Proenkephalin A and proopiomelanocortin peptides in human cerebrospinal fluid

Danxia Liu, George W. Wood, Dominic M. Desiderio

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Precursors to β-endorphin (BE) and methionine enkephalin (ME), and proteolytic enzymes that cleave those BE and ME precursors to BE and ME, were determined in several milliliters of human cerebrospinal fluid. Endogenous peptides were purified by reversed-phase high-performance liquid chromatography (HPLC), and were detected with radioreceptor assay (RRA), radioimmunoassay, and mass spectrometry (MS). Total opioid receptor activity measurements and the profile of HPLC-receptor activity of human CSF samples were both used to monitor neuropeptide metabolism. MS data linked the molecular ion of ME to a unique fragment ion. A later-eluting fraction (84 min) in a 90-min HPLC gradient appeared in all HPLC-RRA profiles, contained opioid receptor activity that discplaced [3H]etorphine, and the quantitative and qualitative patterns of opioid receptor activity in those profiles both changed within the few minutes that elapsed between acquiring the first and second cerebrospinal fluid samples. That 84-min fraction contained precursors to opioid peptides and was fractionated further with a more shallow 120-min HPLC gradient into three sections that displayed δ-opioid receptor-preferring activity, using [3H]ME as ligand. These three sections were hydrolyzed separately with human cerebrospinal fluid as the source for endogenous neuropeptides to yield products that correlated to immunoreactive BE in section I and immunoreactive ME in section III.

Original languageEnglish (US)
Pages (from-to)235-252
Number of pages18
JournalJournal of Chromatography B: Biomedical Sciences and Applications
Volume530
Issue numberC
DOIs
StatePublished - 1990
Externally publishedYes

Fingerprint

Cerebrospinal fluid
Pro-Opiomelanocortin
Methionine Enkephalin
High performance liquid chromatography
Cerebrospinal Fluid
Opioid Receptors
High Pressure Liquid Chromatography
Peptides
Radioligand Assay
Neuropeptides
Mass spectrometry
Assays
Mass Spectrometry
Etorphine
Ions
Endorphins
Opioid Peptides
Reverse-Phase Chromatography
Metabolism
Human Activities

ASJC Scopus subject areas

  • Chemistry(all)
  • Clinical Biochemistry
  • Molecular Medicine

Cite this

Proenkephalin A and proopiomelanocortin peptides in human cerebrospinal fluid. / Liu, Danxia; Wood, George W.; Desiderio, Dominic M.

In: Journal of Chromatography B: Biomedical Sciences and Applications, Vol. 530, No. C, 1990, p. 235-252.

Research output: Contribution to journalArticle

Liu, Danxia ; Wood, George W. ; Desiderio, Dominic M. / Proenkephalin A and proopiomelanocortin peptides in human cerebrospinal fluid. In: Journal of Chromatography B: Biomedical Sciences and Applications. 1990 ; Vol. 530, No. C. pp. 235-252.
@article{c1b547648d3641aeb456e6c1579b1a70,
title = "Proenkephalin A and proopiomelanocortin peptides in human cerebrospinal fluid",
abstract = "Precursors to β-endorphin (BE) and methionine enkephalin (ME), and proteolytic enzymes that cleave those BE and ME precursors to BE and ME, were determined in several milliliters of human cerebrospinal fluid. Endogenous peptides were purified by reversed-phase high-performance liquid chromatography (HPLC), and were detected with radioreceptor assay (RRA), radioimmunoassay, and mass spectrometry (MS). Total opioid receptor activity measurements and the profile of HPLC-receptor activity of human CSF samples were both used to monitor neuropeptide metabolism. MS data linked the molecular ion of ME to a unique fragment ion. A later-eluting fraction (84 min) in a 90-min HPLC gradient appeared in all HPLC-RRA profiles, contained opioid receptor activity that discplaced [3H]etorphine, and the quantitative and qualitative patterns of opioid receptor activity in those profiles both changed within the few minutes that elapsed between acquiring the first and second cerebrospinal fluid samples. That 84-min fraction contained precursors to opioid peptides and was fractionated further with a more shallow 120-min HPLC gradient into three sections that displayed δ-opioid receptor-preferring activity, using [3H]ME as ligand. These three sections were hydrolyzed separately with human cerebrospinal fluid as the source for endogenous neuropeptides to yield products that correlated to immunoreactive BE in section I and immunoreactive ME in section III.",
author = "Danxia Liu and Wood, {George W.} and Desiderio, {Dominic M.}",
year = "1990",
doi = "10.1016/S0378-4347(00)82328-2",
language = "English (US)",
volume = "530",
pages = "235--252",
journal = "Journal of Chromatography B: Biomedical Sciences and Applications",
issn = "0378-4347",
publisher = "Elsevier BV",
number = "C",

