Abstract
Chromogranin A and secretogranin II are members of the so-called chromogranins, the acidic proteins stored in neuroendocrine large dense-core vesicles. We characterized chromogranin A and secretogranin II immunoreactivities in cerebrospinal fluid by radioimmunoassays using synthetic peptides derived from these components (GE-25 for chromogranin A and secretoneurin for secretogranin II). In lumbar cerebrospinal fluid, high levels (more than 1000 fmol/ml) of these two components were found, whereas in ventricular cerebrospinal fluid the secretoneurin levels were relatively low. The cerebrospinal fluid/serum ratio for secretoneurin was close to 170. High-performance liquid chromatography revealed that in both cerebrospinal fluid and extracts from human brain secretoneurin was the predominant immunoreactive component. In cerebrospinal fluid chromogranin A immunoreactivity was present as intermediate-sized peptides with little intact chromogranin A and free GE-25 peptide. In human brain samples smaller peptides including GE-25 were more predominant. Analogous findings for secretoneurin and chromogranin A were obtained for bovine brain samples. We can conclude that chromogranins are present in cerebrospinal fluid in concentrations much higher than those of classical neuropeptides also stored in large dense-core vesicles. Therefore, their degree of proteolytic processing can be analysed with small samples of cerebrospinal fluid. A possible disturbance of proteolytic processing in large dense-core vesicles in various pathological conditions can now be discovered.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1179-1187 |
| Number of pages | 9 |
| Journal | Neuroscience |
| Volume | 63 |
| Issue number | 4 |
| DOIs | |
| State | Published - 1994 |
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ASJC Scopus subject areas
- Neuroscience(all)
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Molecular characterization of immunoreactivities of peptides derived from chromogranin a (GE-25) and from secretogranin II (secretoneurin) in human and bovine cerebrospinal fluid. / Kirchmair, R.; Benzer, A.; Troger, J.; Miller, C.; Marksteiner, J.; Saria, A.; Gasser, R. W.; Hogue-Angeletti, R.; Fischer-Colbrie, R.; Winkler, H.
In: Neuroscience, Vol. 63, No. 4, 1994, p. 1179-1187.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Molecular characterization of immunoreactivities of peptides derived from chromogranin a (GE-25) and from secretogranin II (secretoneurin) in human and bovine cerebrospinal fluid
AU - Kirchmair, R.
AU - Benzer, A.
AU - Troger, J.
AU - Miller, C.
AU - Marksteiner, J.
AU - Saria, A.
AU - Gasser, R. W.
AU - Hogue-Angeletti, R.
AU - Fischer-Colbrie, R.
AU - Winkler, H.
PY - 1994
Y1 - 1994
N2 - Chromogranin A and secretogranin II are members of the so-called chromogranins, the acidic proteins stored in neuroendocrine large dense-core vesicles. We characterized chromogranin A and secretogranin II immunoreactivities in cerebrospinal fluid by radioimmunoassays using synthetic peptides derived from these components (GE-25 for chromogranin A and secretoneurin for secretogranin II). In lumbar cerebrospinal fluid, high levels (more than 1000 fmol/ml) of these two components were found, whereas in ventricular cerebrospinal fluid the secretoneurin levels were relatively low. The cerebrospinal fluid/serum ratio for secretoneurin was close to 170. High-performance liquid chromatography revealed that in both cerebrospinal fluid and extracts from human brain secretoneurin was the predominant immunoreactive component. In cerebrospinal fluid chromogranin A immunoreactivity was present as intermediate-sized peptides with little intact chromogranin A and free GE-25 peptide. In human brain samples smaller peptides including GE-25 were more predominant. Analogous findings for secretoneurin and chromogranin A were obtained for bovine brain samples. We can conclude that chromogranins are present in cerebrospinal fluid in concentrations much higher than those of classical neuropeptides also stored in large dense-core vesicles. Therefore, their degree of proteolytic processing can be analysed with small samples of cerebrospinal fluid. A possible disturbance of proteolytic processing in large dense-core vesicles in various pathological conditions can now be discovered.
AB - Chromogranin A and secretogranin II are members of the so-called chromogranins, the acidic proteins stored in neuroendocrine large dense-core vesicles. We characterized chromogranin A and secretogranin II immunoreactivities in cerebrospinal fluid by radioimmunoassays using synthetic peptides derived from these components (GE-25 for chromogranin A and secretoneurin for secretogranin II). In lumbar cerebrospinal fluid, high levels (more than 1000 fmol/ml) of these two components were found, whereas in ventricular cerebrospinal fluid the secretoneurin levels were relatively low. The cerebrospinal fluid/serum ratio for secretoneurin was close to 170. High-performance liquid chromatography revealed that in both cerebrospinal fluid and extracts from human brain secretoneurin was the predominant immunoreactive component. In cerebrospinal fluid chromogranin A immunoreactivity was present as intermediate-sized peptides with little intact chromogranin A and free GE-25 peptide. In human brain samples smaller peptides including GE-25 were more predominant. Analogous findings for secretoneurin and chromogranin A were obtained for bovine brain samples. We can conclude that chromogranins are present in cerebrospinal fluid in concentrations much higher than those of classical neuropeptides also stored in large dense-core vesicles. Therefore, their degree of proteolytic processing can be analysed with small samples of cerebrospinal fluid. A possible disturbance of proteolytic processing in large dense-core vesicles in various pathological conditions can now be discovered.
UR - http://www.scopus.com/inward/record.url?scp=0027960435&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027960435&partnerID=8YFLogxK
U2 - 10.1016/0306-4522(94)90582-7
DO - 10.1016/0306-4522(94)90582-7
M3 - Article
C2 - 7535395
AN - SCOPUS:0027960435
VL - 63
SP - 1179
EP - 1187
JO - Neuroscience
JF - Neuroscience
SN - 0306-4522
IS - 4
ER -