Mass spectrometric charting of bovine posterior/intermediate pituitary peptides.

Feistner, Gottfried J.; Højrup, Peter; Evans, Christopher J.; Barofsky, Douglas F.; Faull, Kym F.; Roepstorff, Peter

doi:10.1073/pnas.86.16.6013

Cited by 28 publications

(13 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The neuropeptide FF͞SF precursor requires cleavage at an Ala-Phe site to produce neuropeptide FF and at a Trp-Ser site to produce neuropeptide SF (37). A previous study characterizing peptides in bovine pituitary using MS detected a number of nonbasic cleavage products of POMC, provasopressin, and other neuropeptide precursors (38). However, that study relied primarily on the molecular mass (and not MS͞MS analysis, as done in the present study) so the identification of many of the fragments was only tentative.…”

Section: Discussionmentioning

confidence: 57%

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Fei

Lin

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

131

157

View full text Add to dashboard Cite

Cpe fat ͞Cpe fat mice have a naturally occurring point mutation within the carboxypeptidase E gene that inactivates this enzyme, leading to an accumulation of many neuroendocrine peptides containing C-terminal basic residues. These processing intermediates can be readily purified on an anhydrotrypsin affinity resin. Using MS to obtain molecular mass and partial sequence information, more than 100 peptides have been identified. These peptides represent fragments of 16 known secretory pathway proteins, including proenkephalin, proopiomelanocortin, protachykinins A and B, chromogranin A and B, and secretogranin II. Many of the identified peptides represent previously uncharacterized fragments of the precursors. For example, 12 of the 13 chromogranin B-derived peptides found in the present study have not been previously reported. Of these 13 chromogranin B-derived peptides, only five contain consensus cleavage sites for prohormone convertases at both the C and N termini. Two distinct chromogranin B-derived peptides result from cleavage at Trp-Trp bonds, a site not typically associated with neuropeptide processing. An RIA was used to confirm that one of these peptides, designated WE-15, exists in wild-type mouse brain, thus validating the approach to identify peptides in Cpe fat ͞Cpe fat mice. These ''orphan'' peptides are candidate ligands for orphan G protein-coupled receptors. In addition, the general technique of using affinity chromatography to isolate endogenous substrates from a mutant organism lacking an enzyme should be applicable to a wide range of enzymesubstrate systems.peptide processing ͉ carboxypeptidase E ͉ carboxypeptidase D ͉ chromogranin ͉ secretogranin

show abstract

Section: Discussionmentioning

confidence: 57%

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Fei

Lin

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

131

157

View full text Add to dashboard Cite

show abstract

“…We have, indeed, previously been able to tentatively identify many pituitary neuropeptides in this way, including bovine JP(4-24) and CPP(22-39), which had not been anticipated. 1 The early charting experiments only screened for products from precursors that were known to be present in a given tissue. Meanwhile, software is available to screen large databases (Swiss, PIR, Genpept, etc.…”

Section: General Requirements For Ms Chartingmentioning

confidence: 99%

Special feature: Perspective. Mass spectrometric peptide and protein charting

et al. 1995

View full text Add to dashboard Cite

Six years after coining the term "mass spectrometric (MS) peptide chartingÏ for the component analysis of peptide mixtures in a whole tissue, body Ñuid, or an extract thereof, we o †er our current perspective of this Ðeld. Matrixassisted laser desorption/ionization and electrospray ionization have replaced plasma desorption and fast atom bombardment as ionization methods of choice. At the same time, the upper mass range has been extended to now include most peptides and proteins of interest to research on cell-cell communication. In addition to qualitative aspects, quantitative applications of MS charting have become important. In combination with new database search algorithms, on-line liquid chromatography-tandem mass spectrometry promises greater dividends from MS charting than are achievable with molecular mass matching alone. We discuss what is and is not yet possible, and consider foreseeable means for overcoming current limitations. Our intent is to encourage researchers in the biological and medical sciences to take advantage of this powerful methodology in their various Ðelds of endeavor.

