Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues

R. Kirchmair, B. Leitner, R. Fischer-Colbrie, J. Marksteiner, R. Hogue-Angeletti, H. Winkler

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

We have established a radioimmunoassay for GE-25, a peptide present in the C-terminal end of the primary amino acid sequence of chromogranin A where it is flanked by typical proteolytic cleavage sites. Gel-filtration HPLC was used to characterize the molecular sizes of the immunoreactive molecules. The antiserum recognized not only the free peptide but also larger precursors including the proprotein chromogranin A. The tissues with the highest levels of GE-25 immunoreactivity were in decreasing order: the adrenal medulla, the three lobes of the pituitary gland, intestinal mucosa, pancreas and various brain regions. In adrenal medulla and parathyroid gland most of the immunoreactivity was found to be present as intact chromogranin A and some intermediate-sized peptides, without significant amounts of the free peptide. In anterior pituitary, and even more so in intestine, a shift to smaller peptides was seen. In the posterior and intermediate pituitary and in pancreas the predominant immunoreactive material was apparently represented by the free peptide GE-25. In reverse-phase chromatography this peptide eluted exactly like the synthetic standard, which allows a tentative identification as GE-25. In brain tissue the processing of chromogranin A was intermediate, with significant amounts of immunoreactivity corresponding to GE-25 as well as precursor proteins being present. We suggest that in those organs (endocrine pancreas, intermediate and posterior pituitary) where the major hormones are proteolytically processed there is also a concomitant proteolysis of further susceptible peptides. Since GE-25 is apparently formed in vivo and is well conserved between species it seems a good candidate for having specific physiological functions.

Original languageEnglish (US)
Pages (from-to)331-336
Number of pages6
JournalBiochemical Journal
Volume310
Issue number1
StatePublished - 1995
Externally publishedYes

Fingerprint

Chromogranin A
Tissue
Peptides
Adrenal Medulla
Pancreas
Brain
Posterior Pituitary Hormones
Parathyroid Glands
Proteolysis
Protein Precursors
Pituitary Gland
Reverse-Phase Chromatography
Intestinal Mucosa
Adrenal Glands
Islets of Langerhans
Intestines
Radioimmunoassay
Gel Chromatography
Chromatography
chromogranin A (367-391)

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kirchmair, R., Leitner, B., Fischer-Colbrie, R., Marksteiner, J., Hogue-Angeletti, R., & Winkler, H. (1995). Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues. Biochemical Journal, 310(1), 331-336.

Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues. / Kirchmair, R.; Leitner, B.; Fischer-Colbrie, R.; Marksteiner, J.; Hogue-Angeletti, R.; Winkler, H.

In: Biochemical Journal, Vol. 310, No. 1, 1995, p. 331-336.

Research output: Contribution to journalArticle

Kirchmair, R, Leitner, B, Fischer-Colbrie, R, Marksteiner, J, Hogue-Angeletti, R & Winkler, H 1995, 'Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues', Biochemical Journal, vol. 310, no. 1, pp. 331-336.
Kirchmair R, Leitner B, Fischer-Colbrie R, Marksteiner J, Hogue-Angeletti R, Winkler H. Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues. Biochemical Journal. 1995;310(1):331-336.
Kirchmair, R. ; Leitner, B. ; Fischer-Colbrie, R. ; Marksteiner, J. ; Hogue-Angeletti, R. ; Winkler, H. / Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues. In: Biochemical Journal. 1995 ; Vol. 310, No. 1. pp. 331-336.
@article{755037160d914055bb6d24d41912ebb7,
title = "Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues",
abstract = "We have established a radioimmunoassay for GE-25, a peptide present in the C-terminal end of the primary amino acid sequence of chromogranin A where it is flanked by typical proteolytic cleavage sites. Gel-filtration HPLC was used to characterize the molecular sizes of the immunoreactive molecules. The antiserum recognized not only the free peptide but also larger precursors including the proprotein chromogranin A. The tissues with the highest levels of GE-25 immunoreactivity were in decreasing order: the adrenal medulla, the three lobes of the pituitary gland, intestinal mucosa, pancreas and various brain regions. In adrenal medulla and parathyroid gland most of the immunoreactivity was found to be present as intact chromogranin A and some intermediate-sized peptides, without significant amounts of the free peptide. In anterior pituitary, and even more so in intestine, a shift to smaller peptides was seen. In the posterior and intermediate pituitary and in pancreas the predominant immunoreactive material was apparently represented by the free peptide GE-25. In reverse-phase chromatography this peptide eluted exactly like the synthetic standard, which allows a tentative identification as GE-25. In brain tissue the processing of chromogranin A was intermediate, with significant amounts of immunoreactivity corresponding to GE-25 as well as precursor proteins being present. We suggest that in those organs (endocrine pancreas, intermediate and posterior pituitary) where the major hormones are proteolytically processed there is also a concomitant proteolysis of further susceptible peptides. Since GE-25 is apparently formed in vivo and is well conserved between species it seems a good candidate for having specific physiological functions.",
author = "R. Kirchmair and B. Leitner and R. Fischer-Colbrie and J. Marksteiner and R. Hogue-Angeletti and H. Winkler",
year = "1995",
language = "English (US)",
volume = "310",
pages = "331--336",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

