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1.

001-es BibID:BIBFORM033557
035-os BibID:WOS:000233762000030
Első szerző:Havt, Alexandre
Cím:The expression of the pituitary growth hormone-releasing hormone receptor and its splice variants in normal and neoplastic human tissues / Alexandre Havt, Andrew V. Schally, Gabor Halmos, Jozsef L. Varga, Gabor L. Toller, Judit E. Horvath, Karoly Szepeshazi, Frank Köster, Kevin Kovitz, Kate Groot, Marta Zarandi, Celia A. Kanashiro
Dátum:2005
ISSN:0027-8424
Megjegyzések:Various attempts to detect human pituitary growth hormone-releasing hormone receptor (pGHRH-R) in neoplastic extrapituitary tissues have thus far failed. Recently, four splice variants (SVs) of GHRH-R have been described, of which SV1 has the highest structural homology to pGHRH-R and likely plays a role in tumor growth. The aim of this study was to reinvestigate whether human tumors and normal human extrapituitary tissues express the pGHRH-R and to corroborate our previous findings on its SVs. Thus, we developed a real-time PCR method for the detection of the mRNA for the pGHRH-R, its SVs, and the GHRH peptide. Using real-time PCR, Western blotting, and radioligand-binding assays, we detected the mRNA for pGHRH-R and pGHRH-R protein in various human cancer cell lines grown in nude mice and in surgical specimens of human lung cancers. The expression of mRNA for SVs of pGHRH-R and GHRH was likewise found in xenografts of human non-Hodgkin's lymphomas, pancreatic cancer, glioblastoma, small-cell lung carcinomas, and in human nonmalignant prostate, liver, lung, kidney, and pituitary. Western blots showed that these normal and malignant human tissues contain SV1 protein and immunoreactive GHRH. Our results demonstrate that some normal human tissues and tumors express mRNA and protein for the pGHRH-R and its splice variants. These findings confirm and extend the concept that GHRH and its receptors play an important role in the pathophysiology of 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. - 102 : 48 (2005), p. 17424-17429. -
További szerzők:Schally, Andrew Victor Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Varga József L. Toller Gábor L. Horváth Judit E. (New Orleans) Szepesházi Károly Köster, Frank Kovitz, Kevin Groot, Kate Zarándi Márta Kanashiro, Celia A.
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2.

001-es BibID:BIBFORM033707
035-os BibID:WOS:A1995RA15000032
Első szerző:Izdebski, Jan
Cím:Synthesis and biological evaluation of superactive agonists of growth hormone-releasing hormone / Jan Izdebski, Jacek Pinski, Judit E. Horvath, Gabor Halmos, Kate Groot, Andrew V. Schally
Dátum:1995
ISSN:0027-8424
Megjegyzések:Analogs of the 29 amino acid sequence of human growth hormone-releasing hormone (hGH-RH) with agmatine (Agm) in position 29, desaminotyrosine (Dat) in position 1, norleucine (Nle) in position 27, and L-alpha-aminobutyric acid (Abu) in position 15 have been synthesized, and their biological activity was evaluated. Some peptides contained one or two residues of ornithine (Orn) instead of Lys in positions 12 and 21 and additional replacements in positions 8 and 28. All analogs were found to be more potent than hGH-RH-(1-29)-NH2 in the superfused rat pituitary cell system. In tests in vivo in rats after subcutaneous administration, the analogs JI-22, [Dat(1),Orn(12,21),Abu(15),Nle(27),Agm(29)]hGH-RH-(1-29); JI-34, [Dat(1),Orn(12,21),Abu(15),Nle(27),Asp(28),Agm(29)] hGH-RH-(1-29); JI-36, [Dat(1),Thr(8),Orn(12,21), Abu(15),Nle(27),Asp(28),Agm(29)]hGH-RH-(1-29); and JI-38, [Dat(1),Gln(8),Orn(12,21),Abu(15),Nle(27),Asp(28),Agm(29)] hGH-RH-(1-29) displayed a potency 44.6, 80.9, 95.8, and 71.4 times greater, respectively, than that of hGH-RH-(1-29)-NH2 at 15 min and 217.1, 89.7, 87.9, and 116.8 times greater at 30 min. After intravenous administration, JI-22, JI-36, and JI-38 were 3.2-3.8 times more potent than hGH-RH-(1-29)-NH2 at 5 min and 6.1-8.5 times more active at 15 min. All analogs were found to have higher binding affinities for GH-RH receptors on rat pituitary cells than hGH-RH-(1-29)-NH2. Because of high activity and greater stability, these analogs could be considered for therapy of patients with growth hormone deficiency.
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. - 92 : 11 (1995), p. 4872-4876. -
További szerzők:Pinski, Jacek Horváth Judit E. (New Orleans) Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Groot, Kate Schally, Andrew Victor
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3.

