zoltán
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4.

001-es BibID:BIBFORM033743
035-os BibID:WOS:A1992JW79800047
Első szerző:Janáky Tamás
Cím:Short-chain analogs of luteinizing hormone-releasing hormone containing cytotoxic moieties / T. Janáky, A. Juhász, Z. Rékasi, P. Serfözö, J. Pinski, L. Bokser, G. Srkalovic, S. Milovanovic, T. W. Redding, G. Halmos, A. Nagy, A. V. Schally
Dátum:1992
ISSN:0027-8424
Megjegyzések:Five hexapeptide and heptapeptide analogs of luteinizing hormone-releasing hormone (LH-RH) were synthesized for use as carriers for cytotoxic compounds. These short analogs were expected to enhance target selectivity of the antineoplastic agents linked to them. Native LH-RH-(3-9) and LH-RH-(4-9) containing D-lysine and D-ornithine at position 6 were amidated with ethylamine and acylated on the N terminus. The receptor-binding affinity of one hexapeptide carrier AJ-41 (Ac-Ser-Tyr-D-Lys-Leu-Arg-Pro-NH-Et) to human breast cancer cell membranes was similar to that of [D-Trp6]LH-RH. Alkylating nitrogen mustards (melphalan, Ac-melphalan), anthraquinone derivatives including anticancer antibiotic doxorubicin, antimetabolite (methotrexate), and cisplatin-like platinum complex were linked to these peptides through their omega-amino group at position 6. The hybrid molecules showed no LH-RH agonistic activity in vitro and in vivo but had nontypical antagonistic effects on pituitary cells in vitro at the doses tested. These analogs showed a wide range of receptor-binding affinities to rat pituitaries and cell membranes of human breast cancer and rat Dunning prostate cancer. Several of these conjugates exerted some cytotoxic effects on MCF-7 breast cancer cell line.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Proceedings of The National Academy of Sciences of The United States of America. - 89 : 21 (1992), p. 10203-10207. -
További szerzők:Juhász A. Rékási Zoltán Serfőző P. Pinski, Jacek Bokser, L. Srkalovic, G. Milovanovic, Slobodan Redding, T. W. Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Nagy Attila Schally, Andrew Victor
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5.

001-es BibID:BIBFORM033643
Első szerző:Kahán Zsuzsa
Cím:Antagonists of growth hormone-releasing hormone arrest the growth of MDA-MB-468 estrogen-independent human breast cancers in nude mice / Zsuzsanna Kahán, József L. Varga, Andrew V. Schally, Zoltán Rékási, Patricia Armatis, Ioulia Chatzistamou, Tamás Czömpöly, Gábor Halmos
Dátum:2000
ISSN:0167-6806
Megjegyzések:Since antagonists of growth hormone-releasing hormone (GH-RH) inhibit proliferation of various tumors, in this study we investigated the effects of GH-RH antagonists MZ-5-156 or JV-1-36 on growth of estrogen-independent MDA-MB-468 human breast cancers xenografted into nude mice. Both GH-RH antagonists administered at a dose of 20 microg/day induced regression of some and growth-arrest of other tumors, while control tumors continued to grow. After 5 weeks of therapy with MZ-5-156 or JV-1-36, final volume and weight of MDA-MB-468 tumors were significantly decreased (all p values < 0.001) and serum IGF-I levels as well as tumor IGF-I mRNA expression were reduced as compared with controls. High affinity binding sites for IGF-I were detected by the ligand binding method. Gene expression of human IGF-I receptors, as measured by the RT-PCR, was not significantly different in control and treated MDA-MB-468 tumors. In cell culture, IGF-I did not stimulate, GH-RH slightly stimulated, while MZ-5-156 and JV-1-36 inhibited proliferation of MDA-MB-468 cells known to possess defective insulin and IGF-I receptor signaling. The expression of mRNA for human GH-RH was found in five of 8 tumors treated with GH-RH antagonists, and in one of the five control tumors. These results suggest that GH-RH antagonists inhibit MDA-MB-468 breast cancers possibly through mechanisms involving interference with locally produced GH-RH.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Breast Cancer Research and Treatment. - 60 : 1 (2000), p. 71-79. -
További szerzők:Varga József L. Schally, Andrew Victor Rékási Zoltán Armatis, Patricia Chatzistamou, Ioulia Czömpöly Tamás Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus)
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6.

