Biomaterial Database

Neuronal markers, peptides and enzymes in nerves and chromaffin cells in the rat adrenal medulla during postnatal development. 1994

H Holgert, and A Dagerlind, and T Hökfelt, and H Lagercrantz

Department of Woman and Child Health (Neonatology and Neuropediatrics), Karolinska Institute, Stockholm, Sweden.

Neuronal markers, peptides and enzymes were analyzed in the rat adrenal medulla during the postnatal period, i.e., when the 'functional' splanchnic innervation is assumed to 'mature'. Nerve fibers were present on day 2 as indicated by neurofilament 10 (NF10)- and growth associated protein 43 (GAP43)-like immunoreactivities (LIs). Acetylcholinesterase (AChE)- and enkephalin (ENK)-immunoreactive (IR) fibers, presumably of preganglionic nature, increased in number and intensity during the postnatal period. In contrast, calcitonin gene-related peptide (CGRP)- and galanin (GAL)-IR fibers were almost fully developed on day 2. Thus, the presumably sensory innervation of the adrenal gland seems to precede the development of the autonomic nerves. The AChE- and ENK-IR fibers may exert a suppressive effect on ENK-, CGRP- and neurotensin (NT)-LIs in chromaffin cells, since the levels of these peptides were high in the early postnatal period and then decreased. On the other hand, GAL-LI in chromaffin cells was low also in young rats, while GAP43-IR cells were observed at all stages. Neuropeptide tyrosine (NPY) was expressed in many chromaffin cells at all stages and its turnover rate seemed to decrease towards the adult stage. The expression of the catecholamine synthezising enzymes changed only marginally during development. These results indicate that the preganglionic fibers, but not the sensory axons, in the splanchnic nerve are involved in the developmental control of expression of some, but not all, peptides in the chromaffin cells and that these changes thus may reflect the maturation of a 'functional' transmission.

UI	MeSH Term	Description	Entries
D007150	Immunohistochemistry	Histochemical localization of immunoreactive substances using labeled antibodies as reagents.	Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D008297	Male		Males
D008562	Membrane Glycoproteins	Glycoproteins found on the membrane or surface of cells.	Cell Surface Glycoproteins,Surface Glycoproteins,Cell Surface Glycoprotein,Membrane Glycoprotein,Surface Glycoprotein,Glycoprotein, Cell Surface,Glycoprotein, Membrane,Glycoprotein, Surface,Glycoproteins, Cell Surface,Glycoproteins, Membrane,Glycoproteins, Surface,Surface Glycoprotein, Cell,Surface Glycoproteins, Cell
D009412	Nerve Fibers	Slender processes of NEURONS, including the AXONS and their glial envelopes (MYELIN SHEATH). Nerve fibers conduct nerve impulses to and from the CENTRAL NERVOUS SYSTEM.	Cerebellar Mossy Fibers,Mossy Fibers, Cerebellar,Cerebellar Mossy Fiber,Mossy Fiber, Cerebellar,Nerve Fiber
D009419	Nerve Tissue Proteins		Proteins, Nerve Tissue,Tissue Proteins, Nerve
D009474	Neurons	The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.	Nerve Cells,Cell, Nerve,Cells, Nerve,Nerve Cell,Neuron
D009478	Neuropeptide Y	A 36-amino acid peptide present in many organs and in many sympathetic noradrenergic neurons. It has vasoconstrictor and natriuretic activity and regulates local blood flow, glandular secretion, and smooth muscle activity. The peptide also stimulates feeding and drinking behavior and influences secretion of pituitary hormones.	Neuropeptide Y-Like Immunoreactive Peptide,Neuropeptide Tyrosine,Neuropeptide Y Like Immunoreactive Peptide,Tyrosine, Neuropeptide
D009479	Neuropeptides	Peptides released by NEURONS as intercellular messengers. Many neuropeptides are also hormones released by non-neuronal cells.	Neuropeptide
D010452	Peptide Biosynthesis	The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules.	Biosynthesis, Peptide
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides