Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids

Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptid...
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Autor*in:	Cavazza, Antonella [verfasserIn] Marini, Mario [verfasserIn] Roda, L. Giorgio [verfasserIn] Tarantino, Umberto [verfasserIn] Valenti, Angela [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2011

Schlagwörter:	Neuropeptides Osteosarcoma cell line Enzyme hydrolysis

Übergeordnetes Werk:	Enthalten in: Neurochemical research - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1976, 36(2011), 12 vom: 21. Aug.
Übergeordnetes Werk:	volume:36 ; year:2011 ; number:12 ; day:21 ; month:08

Links:	Volltext

DOI / URN:	10.1007/s11064-011-0559-2

Katalog-ID:	SPR016250702

Internformat


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520			\|a Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide.
650		4	\|a Neuropeptides \|7 (dpeaa)DE-He213
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650		4	\|a Enzyme hydrolysis \|7 (dpeaa)DE-He213
700	1		\|a Marini, Mario \|e verfasserin \|4 aut
700	1		\|a Roda, L. Giorgio \|e verfasserin \|4 aut
700	1		\|a Tarantino, Umberto \|e verfasserin \|4 aut
700	1		\|a Valenti, Angela \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Neurochemical research \|d Dordrecht [u.a.] : Springer Science + Business Media B.V, 1976 \|g 36(2011), 12 vom: 21. Aug. \|w (DE-627)320587770 \|w (DE-600)2018503-0 \|x 1573-6903 \|7 nnns
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912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_138
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_152
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
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912			\|a GBV_ILN_224
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912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
912			\|a GBV_ILN_702
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912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
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912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
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912			\|a GBV_ILN_2039
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2107
912			\|a GBV_ILN_2108
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912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2116
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912			\|a GBV_ILN_2119
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912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2472
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912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
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912			\|a GBV_ILN_4307
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author_variant	a c ac m m mm l g r lg lgr u t ut a v av
matchkey_str	article:15736903:2011----::yrlssfusacpnhpeecotesesroaelieasr
hierarchy_sort_str	2011
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publishDate	2011
allfields	10.1007/s11064-011-0559-2 doi (DE-627)SPR016250702 (SPR)s11064-011-0559-2-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Cavazza, Antonella verfasserin aut Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide. Neuropeptides (dpeaa)DE-He213 Osteosarcoma cell line (dpeaa)DE-He213 Enzyme hydrolysis (dpeaa)DE-He213 Marini, Mario verfasserin aut Roda, L. Giorgio verfasserin aut Tarantino, Umberto verfasserin aut Valenti, Angela verfasserin aut Enthalten in Neurochemical research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1976 36(2011), 12 vom: 21. Aug. (DE-627)320587770 (DE-600)2018503-0 1573-6903 nnns volume:36 year:2011 number:12 day:21 month:08 https://dx.doi.org/10.1007/s11064-011-0559-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 36 2011 12 21 08
spelling	10.1007/s11064-011-0559-2 doi (DE-627)SPR016250702 (SPR)s11064-011-0559-2-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Cavazza, Antonella verfasserin aut Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide. Neuropeptides (dpeaa)DE-He213 Osteosarcoma cell line (dpeaa)DE-He213 Enzyme hydrolysis (dpeaa)DE-He213 Marini, Mario verfasserin aut Roda, L. Giorgio verfasserin aut Tarantino, Umberto verfasserin aut Valenti, Angela verfasserin aut Enthalten in Neurochemical research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1976 36(2011), 12 vom: 21. Aug. (DE-627)320587770 (DE-600)2018503-0 1573-6903 nnns volume:36 year:2011 number:12 day:21 month:08 https://dx.doi.org/10.1007/s11064-011-0559-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 36 2011 12 21 08
allfields_unstemmed	10.1007/s11064-011-0559-2 doi (DE-627)SPR016250702 (SPR)s11064-011-0559-2-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Cavazza, Antonella verfasserin aut Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide. Neuropeptides (dpeaa)DE-He213 Osteosarcoma cell line (dpeaa)DE-He213 Enzyme hydrolysis (dpeaa)DE-He213 Marini, Mario verfasserin aut Roda, L. Giorgio verfasserin aut Tarantino, Umberto verfasserin aut Valenti, Angela verfasserin aut Enthalten in Neurochemical research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1976 36(2011), 12 vom: 21. Aug. (DE-627)320587770 (DE-600)2018503-0 1573-6903 nnns volume:36 year:2011 number:12 day:21 month:08 https://dx.doi.org/10.1007/s11064-011-0559-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 36 2011 12 21 08
allfieldsGer	10.1007/s11064-011-0559-2 doi (DE-627)SPR016250702 (SPR)s11064-011-0559-2-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Cavazza, Antonella verfasserin aut Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide. Neuropeptides (dpeaa)DE-He213 Osteosarcoma cell line (dpeaa)DE-He213 Enzyme hydrolysis (dpeaa)DE-He213 Marini, Mario verfasserin aut Roda, L. Giorgio verfasserin aut Tarantino, Umberto verfasserin aut Valenti, Angela verfasserin aut Enthalten in Neurochemical research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1976 36(2011), 12 vom: 21. Aug. (DE-627)320587770 (DE-600)2018503-0 1573-6903 nnns volume:36 year:2011 number:12 day:21 month:08 https://dx.doi.org/10.1007/s11064-011-0559-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 36 2011 12 21 08
