Analysis of proenkephalin A, proopiomelanocortin and protachykinin neuropeptides in human lumbar cerebrospinal fluid by reversed-phase high-performance liquid chromatography, radioimmunoassay and enzymolysis

Harajiri, Shinichiro; Wood, George W.; Desiderio, Dominic M.

doi:10.1016/0378-4347(92)80148-j

Cited by 21 publications

(4 citation statements)

References 25 publications

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“…Rather, most methods infer the presence of a particular peptide from the immunoassay, receptorassay, in situ hybridization, mRNA, or cDNA data; however, the actual amino acid sequence of the peptide is not determined. In cerebrospinal fluid, plasma, etc., it is experimentally difficult to obtain the amino acid sequence of each peptide because of the limited amount of peptide (<fmol) (Harajiri & Desiderio, 1992). Thus, an accurate suffix must be used for the peptide measurement (see above).…”

Section: B Basic Principles Of the Methodsmentioning

confidence: 99%

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Peptide quantification by tandem mass spectrometry

Zhu

Desiderio

1996

Mass Spectrom. Rev.

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Section: B Basic Principles Of the Methodsmentioning

confidence: 99%

“…Other classes of compounds such as cannabinoids (Harvey, 1992), carnitine (Millington & Chace, 1992), and others have also been studied by MSIMS, but this review focuses on peptides.…”

Section: A Objective Of This Reviewmentioning

confidence: 99%

Peptide quantification by tandem mass spectrometry

Zhu

Desiderio

1996

Mass Spectrom. Rev.

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“…15 We have previously used chromatography, radioimmunoassay, radioreceptorassay, and mass spectrometry to study selected neuropeptides, precursors, and enzymes in CSF samples from controls and patients with CNS diseases (especially idiopathic low back pain). [16][17][18][19][20] Many other studies have identified with immunoblotting specific CSF proteins. [21][22][23][24] Improved proteom- ics techniquessespecially mass spectrometry and gel and nongel methodsshave improved the speed, sensitivity, and accuracy of protein identification.…”

Section: Introductionmentioning

confidence: 99%

“…CSF contains a great number of peptides, neuropeptides, enzymes, and proteins that can be readily and accurately monitored in health and disease states − Many other studies have identified with immunoblotting specific CSF proteins. − Improved proteomics techniquesespecially mass spectrometry and gel and nongel methodshave improved the speed, sensitivity, and accuracy of protein identification. More than 500 protein spots on a 2-D gel have been identified in CSF. − Some specific CSF proteins relate to certain CNS disorders .…”

Section: Introductionmentioning

confidence: 99%

Proteomics Analysis of Phosphotyrosyl-Proteins in Human Lumbar Cerebrospinal Fluid

Yuan

Desiderio

2003

J. Proteome Res.

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Cerebrospinal fluid (CSF) is a secretion product of several different central nervous system (CNS) structures, including the choroid plexus in the ventricles. Pathological CNS processes are reflected in the protein composition of CSF. To elucidate the molecular events that occur in the homeostatic and pathological processes of the CNS, the high-throughput characterization of differentially expressed proteins, and of post-translationally modified proteins, is needed for proteomics studies of CSF. Among the post-translational modifications of proteins, phosphorylation is the most common and important mechanism for the reversible regulation of protein function. In this study, CSF phosphotyrosyl (p-Tyr)-proteins were detected with antibodies and were analyzed with proteomics methods. Three different combination methods--1D gel electrophoresis and Western blotting, immunoprecipitation and 2D gel electrophoresis, and 2D gel electrophoresis and Western blotting--were used to detect p-Tyr-proteins in human lumbar CSF samples. Six protein spots, representing four proteins on a 2D Western blot, were identified as p-Tyr-proteins with the 2D gel electrophoresis and Western blotting method. Those four p-Tyr-proteins are kallikrein-6 precursor, complement C4 gamma-chain, gelsolin, and ceruloplasmin precursor. Additionally, four other nonphosphorylated CSF proteins--beta-2-glycoprotein I precursor, fibulin-1 precursor, EGF-containing fibulin-like extracellur matrix protein 1 precursor, and angiotensinogen precursor--were characterized for the first time.

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Mass spectrometric analysis of opioid and tachykinin neuropeptides in non-secreting and ACTH-secreting human pituitary adenomas

Desiderio

Kusmierz

Zhu

et al. 1993

Biol. Mass Spectrom.

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In a study to test the hypothesis that defects in the metabolism of neuropeptides might be a contributing factor to human anterior pituitary tumor formation, the proenkephalin A, proopiomelanocortin (POMC), and tachykinin systems, which produce methionine enkephalin (ME), beta-endorphin (BE), and substance P (SP), respectively, were measured in patients who had a wide variety of pituitary tumors. Mass spectrometry was used to optimize the level of molecular specificity of the ME and BE analytical measurements, and radioimmunoassay was used to measure SP-like immunoreactivity (SP-li). Compared to data obtained from pituitaries from post-mortem controls, the non-secreting tumors contained a significantly lower amount of the POMC neuropeptide, BE. The lower ME level was not significant. However, two adrenocorticotrophic hormone (ACTH)-secreting tumors contained ME, BE, and SP-li amounts that were much higher than both the controls and nonsecreting tumors. These data suggest that a hypometabolism of the POMC precursor may be operating in non-secreting tumors, and that a hypermetabolism of the proenkephalin A, POMC, and tachykinin precursors may be operating in two ACTH-secreting tumors. These data demonstrate that mass spectrometry plays a critical role in the study of human pituitary tumors.

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Analysis of proenkephalin A, proopiomelanocortin and protachykinin neuropeptides in human lumbar cerebrospinal fluid by reversed-phase high-performance liquid chromatography, radioimmunoassay and enzymolysis

Cited by 21 publications

References 25 publications

Peptide quantification by tandem mass spectrometry

Peptide quantification by tandem mass spectrometry

Proteomics Analysis of Phosphotyrosyl-Proteins in Human Lumbar Cerebrospinal Fluid

Mass spectrometric analysis of opioid and tachykinin neuropeptides in non-secreting and ACTH-secreting human pituitary adenomas

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