001-es BibID:BIBFORM033697
035-os BibID:WOS:A1996UW79200078
Első szerző:Nagy Attila
Cím:Cytotoxic analogs of luteinizing hormone-releasing hormone containing doxorubicin or 2-pyrrolinodoxorubicin, a derivative 500-1000 times more potent / Attila Nagy, Andrew V. Schally, Patricia Armatis, Karoly Szepeshazi, Gabor Halmos, Magdolna Kovacs, Marta Zarandi, Kate Groot, Masahiro Miyazaki, Andreas Jungwirth, Judit Horvath
Dátum:1996
ISSN:0027-8424
Megjegyzések:Doxorubicin (DOX) and its daunosamine-modified derivative, 2-pyrrolino-DOX, which is 500-1000 times more active than DOX, were incorporated into agonistic and antagonistic analogs of luteinizing hormone-releasing hormone (LH-RH), The conjugation of DOX with LH-RH analogs was performed by using N-(9-fluorenylmethoxycarbonyl)-DOX-14-O-hemiglutarate, a dicarboxylic acid ester derivative of DOX, Coupling this derivative covalently to the E-amino group of the D-Lys side chain of agonist [D-Lys(6)]LH-RH or antagonistic analog Ac-D-Nal(2)-D-Phe(4Cl)-D-Pal(3)-Ser-Tyr-D-Lys-Leu-Arg-Pro-D-Ala-NH2 [where Nal(2) = 3-(2-naphthyl)alanine, Pal(3) = 3-(3-pyridyl)alanine, and Phe(4Cl) = 4-chlorophenylalanine] was followed by the removal of the 9-fluorenylmethoxycarbonyl protective group to yield cytotoxic derivatives of LH-RH analogs containing DOX, From these DOX containing LH-RH hybrids, intensely potent analogs with daunosamine-modified derivatives of DOX can be readily formed. Thus, cytotoxic LH-RH agonist containing DOX (AN-152) can be converted in a 66% yield by a reaction with a 30-fold excess of 4-iodobutyraldehyde in N,N-dimethylformamide into a derivative having 2-pyrrolino-DOX (AN-207). Hybrid molecules AN-152 and AN-207 fully preserve the cytotoxic activity of their radicals, DOX or 2-pyrrolino-DOX, respectively, in vitro, and also retain the high binding affinity of the peptide hormone portion of the conjugates to rat pituitary receptors for LH-RH, These highly potent cytotoxic analogs of LH-RH were designed as targeted anti-cancer agents for the treatment of various tumors that possess receptors for the carrier peptide, Initial in vivo studies show that the hybrid molecules are much less toxic than the respective cytotoxic radicals incorporated and significantly more active in inhibiting tumor growth.
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. - 93 : 14 (1996), p. 7269-7273. -
További szerzők:Schally, Andrew Victor Armatis, Patricia Szepesházi Károly Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Kovács Magdolna Zarándi Márta Groot, Kate Miyazaki, Masahiro Jungwirth, Andreas Horváth Judit E. (New Orleans)
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4.

001-es BibID:BIBFORM033686
Első szerző:Szepesházi Károly
Cím:A single in vivo administration of bombesin antagonist RC-3095 reduces the levels and mRNA expression of epidermal growth factor receptors in MXT mouse mammary cancers / Karoly Szepeshazi, Andrew V. Schally, Gabor Halmos, Najib Lamharzi, Kate Groot, Judit E. Horvath
Dátum:1997
ISSN:0027-8424
Megjegyzések:Epidermal growth factor (EGF) and its receptors (EGFR) play important roles in tumorigenesis. In various experimental cancers, treatment with antagonists of bombesin/gastrin-releasing peptide (BN/GRP) produces a reduction in EGFRs, concomitant to inhibition of tumor growth. To investigate the mechanisms involved, we monitored concentrations of BN/GRP antagonist RC-3095 in serum of mice, rats, and hamsters given a single subcutaneous or intravenous injection of this analog. In parallel studies, we measured levels and mRNA expression of EGFRs in estrogen-dependent and independent MXT mouse mammary cancers, following a single subcutaneous administration of RC-3095 to tumor-bearing mice. Peak values of RC-3095 in serum were detected 2 min after intravenous or 15 min after subcutaneous injection. The levels of RC-3095 declined rapidly and became undetectable after 3-5 hr. In the estrogen-dependent MXT tumors, the concentration of EGF receptors was reduced by about 60% 6 hr following injection and returned to original level after 24 hr. Levels of mRNA for EGFR fell parallel with the receptor number and were nearly normal after 24 hr. In the hormone-independent MXT cancers, the number of EGFRs decreased progressively, becoming undetectable 6 hr after injection of RC-3095, and returned to normal values at 24 hr, but EGFR mRNA levels remained lower for 48 hr. Thus, in spite of rapid elimination from serum, BN/GRP antagonist RC-3095 can induce a prolonged decrease in levels and mRNA expression of EGFRs. These findings may explain how single daily injections of BN/GRP antagonists can maintain tumor growth inhibition.
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. - 94 : 20 (1997), p. 10913-10918. -
További szerzők:Schally, Andrew Victor Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Lamharzi, Najib Groot, Kate Horváth Judit E. (New Orleans)
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5.