allfieldsSound	10.1007/s11064-011-0559-2 doi (DE-627)SPR016250702 (SPR)s11064-011-0559-2-e DE-627 ger DE-627 rakwb eng 610 ASE 44.90 bkl Cavazza, Antonella verfasserin aut Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide. Neuropeptides (dpeaa)DE-He213 Osteosarcoma cell line (dpeaa)DE-He213 Enzyme hydrolysis (dpeaa)DE-He213 Marini, Mario verfasserin aut Roda, L. Giorgio verfasserin aut Tarantino, Umberto verfasserin aut Valenti, Angela verfasserin aut Enthalten in Neurochemical research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1976 36(2011), 12 vom: 21. Aug. (DE-627)320587770 (DE-600)2018503-0 1573-6903 nnns volume:36 year:2011 number:12 day:21 month:08 https://dx.doi.org/10.1007/s11064-011-0559-2 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 44.90 ASE AR 36 2011 12 21 08
language	English
source	Enthalten in Neurochemical research 36(2011), 12 vom: 21. Aug. volume:36 year:2011 number:12 day:21 month:08
sourceStr	Enthalten in Neurochemical research 36(2011), 12 vom: 21. Aug. volume:36 year:2011 number:12 day:21 month:08
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Neuropeptides Osteosarcoma cell line Enzyme hydrolysis
dewey-raw	610
isfreeaccess_bool	false
container_title	Neurochemical research
authorswithroles_txt_mv	Cavazza, Antonella @@aut@@ Marini, Mario @@aut@@ Roda, L. Giorgio @@aut@@ Tarantino, Umberto @@aut@@ Valenti, Angela @@aut@@
publishDateDaySort_date	2011-08-21T00:00:00Z
hierarchy_top_id	320587770
dewey-sort	3610
id	SPR016250702
language_de	englisch
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The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. 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author	Cavazza, Antonella
spellingShingle	Cavazza, Antonella ddc 610 bkl 44.90 misc Neuropeptides misc Osteosarcoma cell line misc Enzyme hydrolysis Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids
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topic_title	610 ASE 44.90 bkl Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids Neuropeptides (dpeaa)DE-He213 Osteosarcoma cell line (dpeaa)DE-He213 Enzyme hydrolysis (dpeaa)DE-He213
topic	ddc 610 bkl 44.90 misc Neuropeptides misc Osteosarcoma cell line misc Enzyme hydrolysis
topic_unstemmed	ddc 610 bkl 44.90 misc Neuropeptides misc Osteosarcoma cell line misc Enzyme hydrolysis
topic_browse	ddc 610 bkl 44.90 misc Neuropeptides misc Osteosarcoma cell line misc Enzyme hydrolysis
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title	Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids
ctrlnum	(DE-627)SPR016250702 (SPR)s11064-011-0559-2-e
title_full	Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids
author_sort	Cavazza, Antonella
journal	Neurochemical research
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author_browse	Cavazza, Antonella Marini, Mario Roda, L. Giorgio Tarantino, Umberto Valenti, Angela
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title_sort	hydrolysis of substance p in the presence of the osteosarcoma cell line saos-2: release of free amino acids
title_auth	Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids
abstract	Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide.
abstractGer	Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide.
abstract_unstemmed	Abstract The possible hydrolysis of substance P (Arg–Pro–Lys–Pro–Gln–Gln–Phe–Phe–Gly–Leu–Met) in presence of the osteoblastic cell line SaOS-2 was measured by capillary electrophoresis coupled to mass detection. The results obtained indicate that a very rapid disappearance of the intact undecapeptide was associated to a slower appearance of seven of its eight component amino acids. These results can be interpreted as indicating that an extremely fast hydrolysis of substance P by endopeptidases, which released peptidic by-products, was followed by a noticeably slower secondary degradation which released free amino acids. In decreasing quantitative importance, these phenomena appear to originate by the hydrolysis of the $ Pro_{4} $–$ Gln_{5} $ bond, followed by C-terminal sequential degradation of the $ Arg_{1} $–$ Pro_{4} $ tetrapeptide; by the hydrolysis of or $ Phe_{7} $–$ Phe_{8} $ bond (or, possibly, of $ Gln_{6} $–$ Phe_{7} $) leading to release of free Phe and Gln; by hydrolysis of the $ Gly_{9} $–$ Leu_{10} $ bond with subsequent release of Met and Leu. Results obtained appear to be compatible with the expression by SaOS-2 cells of enzymes already known to catalyze substance P hydrolysis, together with an apparent low efficiency of aminopeptidases. Because of the activity of C-terminal fragments on NK1 receptors, the delay between primary hydrolysis of substance P and secondary hydrolysis of its peptidic fragments indicated by the data shown implies a possible persistence of substance P physiological effects even after degradation of the intact peptide.
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container_issue	12
title_short	Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids
url	https://dx.doi.org/10.1007/s11064-011-0559-2
remote_bool	true
author2	Marini, Mario Roda, L. Giorgio Tarantino, Umberto Valenti, Angela
author2Str	Marini, Mario Roda, L. Giorgio Tarantino, Umberto Valenti, Angela
ppnlink	320587770
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isOA_txt	false
hochschulschrift_bool	false
doi_str	10.1007/s11064-011-0559-2
up_date	2024-07-03T21:52:31.336Z
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Hydrolysis of Substance P in the Presence of the Osteosarcoma Cell Line SaOS-2: Release of Free Amino Acids

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