001-es BibID:BIBFORM033639
Első szerző:Plonowski, Artur
Cím:Potentiation of the inhibitory effect of growth hormone-releasing hormone antagonists on PC-3 human prostate cancer by bombesin antagonists indicative of interference with both IGF and EGF pathways / Artur Plonowski, Andrew V. Schally, Jozsef L. Varga, Zoltan Rekasi, Francine Hebert, Gabor Halmos, Kate Groot
Dátum:2000
ISSN:0270-4137
Megjegyzések:BACKGROUND: In view of the involvement of various neuropeptides and growth factors in the progression of androgen-independent prostate cancer, we investigated the effects of antagonists of growth hormone-releasing hormone (GHRH) alone or in combination with an antagonist of bombesin/gastrin-releasing peptide (BN/GRP) on PC-3 human prostate cancers. METHODS: Nude mice implanted with PC-3 tumors received GHRH antagonists MZ-5-156 or JV-1-38, each at 20 microgram/day s.c. In experiment 2, treatment consisted of daily injections of JV-1-38 (20 microgram), BN/GRP antagonist RC-3940-II (10 microgram), or a combination of JV-1-38 and RC-3940-II. Serum IGF-I levels, expression of mRNA for IGF-II, and characteristics of BN/GRP and EGF receptors in tumor tissue were investigated. RESULTS: JV-1-38 induced a greater inhibition of tumor growth and suppression of IGF-II mRNA than MZ-5-156, both compounds causing a similar decrease in serum IGF-I. In experiment 2, JV-1-38 and RC-3940-II produced a comparable reduction in tumor volume (65% and 61%, respectively), but a combination of both antagonists augmented tumor inhibition to 75%. Combined treatment with JV-1-38 and RC-3940-II also led to a greater suppression of IGF-II mRNA (92%), as compared with JV-1-38 (72%) or RC-3940-II (77%). Serum IGF-I concentration was lowered only in mice treated with JV-1-38, while the downregulation of BN/GRP and EGF receptors was specific for groups receiving RC-3940-II. CONCLUSIONS: The inhibitory effects of GHRH antagonists on PC-3 human androgen-independent prostate cancer can be potentiated by concomitant use of BN/GRP antagonists. The combination of both types of analogs apparently interferes with both IGF and bombesin/EGF pathways, and might be clinically useful for the management of androgen-independent prostate cancer.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Prostate. - 44 : 2 (2000), p. 172-180. -
További szerzők:Schally, Andrew Victor Varga József L. Rékási Zoltán Hebert, Francine Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Groot, Kate
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7.

001-es BibID:BIBFORM033638
Első szerző:Rékási Zoltán
Cím:Antagonistic actions of analogs related to growth hormone-releasing hormone (GHRH) on receptors for GHRH and vasoactive intestinal peptide on rat pituitary and pineal cells in vitro / Zoltan Rekasi, Jozsef L. Varga, Andrew V. Schally, Gabor Halmos, Kate Groot, Tamas Czompoly
Dátum:2000
ISSN:0027-8424
Megjegyzések:Peptide analogs of growth hormone-releasing hormone (GHRH) can potentially interact with vasoactive intestinal peptide (VIP) receptors (VPAC(1)-R and VPAC(2)-R) because of the structural similarities of these two hormones and their receptors. We synthesized four new analogs related to GHRH (JV-1-50, JV-1-51, JV-1-52, and JV-1-53) with decreased GHRH antagonistic activity and increased VIP antagonistic potency. To characterize various peptide analogs for their antagonistic activity on receptors for GHRH and VIP, we developed assay systems based on superfusion of rat pituitary and pineal cells. Receptor-binding affinities of peptides to the membranes of these cells were also evaluated by radioligand competition assays. Previously reported GHRH antagonists JV-1-36, JV-1-38, and JV-1-42 proved to be selective for GHRH receptors, because they did not influence VIP-stimulated VPAC(2) receptor-dependent prolactin release from pituitary cells or VPAC(1) receptor-dependent cAMP efflux from pinealocytes but strongly inhibited GHRH-stimulated growth hormone (GH) release. Analogs JV-1-50, JV-1-51, and JV-1-52 showed various degrees of VPAC(1)-R and VPAC(2)-R antagonistic potency, although also preserving a substantial GHRH antagonistic effect. Analog JV-1-53 proved to be a highly potent VPAC(1) and VPAC(2) receptor antagonist, devoid of inhibitory effects on GHRH-evoked GH release. The antagonistic activity of these peptide analogs on processes mediated by receptors for GHRH and VIP was consistent with the binding affinity. The analogs with antagonistic effects on different types of receptors expressed on tumor cells could be utilized for the development of new approaches to treatment of various human cancers.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Proceedings of The National Academy of Sciences of The United States of America. - 97 : 3 (2000), p. 1218-1223. -
További szerzők:Varga József L. Schally, Andrew Victor Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Groot, Kate Czompoly Tamás
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8.