TY - JOUR

T1 - Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues

AU - Kirchmair, R.

AU - Leitner, B.

AU - Fischer-Colbrie, R.

AU - Marksteiner, J.

AU - Hogue-Angeletti, R.

AU - Winkler, H.

PY - 1995

Y1 - 1995

N2 - We have established a radioimmunoassay for GE-25, a peptide present in the C-terminal end of the primary amino acid sequence of chromogranin A where it is flanked by typical proteolytic cleavage sites. Gel-filtration HPLC was used to characterize the molecular sizes of the immunoreactive molecules. The antiserum recognized not only the free peptide but also larger precursors including the proprotein chromogranin A. The tissues with the highest levels of GE-25 immunoreactivity were in decreasing order: the adrenal medulla, the three lobes of the pituitary gland, intestinal mucosa, pancreas and various brain regions. In adrenal medulla and parathyroid gland most of the immunoreactivity was found to be present as intact chromogranin A and some intermediate-sized peptides, without significant amounts of the free peptide. In anterior pituitary, and even more so in intestine, a shift to smaller peptides was seen. In the posterior and intermediate pituitary and in pancreas the predominant immunoreactive material was apparently represented by the free peptide GE-25. In reverse-phase chromatography this peptide eluted exactly like the synthetic standard, which allows a tentative identification as GE-25. In brain tissue the processing of chromogranin A was intermediate, with significant amounts of immunoreactivity corresponding to GE-25 as well as precursor proteins being present. We suggest that in those organs (endocrine pancreas, intermediate and posterior pituitary) where the major hormones are proteolytically processed there is also a concomitant proteolysis of further susceptible peptides. Since GE-25 is apparently formed in vivo and is well conserved between species it seems a good candidate for having specific physiological functions.

AB - We have established a radioimmunoassay for GE-25, a peptide present in the C-terminal end of the primary amino acid sequence of chromogranin A where it is flanked by typical proteolytic cleavage sites. Gel-filtration HPLC was used to characterize the molecular sizes of the immunoreactive molecules. The antiserum recognized not only the free peptide but also larger precursors including the proprotein chromogranin A. The tissues with the highest levels of GE-25 immunoreactivity were in decreasing order: the adrenal medulla, the three lobes of the pituitary gland, intestinal mucosa, pancreas and various brain regions. In adrenal medulla and parathyroid gland most of the immunoreactivity was found to be present as intact chromogranin A and some intermediate-sized peptides, without significant amounts of the free peptide. In anterior pituitary, and even more so in intestine, a shift to smaller peptides was seen. In the posterior and intermediate pituitary and in pancreas the predominant immunoreactive material was apparently represented by the free peptide GE-25. In reverse-phase chromatography this peptide eluted exactly like the synthetic standard, which allows a tentative identification as GE-25. In brain tissue the processing of chromogranin A was intermediate, with significant amounts of immunoreactivity corresponding to GE-25 as well as precursor proteins being present. We suggest that in those organs (endocrine pancreas, intermediate and posterior pituitary) where the major hormones are proteolytically processed there is also a concomitant proteolysis of further susceptible peptides. Since GE-25 is apparently formed in vivo and is well conserved between species it seems a good candidate for having specific physiological functions.

UR - http://www.scopus.com/inward/record.url?scp=0029162316&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029162316&partnerID=8YFLogxK

M3 - Article

C2 - 7646465

AN - SCOPUS:0029162316

VL - 310

SP - 331

EP - 336

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -