Cellular Localization of a chromogranin B-like derived peptides
in leeches
Michel
Salzet
Laboratoire de Neuroimmunologie des
Annélides,
Université des Sciences et Technologies de Lille.
59650 Villeneuve d'Ascq, FRANCE.
Keywords:
chromogranin B, leech, Immunocytochemistry, Secretolytin
Abstract
Using immunocytochemistry techniques, we demonstrated specific
immunostaining with antibodies rose against fragment (547-560)
and (614-626) of bovine chromogranin B (CGB) at the level
of brain and the tegument of the leech Theromyzon tessulatum.
The used of these antibodies on leech sections revealed immunopositive
labeling in neurons and glial cells of the central nervous
system (CNS), and epidermal glandular cells of the tegument.
Co-localization between two antibodies rose against different
fragment of bovine CGB have been demonstrated in neurons and
glial cells of leech CNS like in vertebrates. Finally, the
whole of the data showed for the first time the presence in
leeches of CGB like derived peptides.
1.
Introduction
Chromogranins
are acidic proteins which are found throughout neuroendocrine
system [1]. They comprise several defined proteins which have
been named chromogranin A [2, 3], chromogranin B [4] [5]; secretogranin
II [6] [7], 7B2 [8], ProSAAS [9]. These proteins distribution
have been undergone in rat brain in great detail [1, 6, 10-12].
Interestingly, prochromogranin B (CGB) is known to be processed
in several peptides i.e. GAWK, CCB, BAM-1745, OA21, OA8, LE-20,
NL-10, OY-10 presenting several different biological functions
[5]. In addition to their roles as helper proteins in the packaging
of peptides, they may serve as pro-hormones to generate biologically
active peptides such as vasostatin-1 and secretolytin [13, 14].
These molecules derived from CGA and CGB respectively, possess
antimicrobial properties [13, 14]. From the C-terminal part
of CGB, two peptides have been identified in both rat and bovine
endocrine tissue i.e. the peptide 11 (PE11) at position 552-562
[15] and secretolytin at position 614-621 [13]. We have recently
demonstrated that immune cells also contain CGA and CGB [16-18]
like proenkephalin [19]. Moreover, secretolytin is shown to
be released from monocytes in vitro under interleukin 6 stimulation
[20]. In the present study, we demonstrate using the immunocytochemical
technique that chromogranin B derived peptides like a leech
secretolytin are also present in leeches like we also previously
demonstrated for enkelytin, another antimicrobial neuropeptide
derived peptide, the proenkephalin [21-23].
...
...
...
...
REFERENCES:
1. Fahrenkamp, A.G., et al., Immunohistochemical distribution
of chromogranins A and B and secretogranin II in neuroendocrine
tumours of the gastrointestinal tract. Virchows Arch, 1995.
426(4): p. 361-7.
2. Blaschko, H., et al., Secretion of a chromaffin granule protein,
chromogranin, from the adrenal gland after splanchnic stimulation.
Nature, 1967. 215(96): p. 58-9.
3. Blaschko, H., Biochemical studies on chromaffin cells. Naunyn
Schmiedebergs Arch Exp Pathol Pharmakol, 1967. 257(1): p. 143-7.
4. Benjannet, S., et al., Chromogranin B (secretogranin I),
a putative precursor of two novel pituitary peptides through
processing at paired basic residues. FEBS Lett, 1987. 224(1):
p. 142-8.
5. Grandy, D.K., et al., Nucleotide and deduced amino acid sequence
of bovine adrenal medulla chromogranin B (secretogranin I).
Cell Mol Neurobiol, 1992. 12(2): p. 185-92.
6. Schmid, K.W., et al., Chromogranin A, secretogranin II and
vasoactive intestinal peptide in phaeochromocytomas and ganglioneuromas.
Histopathology, 1993. 22(6): p. 527-33.
7. Overdick, B., et al., Presence and distribution of a new
neuropeptide, secretoneurin, in human retina. Peptides, 1996.
17(1): p. 1-4.
8. Day, R., et al., Maintained PC1 and PC2 expression in the
AtT-20 variant cell line 6T3 lacking regulated secretion and
POMC: restored POMC expression and regulated secretion after
cAMP treatment. DNA Cell Biol, 1995. 14(2): p. 175-88.