001-es BibID:BIBFORM033636
035-os BibID:PMID:10830299 WOS:000088386100031
Első szerző:Rékási Zoltán
Cím:Antagonists of growth hormone-releasing hormone and vasoactive intestinal peptide inhibit tumor proliferation by different mechanisms : evidence from in vitro studies on human prostatic and pancreatic cancers / Zoltan Rekasi, Jozsef L. Varga, Andrew V. Schally, Gabor Halmos, Patricia Armatis, Kate Groot, Tamas Czompoly
Dátum:2000
ISSN:0013-7227
Megjegyzések:Antagonists of GH-releasing hormone (GHRH) and vasoactive intestinal peptide (VIP) inhibit the proliferation of various tumors in vitro and in vivo, but a comparison of their antitumor effects and mechanisms of action has not been reported to date. We recently synthesized and characterized a series of analogs, some of which are primarily GHRH antagonists (JV-1-36, JV-1-38, and JV-1-42), whereas others are more selective for VIP receptors (VPAC-R; JV-1-50, JV-1-51, JV-1-52, and JV-1-53). LNCaP human prostatic cancer cells express VPAC-R, with predominant subtype 1 determined by RT-PCR. Our studies show that GHRH antagonists significantly inhibit the proliferation of both VPAC-R positive LNCaP cells (P < 0.001) and VPAC-R negative MiaPaCa-2 human pancreatic cancer cells cultured in vitro (P < 0.05 to P < 0.001). Growth inhibition of LNCaP cells is accompanied by a proportional reduction in prostate-specific antigen (PSA) secretion (P < 0.001). In a superfusion system, the inhibitory activities of the analogs on the rate of VIP and GHRH-induced PSA secretion correlate well with their VPAC-R binding affinities to LNCaP cell membranes. Antagonists more selective for VPAC-R display a stronger inhibition of inducible PSA release than GHRH antagonists, but have smaller effects or no effects on proliferation and PSA secretion in culture. Collectively, our findings demonstrate that the antiproliferative activity of the analogs on cancer cells is not correlated to their VPAC-R antagonistic potencies. Because GHRH antagonists inhibit the proliferation of LNCaP cells more powerfully than VPAC-R antagonists and also suppress the growth ofVPAC-R-negative MiaPaCa-2 cells, it can be concluded that their antiproliferative effect is exerted through a mechanism independent of VPAC-R.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Endocrinology. - 141 : 6 (2000), p. 2120-2128. -
További szerzők:Varga József L. Schally, Andrew Victor Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Armatis, Patricia Groot, Kate Czompoly Tamás
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9.

001-es BibID:BIBFORM033622
035-os BibID:WOS:000089341400050 PMID:10962031
Első szerző:Rékási Zoltán
Cím:Isolation and sequencing of cDNAs for splice variants of growth hormone-releasing hormone receptors from human cancers / Zoltan Rekasi, Tamas Czompoly, Andrew V. Schally, Gabor Halmos
Dátum:2000
Megjegyzések:The proliferation of various tumors is inhibited by the antagonists of growth hormone-releasing hormone (GHRH) in vitro and in vivo, but the receptors mediating the effects of GHRH antagonists have not been identified so far. Using an approach based on PCR, we detected two major splice variants (SVs) of mRNA for human GHRH receptor (GHRH-R) in human cancer cell lines, including LNCaP prostatic. MiaPaCa-2 pancreatic. MDA-MB-468 breast, OV-1063 ovarian, and H-69 small-cell lung carcinomas. In addition, high-affinity, low-capacity binding sites for GHRH antagonists were found on the membranes of cancer cell lines such as MiaPaCa-2 that are negative for the vasoactive intestinal peptide/pituitary adenylate cyclase-activating polypeptide receptor (VPAC-R) or lines such as LNCaP that are positive for VPAC-R. Sequence analysis of cDNAs revealed that the first three exons in SV1 and SV2 are replaced by a fragment of retained intron 3 having a new putative in-frame start codon. The rest of the coding region of SV1 is identical to that of human pituitary GHRH-R. whereas in SV2 exon 7 is spliced out, resulting in a 1-nt upstream frameshift. which leads to a premature stop codon in exon 8. The intronic sequence may encode a distinct 25-aa fragment of the N-terminal extracellular domain, which could serve as a proposed signal peptide. The continuation of the deduced protein sequence coded by exons 4-13 in SV1 is identical to that of pituitary GHRH-R. SV2 may encode a GHRH-R isoform truncated after the second transmembrane domain. Thus SVs of GHRH-Rs have now been identified in human extrapituitary cells. The findings support the view that distinct receptors are expressed on human cancer cells, which may mediate the antiproliferative effect of GHRH antagonists.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Proceedings of The National Academy of Sciences of The United States of America. - 97 : 19 (2000), p. 10561-10566. -
További szerzők:Czompoly Tamás Schally, Andrew Victor Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus)
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10.