001-es BibID:BIBFORM033898
035-os BibID:(PMID)8008640
Első szerző:Szőke Balázs
Cím:LH-RH analogue carrying a cytotoxic radical is internalized by rat pituitary cells in vitro / Balázs Szőke, Judit Horváth, Gábor Halmos, Zoltán Rékási, Kate Groot, Attila Nagy, Andrew V. Schally
Dátum:1994
ISSN:0196-9781
Megjegyzések:The binding and internalization of a cytotoxic analogue of luteinizing hormone-releasing hormone (LH-RH), T-98 (agonist [D-Lys6]LH-RH linked to glutaryl-2-(hydroxymethyl)anthraquinone), by rat anterior pituitary cells was investigated. Analogue T-98 was bound to pituitary membrane binding sites for LH-RH with a high affinity (Kd = 1.2 nM) and was 17 times more potent in releasing luteinizing hormone (LH) from superfused rat pituitary cells than LH-RH. The labeling of this cytotoxic LH-RH analogue was carried out both with radioactive (125I) and nonradioactive iodine. Monoiodination of the Tyr5 residue of T-98 did not significantly affect its binding affinity but greatly decreased its LH-releasing activity to about 3% of the original value. Di-iodination in the same position lowered binding affinity twenty-threefold and further diminished LH-releasing potency. [125I]T-98 was found to bind very strongly to polystyrene, which precluded the use of regular tissue culture plasticware in our experiments. In pituitary cells cultured in glass vials, binding and internalization of [125I]T-98 were observed, which were time and temperature dependent, and which could be inhibited by excess unlabeled analogue. No enzymatic degradation of labeled T-98 was detected in the culture medium during the incubation. Our results indicate that T-98 is internalized by pituitary gonadotropes through receptor-mediated endocytosis. Because this new class of compounds was designed as anticancer drugs, our findings also suggest that this cytotoxic LH-RH agonist may also be internalized by LH-RH receptors present in breast, prostate, ovarian, and other tumors.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
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Megjelenés:Peptides. - 15 : 2 (1994), p. 359-366. -
További szerzők:Horváth Judit E. (New Orleans) Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Rékási Zoltán Groot, Kate Nagy Attila Schally, Andrew Victor
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6.

001-es BibID:BIBFORM033588
035-os BibID:PMID:15469915 WOS:000224688700034
Első szerző:Toller Gábor L.
Cím:Development of a polyclonal antiserum for the detection of the isoforms of the receptors for human growth hormone-releasing hormone on tumors / Gabor L. Toller, Judit E. Horvath, Andrew V. Schally, Gabor Halmos, Jozsef L. Varga, Kate Groot, David Chism, Marta Zarandi
Dátum:2004
ISSN:0027-8424
Megjegyzések:Antagonists of growth hormone-releasing hormone (GHRH) inhibit the growth of various human cancers by multiple mechanisms, which include direct effects on tumor cells through the splice variants (SV) of the GHRH receptor. Our findings suggest that the tumoral protein encoded by SV 1 (SV1) is a likely functional receptor. The aim of this study was to develop a polyclonal antiserum against a polypeptide analog of segment 1-25 of the putative SV1 receptor protein. Rabbits were immunized with [Ala-23]SV1 (1-25)-Tyr-26-Cys-27-NH2 as a hapten, conjugated to BSA or keyhole limpet hemocyanin. The antisera thus generated were evaluated by RIA for binding to the radiolabeled hapten. The specificity and sensitivity of the antisera were studied on xenografts of RL and HT human non-Hodgkin's lymphomas. The sera raised against keyhole limpet hemocyanin-SV1 hapten, showed binding values of 50-75% at a 1:56,000 dilution. In Western blot analyses, the purified polyclonal antibody recognized a specific signal with a molecular mass of approximately 40 kDa in RL and HT lymphomas. This band corresponds to the estimated molecular mass of the GHRH receptor isoform encoded by SV1. RT-PCR and ligand binding studies also revealed the expression of SV1 and the presence of high-affinity binding sites for GHRH on RL and HT tumors. Because the antiserum developed recognizes the tumoral GHRH receptor protein encoded by SV1, it should be of value in various investigations.
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. - 101 : 42 (2004), p. 15160-15165. -
További szerzők:Horváth Judit E. (New Orleans) Schally, Andrew Victor Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Varga József L. Groot, Kate Chism, David Zarándi Márta
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7.