}

TY - JOUR

T1 - Proenkephalin A and proopiomelanocortin peptides in human cerebrospinal fluid

AU - Liu, Danxia

AU - Wood, George W.

AU - Desiderio, Dominic M.

PY - 1990

Y1 - 1990

N2 - Precursors to β-endorphin (BE) and methionine enkephalin (ME), and proteolytic enzymes that cleave those BE and ME precursors to BE and ME, were determined in several milliliters of human cerebrospinal fluid. Endogenous peptides were purified by reversed-phase high-performance liquid chromatography (HPLC), and were detected with radioreceptor assay (RRA), radioimmunoassay, and mass spectrometry (MS). Total opioid receptor activity measurements and the profile of HPLC-receptor activity of human CSF samples were both used to monitor neuropeptide metabolism. MS data linked the molecular ion of ME to a unique fragment ion. A later-eluting fraction (84 min) in a 90-min HPLC gradient appeared in all HPLC-RRA profiles, contained opioid receptor activity that discplaced [3H]etorphine, and the quantitative and qualitative patterns of opioid receptor activity in those profiles both changed within the few minutes that elapsed between acquiring the first and second cerebrospinal fluid samples. That 84-min fraction contained precursors to opioid peptides and was fractionated further with a more shallow 120-min HPLC gradient into three sections that displayed δ-opioid receptor-preferring activity, using [3H]ME as ligand. These three sections were hydrolyzed separately with human cerebrospinal fluid as the source for endogenous neuropeptides to yield products that correlated to immunoreactive BE in section I and immunoreactive ME in section III.

AB - Precursors to β-endorphin (BE) and methionine enkephalin (ME), and proteolytic enzymes that cleave those BE and ME precursors to BE and ME, were determined in several milliliters of human cerebrospinal fluid. Endogenous peptides were purified by reversed-phase high-performance liquid chromatography (HPLC), and were detected with radioreceptor assay (RRA), radioimmunoassay, and mass spectrometry (MS). Total opioid receptor activity measurements and the profile of HPLC-receptor activity of human CSF samples were both used to monitor neuropeptide metabolism. MS data linked the molecular ion of ME to a unique fragment ion. A later-eluting fraction (84 min) in a 90-min HPLC gradient appeared in all HPLC-RRA profiles, contained opioid receptor activity that discplaced [3H]etorphine, and the quantitative and qualitative patterns of opioid receptor activity in those profiles both changed within the few minutes that elapsed between acquiring the first and second cerebrospinal fluid samples. That 84-min fraction contained precursors to opioid peptides and was fractionated further with a more shallow 120-min HPLC gradient into three sections that displayed δ-opioid receptor-preferring activity, using [3H]ME as ligand. These three sections were hydrolyzed separately with human cerebrospinal fluid as the source for endogenous neuropeptides to yield products that correlated to immunoreactive BE in section I and immunoreactive ME in section III.

UR - http://www.scopus.com/inward/record.url?scp=0025179208&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025179208&partnerID=8YFLogxK

U2 - 10.1016/S0378-4347(00)82328-2

DO - 10.1016/S0378-4347(00)82328-2

M3 - Article

C2 - 1964161

AN - SCOPUS:0025179208

VL - 530

SP - 235

EP - 252

JO - Journal of Chromatography B: Biomedical Sciences and Applications

JF - Journal of Chromatography B: Biomedical Sciences and Applications

SN - 0378-4347

IS - C

ER -