001-es BibID:BIBFORM033614
035-os BibID:PMID:11390017 WOS:000169181800005
Első szerző:Rékási Zoltán
Cím:Antiproliferative actions of growth hormone-releasing hormone antagonists on MiaPaCa-2 human pancreatic cancer cells involve cAMP independent pathways / Zoltan Rekasi, Jozsef L. Varga, Andrew V. Schally, Artur Plonowski, Gabor Halmos, Balazs Csernus, Patricia Armatis, Kate Groot
Dátum:2001
ISSN:0196-9781
Megjegyzések:We evaluated the effects of GHRH antagonists on the proliferation of MiaPaCa-2 human pancreatic cancer cells and cAMP signaling in vitro. GHRH antagonists inhibited the proliferation of MiaPaCa-2 cells in vitro in a dose-dependent way and caused a significant elevation in cAMP production. In a superfusion system, short-term exposure of the cells to GHRH antagonists evoked an acute, dose-dependent release of cAMP into the medium. Native GHRH, which stimulates cAMP efflux from pituitary at nanomolar doses, did not influence cAMP release from cultured or superfused MiaPaCa-2 cells even at 10-30 microM. VIP, PACAP, secretin and glucagon also did not influence cell proliferation or cAMP production. Adenylate cyclase activator forskolin (FSK) caused a greater cAMP response, but a smaller antiproliferative effect than GHRH antagonists. Combined treatment with FSK and GHRH antagonist JV-1-38 potentiated the cAMP-inducing effect of FSK, but did not produce a greater inhibition of cell proliferation than JV-1-38 alone. A selective accumulation of radiolabeled GHRH antagonist [(125)I]JV-1-42 in vivo in MiaPaCa-2 carcinoma xenografted into nude mice was also observed. In conclusion, second messengers other than cAMP participate in the signal transduction pathways of GHRH analogs mediated by tumoral GHRH receptors.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Peptides. - 22 : 6 (2001), p. 879-886. -
További szerzők:Varga József L. Schally, Andrew Victor Plonowski, Artur Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Csernus Balázs Armatis, Patricia Groot, Kate
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11.

001-es BibID:BIBFORM044063
Első szerző:Schally, Andrew Victor
Cím:The actions of Luteinizing hormone-releasing hormone agonists, antagonosts, and cytotoxic analogues on the luteinizing hormone-releasing hormone receptors on the pituitary and tumors / Andrew V. Schally, Gabor Halmos, Zoltán Rékasi, José M. Arencibia-Jimenez
Dátum:2001
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok könyvfejezet
Megjelenés:Infertility and Reproductive Medicine / ed. Paul Devroey. - p. 17-44.
További szerzők:Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Rékási Zoltán Arencibia-Jimenez, José M.
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12.

001-es BibID:BIBFORM033619
035-os BibID:PMID:11027415 WOS:000089614600010
Első szerző:Schally, Andrew Victor
Cím:Peptide analogs in the therapy of prostate cancer / Andrew V. Schally, Ana Maria Comaru-Schally, Artur Plonowski, Attila Nagy, Gabor Halmos, Zoltan Rekasi
Dátum:2000
ISSN:0270-4137
Megjegyzések:The use of peptide analogs in the therapy of prostate cancer is reviewed. The preferred primary treatment of advanced androgen-dependent prostate cancer is presently based on the use of depot preparations of LH-RH agonists. This treatment is likewise recommended in patients with rising PSA levels after surgery or radiotherapy. LH-RH agonists with or without antiandrogens can be also utilized prior to or following various local treatments in patients with clinically localized prostate cancer and at high risk for disease recurrence. LH-RH antagonists like Cetrorelix are in clinical trials. However, most patients with advanced prostatic carcinoma treated by any modality of androgen deprivation eventually relapse. Treatment of relapsed androgen-independent prostate cancer remains a major challenge, but new therapeutic modalities are being developed based on antagonists of growth hormone-releasing hormone (GH-RH) and bombesin, which inhibit growth factors or their receptors. Another approach consists of cytotoxic analogs of LH-RH, bombesin, and somatostatin containing doxorubicin or 2-pyrrolinodoxorubicin, which can be targeted to receptors for these peptides found in prostate cancers and their metastases. These cytotoxic analogs inhibit growth of experimental androgen-dependent or -independent prostate cancers and reduce the incidence of metastases. A rational therapy with peptide analogs could be selected on the basis of receptors present in biopsy samples. The approaches based on peptide analogs should result in a more effective treatment for prostate cancer.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Prostate. - 45 : 2 (2000), p. 158-166. -
További szerzők:Comaru-Schally, Ana Maria Plonowski, Artur Nagy Attila Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Rékási Zoltán
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