9. Fricker, L.D., et al., Identification and characterization
of proSAAS, a granin-like neuroendocrine peptide precursor that
inhibits prohormone processing. J Neurosci, 2000. 20(2): p.
639-48.
10. Schmid, K.W., et al., Immunohistochemical localization of
chromogranins A and B and secretogranin II in normal, hyperplastic
and neoplastic prostate. Histopathology, 1994. 24(3): p. 233-9.
11. Schmid, K.W., et al., Immunohistochemical demonstration
of chromogranin A, chromogranin B, and secretogranin II in extra-adrenal
paragangliomas. Mod Pathol, 1994. 7(3): p. 347-53.
12. Schmid, K.W., et al., Immunohistochemical comparison of
chromogranins A and B and secretogranin II with calcitonin and
calcitonin gene-related peptide expression in normal, hyperplastic
and neoplastic C-cells of the human thyroid. Histopathology,
1992. 21(3): p. 225-32.
13. Strub, J.M., et al., Antibacterial activity of secretolytin,
a chromogranin B-derived peptide (614-626), is correlated with
peptide structure. FEBS Lett, 1996. 379(3): p. 273-8.
14. Metz-Boutigue, M.H., et al., Antibacterial peptides are
present in chromaffin cell secretory granules. Cell Mol Neurobiol,
1998. 18(2): p. 249-66.
15. Kroesen, S., et al., Rat brain: distribution of immunoreactivity
of PE-11, a peptide derived from chromogranin B. Eur J Neurosci,
1996. 8(12): p. 2679-89.
16. Salzet, M., Immune cells express endocrine markers. Neuroendocrinol
Lett, 2002. 23(1): p. 8-9.
17. Salzet, M., Neuroimmunology of opioids from invertebrates
to human. Neuroendocrinol Lett, 2001. 22(6): p. 467-74.
18. Salzet, M., Vertebrate innate immunity resembles a mosaic
of invertebrate immune responses. Trends Immunol, 2001. 22(6):
p. 285-8.
19. Tasiemski, A., et al., The presence of antibacterial and
opioid peptides in human plasma during coronary artery bypass
surgery. J Neuroimmunol, 2000. 109(2): p. 228-35.
20. Taseimki et al., 20002
21. Tasiemski, A., et al., Proenkephalin A-derived peptides
in invertebrate innate immune processes. Brain Res Mol Brain
Res, 2000. 76(2): p. 237-52.
22. Salzet, M., Neuroimmunology of opioids from invertebrates
to human. Neuroendocrinol Lett, 2001. 22(6): p. 467-74.
23. Salzet, M. and A. Tasiemski, Involvement of pro-enkephalin-derived
peptides in immunity. Dev Comp Immunol, 2001. 25(3): p. 177-85.
24. Malecha, J., et al., [Evidence of apparent vasopressin and
oxytocin peptides in the brain of the leech Rhynchobdelle Theromyzon
tessulatum (O.F.M.)]. Gen Comp Endocrinol, 1986. 64(1): p. 13-20.
25. Malecha, J., [Osmoregulation in Hirudinea Rhynchobdellida
Theromyzon tessulatum (O.F.M.). Experimental localization of
the secretory zone of a regulation factor of water balance].
Gen Comp Endocrinol, 1983. 49(3): p. 344-51.
26. Salzet, M., et al., Oxytocin-like peptide: a novel epitope
colocalized with the FMRFamide-like peptide in the supernumerary
neurons of the sex segmental ganglia of leeches--morphological
and biochemical characterization; putative anti-diuretic function.
Brain Res, 1993. 601(1-2): p. 173-84.
27. Kimura, N., et al., Immunohistochemical expression of chromogranins
A and B, prohormone convertases 2 and 3, and amidating enzyme
in carcinoid tumors and pancreatic endocrine tumors. Mod Pathol,
2000. 13(2): p. 140-6.
28. Stefano, G.B., B. Salzet, and G.L. Fricchione, Enkelytin
and opioid peptide association in invertebrates and vertebrates:
immune activation and pain. Immunol Today, 1998. 19(6): p. 265-8.
|