001-es BibID:BIBFORM033591
035-os BibID:WOS:000188921200052
Első szerző:Varga József L.
Cím:Increased activity of antagonists of growth hormone-releasing hormone substituted at positions 8, 9, and 10 / Jozsef L. Varga, Andrew V. Schally, Judit E. Horvath, Magdolna Kovacs, Gabor Halmos, Kate Groot, Gabor L. Toller, Zoltan Rekasi, Marta Zarandi
Dátum:2004
ISSN:0027-8424
Megjegyzések:Antagonists of human growth hormone-releasing hormone (hGHRH) with increased potency and improved enzymatic and chemical stability are needed for potential clinical applications. We synthesized 21 antagonistic analogs of hGHRH(1-29)NH2, substituted at positions 8, 9, and 10 of the common core sequence {phenylacetyl-Tyr1, D-Arg(2,28), para-chloro-phenylalanine 6, Arg(9)/homoarginine 9, Tyr(10)/O-methyltyrosine 10, alpha-aminobutyric acid 15, norleucine 27, Har(29)} hGHRH(1-29)NH2. Inhibitory effects on hGHRH-induced GH release were evaluated in vitro in a superfused rat pituitary system, as well as in vivo after i.v. injection into rats. The binding affinities of the peptides to pituitary GHRH receptors were also determined. Introduction of para-amidinophenylalanine 10 yielded antagonists JV-1-62 and -63 with the highest activities in vitro and lowest receptor dissociation constants (K-i = 0.057-0.062 nM). Antagonists JV-1-62 and -63 also exhibited the strongest effect in vivo, significantly (P < 0.05-0.001) inhibiting hGHRH-induced GH release for at least 1 h. Para-aminopherylalanine 10 and O-ethyltyrosine 10 substitutions yielded antagonists potent in vitro, but His(10), 3,3'-diphenylalanine 10, 2-naphthylalanine 10,and cyclohexylalanine 10 modifications were detrimental. Antagonists containing citrulline 9 (in MZ-J-7-72), amidinophenylalanine 9 (in JV-1-65), HiS(9), D-Arg(9), citrulline 8, AIa(8), D-Ala(8), or alpha-aminobutyric acid 8 substituents also had high activity and receptor affinity in vitro. However, in vitro potencies of analogs with substitution in position 9 correlated poorly with acute endocrine effects in vivo, as exemplified by the weak and/or short inhibitory actions of antagonists JV-1-65 and MZ-J-7-72 on GH release in vivo. Nevertheless, antagonist JV-1-65 was more potent than JV-1-63 in tests on inhibition of the growth of human prostatic and lung cancer lines xenografted into nude mice. This indicates that oncological activity may be based on several mechanisms. hGHRH antagonists with improved efficacy could be useful for treatment of cancers that depend on insulin-like growth factors or GHRH.
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. - 101 : 6 (2004), p. 1708-1713. -
További szerzők:Schally, Andrew Victor Horváth Judit E. (New Orleans) Kovács Magdolna Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Groot, Kate Toller Gábor L. Rékási Zoltán Zarándi Márta
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8.

