Reiner Fischer-Colbrie

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Secretogranin II (chromogranin C), originally described as tyrosine sulfated protein of the anterior pituitary, is present in large dense core vesicles of several endocrine cells and neurons. We raised antisera in rabbits to conjugates of two synthetic peptides (bovine secretogranin 133-151 and rat secretogranin 154-186) flanked in the primary structure of(More)
The chromogranins comprise a class of acidic proteins that are secreted from large dense core vesicles and expressed in neuronal and endocrine tissues. We describe here the molecular characterization of NESP55 (neuroendocrine secretory protein of Mr 55,000), a novel member of the chromogranins. Several NESP55 cDNA clones were isolated from bovine chromaffin(More)
Secretogranin II is an acidic secretory protein in large dense core vesicles of endocrine, neuroendocrine and neuronal tissues. It comprises, together with chromogranins A and B, the class of proteins collectively called chromogranins. In this review the physico-chemical properties, genomic organization, tissue distribution, synthesis regulation, ontogeny(More)
The chromogranins (chromogranin A and chromogranin B), secretogranins (secretogranin II and secretogranin III), and additional related proteins (7B2, NESP55, proSAAS, and VGF) that together comprise the granin family subserve essential roles in the regulated secretory pathway that is responsible for controlled delivery of peptides, hormones,(More)
Genomic imprinting results in parent-of-origin-dependent monoallelic expression of selected genes. Although their importance in development and physiology is recognized, few imprinted genes have been investigated for their effects on brain function. Gnas is a complex imprinted locus whose gene products are involved in early postnatal adaptations and(More)
Antisera against bovine chromogranin A, B, and C were used to identify these proteins in human tissues by one- and two-dimensional immunoblotting and by immunohistochemistry. Human chromaffin granules contain all three chromogranins. Their molecular weight differs slightly from the bovine proteins. Chromogranin B and to a lesser degree chromogranin A are(More)
The distribution of secretoneurin, a peptide derived from its precursor secretogranin II by proteolytic processing, was studied in the central nervous system of the rat by immunocytochemistry and radioimmunoassay and compared to the distribution of secretogranin II messenger RNA by using in situ hybridization. With a specific antiserum a distinct staining(More)
We have analyzed the properties and subcellular localization of synaptophysin (protein p38) in bovine adrenal medulla. In one-dimensional immunoblotting the adrenal antigen appears identical to synaptophysin of rat synaptic vesicles. In two-dimensional immunoblotting it migrates as a heterogeneous band varying in pI from 4.5 to 5.8. Subcellular(More)