Presence and release of SR-17 (chromogranin B(586-602)) in the porcine splenic nerve and its enzymatic degradation by CD26/dipeptidyl peptidase IV
Autor: | Etienne J. Nouwen, Jan Depreitere, Zesheng Wang, Simon Scharpé, E.P. Coen, Werner De Potter, Anne-Marie Lambeir, Christine Durinx |
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Rok vydání: | 2002 |
Předmět: |
medicine.medical_specialty
Physiology Swine Dipeptidyl Peptidase 4 Clinical Biochemistry Molecular Sequence Data Spleen Enzyme-Linked Immunosorbent Assay In Vitro Techniques Biochemistry Axonal Transport Dipeptidyl peptidase Cellular and Molecular Neuroscience Norepinephrine Endocrinology Internal medicine medicine Splenocyte Chromogranins Animals Humans Amino Acid Sequence Phentolamine Antiserum biology Chemistry Chromogranin A Molecular biology Immunohistochemistry Peptide Fragments medicine.anatomical_structure Models Animal Axoplasmic transport biology.protein Adrenal medulla Free nerve ending Chromogranin B |
Zdroj: | Regulatory peptides |
ISSN: | 0167-0115 |
Popis: | Using the pig splenic nerve as a model, we investigated the proteolytic processing of porcine chromogranin B (CgB) during its axonal transport. An ELISA was developed for SR-17 (CgB 586–602 ), a novel CgB-derived peptide, originally found in the adrenal medulla. The results demonstrate that CgB is processed in an early stage during its axonal transport. Immunohistochemical data, based on a rabbit anti-SR-17 antiserum, show that the spleen CgB/SR-17 is exclusively present in the nerve endings. No SR-17 immunoreactivity (IR) was found in splenocytes. We also provide evidence that SR-17 is co-released with noradrenaline (NA) upon electrical stimulation of the splenic nerve. Its release is frequency-dependent and strongly enhanced in the presence of the α-blocking agent phentolamine. In addition, we show that the new CgB-peptide can serve as a substrate for the lymphocyte surface glycoprotein CD26, also known as dipeptidyl peptidase IV (DPP IV), generating a new peptide ER-15 (CgB 588–602 ). |
Databáze: | OpenAIRE |
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