001-es BibID:BIBFORM033541
035-os BibID:WOS:000236362600052
Első szerző:Zarándi Márta
Cím:Lipopeptide antagonists of growth hormone-releasing hormone with improved antitumor activities / Marta Zarandi, Jozsef L. Varga, Andrew V. Schally, Judit E. Horvath, Gabor L. Toller, Magdolna Kovacs, Markus Letsch, Kate Groot, Patricia Armatis, Gabor Halmos
Dátum:2006
ISSN:0027-8424
Megjegyzések:Antagonists of growth hormone-releasing hormone (GHRH) synthesized previously inhibit proliferation of various human cancers, but derivatisation with fatty acids could enhance their clinical efficacy. We synthesized a series of antagonists of GHRH(1-29)NH2 acylated at the N terminus with monocarboxylic or alpha,omega-dicarboxylic acids containing six to sixteen carbon atoms. These peptides are analogs of prior potent antagonists JV-1-36, JV-1-38, and JV-1-65 with phenylacetyl group at their N terminus. Several new analogs, including MZ-J-7-46 and MZA-7-30, more effectively inhibited GHRH-induced GH release in vitro in a superfused rat pituitary system than their parent compound JV-1-36 and had increased binding affinities to rat pituitary GHRH receptors, but they showed weaker inhibition of GH release in vivo than JV-1-36. All antagonists acylated with fatty acids containing 8-14 carbon atoms inhibited the proliferation of MiaPaCa-2 human pancreatic cancer cells in vitro better than JV-1-36 or JV-1-65. GHRH antagonist MZ-J-7-114 (5 mu g/day) significantly suppressed the growth of PC-3 human androgen-independent prostate cancers xenografted into nude mice and reduced serum lGF-I levels, whereas antagonist JV-1-38 had no effect at the dose of 10 mu g/day. GHRH antagonists including MZ-J-7-46 and MZ-J-7-114 acylated with octanoic acid and MZ-J-7-30 and MZ-J-7-110 acylated with 1,12-dodecanedicarboxylic acid represent relevant improvements over earlier antagonists. These and previous results suggest that this class of GHRH antagonists might be effective in the treatment of various 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. - 103 : 12 (2006), p. 4610-4615. -
További szerzők:Varga József L. Schally, Andrew Victor Horváth Judit E. (New Orleans) Toller Gábor L. Kovács Magdolna Letsch, Markus Groot, Kate Armatis, Patricia Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus)
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9.

001-es BibID:BIBFORM033755
Első szerző:Zarándi Márta
Cím:Synthesis and in vitro biological activities of new potent GH-RH antagonists with citrulline substitutions / Márta Zarándi, Magdolna Kovács, Judit E. Horváth, Gábor Halmos, Kate Groot, Andrew V. Schally
Dátum:1998
ISSN:0196-9781
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok előadáskivonat
Megjelenés:Peptides 1996 : Proceedings of the Twenty-Fourth European Peptide Symposium, September 8-13, 1996, Edinburg, Scotland / eds. by Robert Ramage, Roger Epton. - p. 933-934.
További szerzők:Kovács Magdolna Horváth Judit E. (New Orleans) Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Groot, Kate Schally, Andrew Victor
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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10.

001-es BibID:BIBFORM033695
035-os BibID:PMID:9145431 WOS:A1997WX50100015
Első szerző:Zarándi Márta
Cím:Synthesis and in vitro evaluation of new potent antagonists of growth hormone-releasing hormone (GH-RH) / Marta Zarandi, Magdolna Kovacs, Judit E. Horvath, Katalin Toth, Gabor Halmos, Kate Groot, Attila Nagy, Zoltan Kele, Andrew V. Schally
Dátum:1997
ISSN:0196-9781
Megjegyzések:In the search for more potent antagonists of hGH-RH, 20 new analogs were synthesized, purified and tested in vitro. All the analogs were based on the N-terminal sequence of 28 or 29 amino acid residues of hGH-RH, but contained D-Arg2 and Nle27 modifications. Most analogs had Phe (pCl)6 and Agm29 substituents. The effect of other substitutions such as Abu8 and/or Abu15 and Ala15 and various hydrophobic and hydrophilic D or L amino acids at position 8 were also investigated. All the peptides were acylated at the N-terminus in an attempt to increase the antagonistic activity. In the superfused rat pituitary cell system, most analogs inhibited more powerfully the GH release induced by GH-RH than the standard antagonist [Ac-Tyr1, D-Arg2]hGH-RH (1-29)-NH2. Some antagonists were long acting. Among the peptides synthesized, antagonist PhAc[D-Arg2, Phe(pCl)6, Abu15, Nle27]hGH-RH (1-28) Agm (MZ-5-156) appeared to be the most potent and inhibited GH release in vitro 63-200 times more powerfully than the standard antagonist. MZ-5-156 and other antagonists showed high binding affinities to membrane receptors for GH-RH. Some of these hGH-RH antagonists could be further developed for possible onocological applications.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Peptides. - 18 : 3 (1997), p. 423-430. -
További szerzők:Kovács Magdolna Horváth Judit E. (New Orleans) Tóth Katalin Halmos Gábor (1962-) (gyógyszerész, receptorfarmakológus, experimentális onkológus) Groot, Kate Nagy Attila Kele Zoltán Schally, Andrew Victor
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