Linked Life Data

11680901

Source:http://linkedlifedata.com/resource/pubmed/id/11680901

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-10-29
pubmed:abstractText
In an attempt to identify peptides that may be involved in the obese phenotype observed in CpEfat/CpEfat mice (deficient in Carboxypeptidase E, CpE) samples from fourteen neuroendocrine tissues in wild-type and CpEfat/CpEfat mice were obtained. Peptides were purified from these tissues and potential CpE substrate peptides were enriched using an anhydrotrypsin column that captures peptides with basic C-termini. Bound peptides were subjected to tryptic digestion and followed by liquid chromatography-mass spectrometry analysis. The relative levels of CpEfat/CpEfat versus wild-type peptides were determined by comparison of the ion intensities. Peptide ions elevated in the CpEfat/CpEfat samples were identified by targeted liquid chromatography-tandem mass spectrometry. From those ions, 27 peptides derived from known neuropeptides (including CpE substrates) were identified, together with another 25 peptides from proteins not known to be components of the neuropeptide processing pathway. The known CpE substrates identified included the recently discovered proSAAS, granin-like neuroendocrine peptide precursor that inhibits prohormone processing. The approach demonstrated the feasibility of using an affinity-based method for identifying differences in specific classes of peptides between normal and mutant mice.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1615-9853
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11680901-Amino Acid Sequence, pubmed-meshheading:11680901-Animals, pubmed-meshheading:11680901-Carboxypeptidase H, pubmed-meshheading:11680901-Carboxypeptidases, pubmed-meshheading:11680901-Chromatography, Liquid, pubmed-meshheading:11680901-Mass Spectrometry, pubmed-meshheading:11680901-Mice, pubmed-meshheading:11680901-Mice, Mutant Strains, pubmed-meshheading:11680901-Molecular Sequence Data, pubmed-meshheading:11680901-Neuropeptides, pubmed-meshheading:11680901-Neurosecretory Systems, pubmed-meshheading:11680901-Obesity, pubmed-meshheading:11680901-Protein Precursors, pubmed-meshheading:11680901-Protein Processing, Post-Translational, pubmed-meshheading:11680901-Proteome, pubmed-meshheading:11680901-Substrate Specificity, pubmed-meshheading:11680901-Tissue Distribution
pubmed:year
2001
pubmed:articleTitle
Identification of incompletely processed potential carboxypeptidase E substrates from CpEfat/CpEfat mice.
pubmed:affiliation
Departments of Biochemistry and Genetics, Amgen, Thousand Oaks, CA, USA.
pubmed:publicationType
Journal Article, Comparative Study