show abstract

“…3 and references therein) employed in molecular biological research to detect genes that show altered expression during development or after application of a physiological stimulus. MS offers unique opportunities for the qualitative and quantitative analysis of a peptide mixture (4) and has been used to tentatively detect previously identified peptides in neuroendocrine tissue (5)(6)(7). Furthermore, MS can reveal the presence of unpredicted components (i.e., analytes with masses that do not correspond to those of previously described peptides; refs.…”

mentioning

confidence: 99%

Pattern changes of pituitary peptides in rat after salt-loading as detected by means of direct, semiquantitative mass spectrometric profiling

Jiménez

Dreisewerd

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

We have established a differential peptide display method, based on a mass spectrometric technique, to detect peptides that show semiquantitative changes in the neurointermediate lobe (NIL) of individual rats subjected to salt-loading. We employed matrix-assisted laser desorption͞ ionization mass spectrometry, using a single-reference peptide in combination with careful scanning of the whole crystal rim of the matrix-analyte preparation, to detect in a semiquantitative manner the molecular ions present in the unfractionated NIL homogenate. Comparison of the mass spectra generated from NIL homogenates of salt-loaded and control rats revealed a selective and significant decrease in the intensities of several molecular ion species of the NIL homogenates from salt-loaded rats. These ion species, which have masses that correspond to the masses of oxytocin, vasopressin, neurophysins, and an unidentified putative peptide, were subsequently chemically characterized. We confirmed that the decreased molecular ion species are peptides derived exclusively from propressophysin and prooxyphysin (i.e., oxytocin, vasopressin, and various neurophysins). The putative peptide is carboxyl-terminal glycopeptide. The carbohydrate moiety of the latter peptide was determined by electrospray tandem MS as bisected biantennary Hex 3 HexNAc 5 Fuc. This posttranslational modification accounts for the mass difference between the predicted mass of the peptide based on cDNA studies and the measured mass of the mature peptide.For cell-to-cell signaling, neurons commonly employ multiple peptides that are derived from one precursor or various precursors. Because neuronal input may control the expression of peptide genes as well as the processing and release of mature peptides, changes in neuronal input may lead to alterations of the cellular pattern of bioactive peptides, resulting in adjustments of physiological processes and behavior (1, 2). To characterize the changes in peptide patterns, a method is needed that can detect the cellular profile of peptides as well as the changes in the relative levels of individual peptides. We propose to call such a method a ''differential peptide display method,'' in analogy to similar methods (e.g., the differential display polymerase chain reaction; see ref. 3 and references therein) employed in molecular biological research to detect genes that show altered expression during development or after application of a physiological stimulus. MS offers unique opportunities for the qualitative and quantitative analysis of a peptide mixture (4) and has been used to tentatively detect previously identified peptides in neuroendocrine tissue (5-7). Furthermore, MS can reveal the presence of unpredicted components (i.e., analytes with masses that do not correspond to those of previously described peptides; refs. 5 and 7). Finally, tandem MS can provide amino acid sequence information for predicted as well as novel peptides (8). Among the several soft-ionization MS techniques available, matrix-assisted laser des...

show abstract

Mass spectrometric charting of bovine posterior/intermediate pituitary peptides.

Cited by 28 publications

References 40 publications

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Special feature: Perspective. Mass spectrometric peptide and protein charting

Pattern changes of pituitary peptides in rat after salt-loading as detected by means of direct, semiquantitative mass spectrometric profiling

Contact Info

Product

Resources

About

Mass spectrometric charting of bovine posterior/intermediate pituitary peptides.

Cited by 28 publications

References 40 publications

Identification of peptides from brain and pituitary of Cpe fat /Cpe fat mice

Identification of peptides from brain and pituitary of Cpe fat /Cpe fat mice

Special feature: Perspective. Mass spectrometric peptide and protein charting

Pattern changes of pituitary peptides in rat after salt-loading as detected by means of direct, semiquantitative mass spectrometric profiling

Contact Info

Product

Resources

About

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice