Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2004-1-26
pubmed:abstractText
Granin-family proteins, including chromogranin A (CgA) and secretogranin III (SgIII), are transported to secretory granules (SGs) in neuroendocrine cells. We previously showed that SgIII binds strongly to CgA in an intragranular milieu and targets CgA to SGs in pituitary and pancreatic endocrine cells. In this study, we demonstrated that with a sucrose density gradient of rat insulinoma-derived INS-1 cell homogenates, SgIII was localized to the SG fraction and was fractionated to the SG membrane (SGM) despite lacking the transmembrane region. With depletion of cholesterol from the SGM using methyl-beta-cyclodextrin, SgIII was impaired to bind to the SGM. Both SgIII and CgA were solubilized from the SGM by Triton X-100 in contrast to the Triton X-100 insolubility of carboxypeptidase E. SgIII and carboxypeptidase E strongly bound to the SGM-type liposome in intragranular conditions, but CgA did not. Instead, CgA bound to the SGM-type liposome only in the presence of SgIII. Immunocytochemical and pulse-chase experiments revealed that SgIII deleting the N-terminal lipid-binding region missorted to the constitutive pathway in mouse corticotroph-derived AtT-20 cells. Thus, we suggest that SgIII directly binds to cholesterol components of the SGM and targets CgA to SGs in pituitary and pancreatic endocrine cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/8-Bromo Cyclic Adenosine..., http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidase H, http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, http://linkedlifedata.com/resource/pubmed/chemical/Chromogranin A, http://linkedlifedata.com/resource/pubmed/chemical/Chromogranins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclodextrins, http://linkedlifedata.com/resource/pubmed/chemical/Detergents, http://linkedlifedata.com/resource/pubmed/chemical/Lipids, http://linkedlifedata.com/resource/pubmed/chemical/Liposomes, http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Sucrose, http://linkedlifedata.com/resource/pubmed/chemical/beta-Cyclodextrins, http://linkedlifedata.com/resource/pubmed/chemical/chromogranin A, mouse, http://linkedlifedata.com/resource/pubmed/chemical/chromogranin A, rat, http://linkedlifedata.com/resource/pubmed/chemical/methyl-beta-cyclodextrin
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3627-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:14597614-8-Bromo Cyclic Adenosine Monophosphate, pubmed-meshheading:14597614-Animals, pubmed-meshheading:14597614-Carboxypeptidase H, pubmed-meshheading:14597614-Cell Line, pubmed-meshheading:14597614-Centrifugation, Density Gradient, pubmed-meshheading:14597614-Cholesterol, pubmed-meshheading:14597614-Chromogranin A, pubmed-meshheading:14597614-Chromogranins, pubmed-meshheading:14597614-Cyclodextrins, pubmed-meshheading:14597614-Detergents, pubmed-meshheading:14597614-Endocrine System, pubmed-meshheading:14597614-Immunohistochemistry, pubmed-meshheading:14597614-Lipids, pubmed-meshheading:14597614-Liposomes, pubmed-meshheading:14597614-Mice, pubmed-meshheading:14597614-Microscopy, Confocal, pubmed-meshheading:14597614-Octoxynol, pubmed-meshheading:14597614-Protein Binding, pubmed-meshheading:14597614-Protein Structure, Tertiary, pubmed-meshheading:14597614-Proteins, pubmed-meshheading:14597614-RNA, Messenger, pubmed-meshheading:14597614-Rats, pubmed-meshheading:14597614-Secretory Vesicles, pubmed-meshheading:14597614-Subcellular Fractions, pubmed-meshheading:14597614-Sucrose, pubmed-meshheading:14597614-Xenopus, pubmed-meshheading:14597614-beta-Cyclodextrins
pubmed:year
2004
pubmed:articleTitle
Secretogranin III binds to cholesterol in the secretory granule membrane as an adapter for chromogranin A.
pubmed:affiliation
Department of Molecular Medicine, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi 371-8512, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't