Dipeptide inhibitors of ubiquitin-mediated protein turnover prevent growth factor-induced neurite outgrowth in rat pheochromocytoma PC12 cells. 1992

H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
Department of Biological Chemistry, College of Medicine, University of California, Irvine 92717-1700.

Dipeptide inhibitors of the ubiquitin-dependent proteolysis pathway governed by N-terminal recognition (N-end rule) in reticulocyte lysates significantly suppress NGF- and bFGF-induced neurite outgrowth in rat pheochromocytoma PC12 cells, but do not cause retraction of already formed neurites. Peptides which do not inhibit proteolysis are also without effect on PC12 cell differentiation. Suppression of neurite outgrowth is readily reversible upon removal of the inhibitors. These data demonstrate a requirement for specific protein turnover in the process of neuron-like differentiation in PC12 cells and provide the first demonstration of a physiological role for the N-end rule.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009414 Nerve Growth Factors Factors which enhance the growth potentialities of sensory and sympathetic nerve cells. Neurite Outgrowth Factor,Neurite Outgrowth Factors,Neuronal Growth-Associated Protein,Neuronotrophic Factor,Neurotrophic Factor,Neurotrophic Factors,Neurotrophin,Neurotrophins,Growth-Associated Proteins, Neuronal,Neuronal Growth-Associated Proteins,Neuronotrophic Factors,Neurotrophic Protein,Neurotrophic Proteins,Proteins, Neuronal Growth-Associated,Factor, Neurite Outgrowth,Factor, Neuronotrophic,Factor, Neurotrophic,Factors, Nerve Growth,Factors, Neurite Outgrowth,Factors, Neuronotrophic,Factors, Neurotrophic,Growth Associated Proteins, Neuronal,Growth-Associated Protein, Neuronal,Neuronal Growth Associated Protein,Neuronal Growth Associated Proteins,Outgrowth Factor, Neurite,Outgrowth Factors, Neurite,Protein, Neuronal Growth-Associated
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D012156 Reticulocytes Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes. Reticulocyte
D004151 Dipeptides Peptides composed of two amino acid units. Dipeptide
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D014452 Ubiquitins A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins. Ubiquitin-Like Protein,Ubiquitin-Like Proteins,Protein, Ubiquitin-Like,Proteins, Ubiquitin-Like,Ubiquitin Like Protein,Ubiquitin Like Proteins
D016222 Fibroblast Growth Factor 2 A single-chain polypeptide growth factor that plays a significant role in the process of WOUND HEALING and is a potent inducer of PHYSIOLOGIC ANGIOGENESIS. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to FIBROBLAST GROWTH FACTOR 1 and has potent heparin-binding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor (FIBROBLAST GROWTH FACTOR 1). Basic Fibroblast Growth Factor,Fibroblast Growth Factor, Basic,HBGF-2,Cartilage-Derived Growth Factor,Class II Heparin-Binding Growth Factor,FGF-2,FGF2,Fibroblast Growth Factor-2,Heparin-Binding Growth Factor Class II,Prostate Epithelial Cell Growth Factor,Prostatropin,Cartilage Derived Growth Factor,FGF 2

Related Publications

H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
June 1984, Cell biology international reports,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
July 1994, Brain research. Developmental brain research,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
August 2007, Journal of pharmacological sciences,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
May 1988, Journal of cellular physiology,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
November 2003, Neuroscience letters,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
October 1999, The Journal of antibiotics,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
July 2009, Cytotechnology,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
October 1997, Neurochemistry international,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
January 1995, Neuroscience letters,
H Hondermarck, and J Sy, and R A Bradshaw, and S M Arfin
June 1993, Journal of neurochemistry,
Copied contents to your clipboard!