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  • 1
    Publication Date: 1987-10-30
    Description: To investigate whether a particular receptor subtype can be coupled to multiple effector systems, recombinant M2 muscarinic receptors were expressed in cells lacking endogenous receptor. The muscarinic agonist carbachol both inhibited adenylyl cyclase and stimulated phosphoinositide hydrolysis. The stimulation of phosphoinositide hydrolysis was significantly less efficient and more dependent on receptor levels than the inhibition of adenylyl cyclase. Both responses were mediated by guanine nucleotide binding proteins, as evidenced by their inhibition by pertussis toxin; the more efficiently coupled adenylyl cyclase response was significantly more sensitive. Thus, individual subtypes of a given receptor are capable of regulating multiple effector pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ashkenazi, A -- Winslow, J W -- Peralta, E G -- Peterson, G L -- Schimerlik, M I -- Capon, D J -- Ramachandran, J -- CA16417/CA/NCI NIH HHS/ -- HL23632/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):672-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2823384" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylate Cyclase Toxin ; Adenylyl Cyclases/*metabolism ; Animals ; Carbachol/pharmacology ; Cell Line ; Cricetinae ; Cyclic AMP/biosynthesis ; GTP-Binding Proteins/*metabolism ; Gene Expression Regulation ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Triphosphate/analogs & derivatives/metabolism ; Oxotremorine/pharmacology ; Pertussis Toxin ; Phosphatidylinositols/*metabolism ; Receptors, Muscarinic/*metabolism ; Recombinant Proteins ; Thionucleotides/metabolism ; Virulence Factors, Bordetella/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1986-07-11
    Description: Mammalian cell lines have been engineered to produce a secreted form of the AIDS retrovirus envelope glycoprotein. The recombinant protein has been isolated from growth-conditioned culture media and used to immunize animals. Antibodies directed against the recombinant molecule were found to react with the envelope glycoprotein produced in virus-infected cells. Furthermore, these antibodies were able to directly inactivate the AIDS retrovirus in a neutralization assay in vitro. The expression system reported here should provide sufficient quantities of the AIDS retrovirus envelope protein for biological and vaccination studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lasky, L A -- Groopman, J E -- Fennie, C W -- Benz, P M -- Capon, D J -- Dowbenko, D J -- Nakamura, G R -- Nunes, W M -- Renz, M E -- Berman, P W -- HL 33774-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jul 11;233(4760):209-12.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3014647" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Animals ; Antibodies, Viral/*immunology ; Antigens, Viral/biosynthesis/*immunology ; Cricetinae ; Deltaretrovirus/*immunology ; Guinea Pigs ; HIV Antibodies ; HIV Antigens ; Humans ; Immune Sera/immunology ; Male ; Neutralization Tests ; Rabbits ; Recombinant Proteins/biosynthesis/immunology ; Viral Envelope Proteins/biosynthesis/*immunology ; Viral Vaccines/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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