2 Citations (Scopus)

Abstract

Incubation of bovine hippocampal membranes with [α-32P]GTP and exposure to ultraviolet light resulted in the labelling of seven species with apparent molecular masses of 200, 74, 55, 53, 50, 43 and 40 kDa. Labelling of the 55 kDa species was greatly enhanced in the presence of carboxyl terminal fragments [neuropeptide Y-(18-36)] of neuropeptide Y. Labelling occurred with [α-32P]GTP but not [α-32P]ATP. A group of putative direct G protein activating peptides including mastoparan, melittin, substance P and adrenocorticotropic hormone (ACTH)-(1-24), were also able to stimulate the labelling of this protein. Labelling of the 55 kDa protein could be demonstrated in bovine brain but not peripheral tissues. Western blot analysis using an antibody against the common α subunit of G proteins recognized a protein co-migrating with the 55 kDa GTP-binding protein. These findings demonstrate the existence of a previously uncharacterized neuronal protein, with an apparent molecular mass of 55 kDa, that binds GTP in response to neuropeptide Y and other peptides.

Original languageEnglish (US)
Pages (from-to)279-291
Number of pages13
JournalEuropean Journal of Pharmacology: Molecular Pharmacology
Volume268
Issue number3
DOIs
StatePublished - Aug 16 1994

Fingerprint

Neuropeptide Y
Guanosine Triphosphate
GTP-Binding Proteins
Proteins
Melitten
Peptides
Ultraviolet Rays
Substance P
Adrenocorticotropic Hormone
Adenosine Triphosphate
Western Blotting
Membranes
Antibodies
Brain

Keywords

  • GTP
  • Neuropeptide Y
  • Photolabeling

ASJC Scopus subject areas

  • Pharmacology

Cite this

Neuropeptide Y promotes GTP photo-incorporation into a 55 kDa protein. / Zhu, Jianhua; Toews, Myron Lee; MacDonald, Richard G; Hexum, Terry D.

In: European Journal of Pharmacology: Molecular Pharmacology, Vol. 268, No. 3, 16.08.1994, p. 279-291.

Research output: Contribution to journalArticle

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abstract = "Incubation of bovine hippocampal membranes with [α-32P]GTP and exposure to ultraviolet light resulted in the labelling of seven species with apparent molecular masses of 200, 74, 55, 53, 50, 43 and 40 kDa. Labelling of the 55 kDa species was greatly enhanced in the presence of carboxyl terminal fragments [neuropeptide Y-(18-36)] of neuropeptide Y. Labelling occurred with [α-32P]GTP but not [α-32P]ATP. A group of putative direct G protein activating peptides including mastoparan, melittin, substance P and adrenocorticotropic hormone (ACTH)-(1-24), were also able to stimulate the labelling of this protein. Labelling of the 55 kDa protein could be demonstrated in bovine brain but not peripheral tissues. Western blot analysis using an antibody against the common α subunit of G proteins recognized a protein co-migrating with the 55 kDa GTP-binding protein. These findings demonstrate the existence of a previously uncharacterized neuronal protein, with an apparent molecular mass of 55 kDa, that binds GTP in response to neuropeptide Y and other peptides.",
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AU - Zhu, Jianhua

AU - Toews, Myron Lee

AU - MacDonald, Richard G

AU - Hexum, Terry D.

PY - 1994/8/16

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N2 - Incubation of bovine hippocampal membranes with [α-32P]GTP and exposure to ultraviolet light resulted in the labelling of seven species with apparent molecular masses of 200, 74, 55, 53, 50, 43 and 40 kDa. Labelling of the 55 kDa species was greatly enhanced in the presence of carboxyl terminal fragments [neuropeptide Y-(18-36)] of neuropeptide Y. Labelling occurred with [α-32P]GTP but not [α-32P]ATP. A group of putative direct G protein activating peptides including mastoparan, melittin, substance P and adrenocorticotropic hormone (ACTH)-(1-24), were also able to stimulate the labelling of this protein. Labelling of the 55 kDa protein could be demonstrated in bovine brain but not peripheral tissues. Western blot analysis using an antibody against the common α subunit of G proteins recognized a protein co-migrating with the 55 kDa GTP-binding protein. These findings demonstrate the existence of a previously uncharacterized neuronal protein, with an apparent molecular mass of 55 kDa, that binds GTP in response to neuropeptide Y and other peptides.

AB - Incubation of bovine hippocampal membranes with [α-32P]GTP and exposure to ultraviolet light resulted in the labelling of seven species with apparent molecular masses of 200, 74, 55, 53, 50, 43 and 40 kDa. Labelling of the 55 kDa species was greatly enhanced in the presence of carboxyl terminal fragments [neuropeptide Y-(18-36)] of neuropeptide Y. Labelling occurred with [α-32P]GTP but not [α-32P]ATP. A group of putative direct G protein activating peptides including mastoparan, melittin, substance P and adrenocorticotropic hormone (ACTH)-(1-24), were also able to stimulate the labelling of this protein. Labelling of the 55 kDa protein could be demonstrated in bovine brain but not peripheral tissues. Western blot analysis using an antibody against the common α subunit of G proteins recognized a protein co-migrating with the 55 kDa GTP-binding protein. These findings demonstrate the existence of a previously uncharacterized neuronal protein, with an apparent molecular mass of 55 kDa, that binds GTP in response to neuropeptide Y and other peptides.

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KW - Photolabeling

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