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Cellular mechanisms of somatostatin action in the gut

dc.contributor.authorDelValle, Johnen_US
dc.contributor.authorPark, Jungen_US
dc.contributor.authorChiba, Tsutomuen_US
dc.contributor.authorYamada, Tadatakaen_US
dc.date.accessioned2006-04-10T13:37:20Z
dc.date.available2006-04-10T13:37:20Z
dc.date.issued1990-09en_US
dc.identifier.citationDelValle, John, Park, Jung, Chiba, Tsutomu, Yamada, Tadataka (1990/09)."Cellular mechanisms of somatostatin action in the gut." Metabolism 39(9, Supplement 2): 134-137. <http://hdl.handle.net/2027.42/28402>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WN4-4C2SHDV-76/2/f4fe050a806074a9b0ee0cd83b14322den_US
dc.identifier.urihttps://hdl.handle.net/2027.42/28402
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1976208&dopt=citationen_US
dc.description.abstractWe have used isolated canine parietal cells to examine the receptor and postreceptor events mediating the inhibitory effects of somatostatin on acid secretion. Somatostatin-14 (S14) and somatostatin-28 (S28) dose dependently inhibited parietal cells stimulated by secretagogues that activate both the adenylate cyclase/cyclic adenosine monophosphate and the inositol phospholipid/protein kinase C cascades. The inhibitory action was mediated via a specific cell surface receptor that consists of a single subunit protein (molecular weight 99,000 d). This receptor recognized S14 and S28 equally well. Somatostatin inhibited parietal cell activity via mechanisms that are both dependent on and independent of a pertussis toxin-sensitive inhibitory guanine nucleotide binding protein.en_US
dc.format.extent543678 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleCellular mechanisms of somatostatin action in the guten_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMedicine (General)en_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Internal Medicine, The University of Michigan Medical Center, Ann Arbor, MI, USA; Third Department of Internal Medicine, Kobe University School of Medicine, Kobe, Japan.en_US
dc.contributor.affiliationumThird Department of Internal Medicine, Kobe University School of Medicine, Kobe, Japan; Department of Internal Medicine, The University of Michigan Medical Center, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumThird Department of Internal Medicine, Kobe University School of Medicine, Kobe, Japan; Department of Internal Medicine, The University of Michigan Medical Center, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumThird Department of Internal Medicine, Kobe University School of Medicine, Kobe, Japan; Department of Internal Medicine, The University of Michigan Medical Center, Ann Arbor, MI, USAen_US
dc.identifier.pmid1976208en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/28402/1/0000177.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0026-0495(90)90231-Zen_US
dc.identifier.sourceMetabolismen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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