scholarly journals Increase in Insulin-like Growth Factor II Receptor within Ischemic Neurons following Focal Cerebral Infarction

1995 ◽  
Vol 15 (6) ◽  
pp. 1022-1031 ◽  
Author(s):  
Diane T. Stephenson ◽  
Karen Rash ◽  
James A. Clemens
Keyword(s):  
Growth Factor ◽  
Pyramidal Neurons ◽  
Focal Cerebral Ischemia ◽  
Morphological Changes ◽  
Neuron Specific Enolase ◽  
Growth Factor Receptor ◽  
Staining Intensity ◽  
Insulin Like Growth Factor ◽  
Neuronal Markers ◽  
Factor Ii

The mechanisms underlying the response of the brain to ischemia are not fully understood. Biochemical and morphological changes following neocortical infarction can be investigated in rats using a model of focal cerebral ischemia induced by unilateral occlusion of the middle cerebral artery (MCA). Evaluation of ischemic damage often employs conventional histologic stains. Immunocytochemistry can be used as a valuable tool in this model to define changes in specific proteins of interest. In this study, an antiserum raised against insulin-like growth factor II (IGF-II) receptor was used to evaluate changes of IGF-II receptor immunoreactivity in the cerebral cortex of rats 4 and 7 days following permanent MCA occlusion. IGF-II receptor immunoreactivity was found to be associated with neocortical pyramidal neurons within the core of the ischemic infarct itself. The staining intensity was markedly elevated above that observed in nonischemic neurons. Immunopositive neurons exhibited a punctate staining pattern. These neurons appeared to correspond to argentophilic neurons, as defined by modified Bielschowsky silver staining. Evaluation of other neuronal markers revealed the absense of immunoreactivity for neuron-specific enolase and for tyrosine hydroxylase within the ischemic area. These observations show an increase in a specific growth factor receptor within neurons in the ischemic core of a focal infarct several days following permanent focal infarction, a time when neurons are presumed to be dead. The significance and the potential role of IGF-II receptor in lesion-induced plasticity are discussed.

Insulin-like growth factor II in mammalian brain interacts with two types of insulin-like growth factor receptor

1986 ◽  
Vol 14 (6) ◽  
pp. 1161-1162
Author(s):  
STEEN GAMMELTOFT ◽  
GISELA HASELBACHER ◽  
ROBERT BALLOTTI ◽  
BENGT WESTERMARK ◽  
RENÉ E. HUMBEL ◽  
...  
Keyword(s):  
Growth Factor ◽  
Growth Factor Receptor ◽  
Mammalian Brain ◽  
Insulin Like Growth Factor ◽  
Factor Ii

scholarly journals Insulin-like Growth Factor II Prevents MPP+ and Glucocorticoid Mitochondrial-Oxidative and Neuronal Damage in Dopaminergic Neurons

Antioxidants ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 41
Author(s):  
Silvia Claros ◽  
Pablo Cabrera ◽  
Nadia Valverde ◽  
Silvana Y. Romero-Zerbo ◽  
Manuel Víctor López-González ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Growth Factor ◽  
Dopaminergic Neurons ◽  
Neuronal Damage ◽  
Cell Damage ◽  
Antioxidant Response ◽  
Insulin Like Growth Factor ◽  
Neuroprotective Effects ◽  
Neuronal Markers ◽  
Factor Ii

Stress seems to contribute to Parkinson’s disease (PD) neuropathology, probably by dysregulation of the hypothalamic–pituitary–adrenal axis. Key factors in this pathophysiology are oxidative stress and mitochondrial dysfunction and neuronal glucocorticoid-induced toxicity. The insulin-like growth factor II (IGF-II), a pleiotropic hormone, has shown antioxidant and neuroprotective effects in some neurodegenerative disorders. Our aim was to examine the protective effect of IGF-II on a dopaminergic cellular combined model of PD and mild to moderate stress measuring oxidative stress parameters, mitochondrial and neuronal markers, and signalling pathways. IGF-II counteracts the mitochondrial-oxidative damage produced by the toxic synergistic effect of corticosterone and 1-methyl-4-phenylpyridinium, protecting dopaminergic neurons from death and neurodegeneration. IGF-II promotes PKC activation and nuclear factor (erythroid-derived 2)-like 2 antioxidant response in a glucocorticoid receptor-dependent pathway, preventing oxidative cell damage and maintaining mitochondrial function. Thus, IGF-II is a potential therapeutic tool for treatment and prevention of disease progression in PD patients suffering mild to moderate emotional stress.

Mannose 6-phosphate Receptor (MPR 300) Proteins from Goat and Chicken Bind Human IGF-II

2006 ◽  
Vol 26 (2) ◽  
pp. 101-112 ◽  
Author(s):  
Suresh Koduru ◽  
Sivaramakrishna Yadavalli ◽  
Siva Kumar Nadimpalli
Keyword(s):  
Plasma Membrane ◽  
Growth Factor ◽  
Lysosomal Enzymes ◽  
Growth Factor Receptor ◽  
Cell Receptor ◽  
Insulin Like Growth Factor ◽  
Fish Embryo ◽  
Multifunctional Protein ◽  
Factor Ii ◽  
Mannose 6 Phosphate

Mannose 6-phosphate receptor proteins (MPR 300 and 46) in mammals have been shown to mediate transport of lysosomal enzymes to lysosomes intracellularly. Both receptors are also expressed on the plasma membrane. Only MPR 300 protein on the plasma membrane has been shown to be a multifunctional protein which in addition to binding mannose 6-phosphate containing proteins also binds human insulin-like growth factor-II (IGF-II) causing its internalization [Hille-Rehfeld, A. (1995) Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes. Biochim. Biophys. Acta. 1241: 177–194]. This property has been shown to be exhibited by other mammalian receptors but not by the chicken and frog receptors. In a recent study however it was shown that the fish embryo MPR 300 binds human IGF-II. [Mendez, E., Planas, J.V., Castillo, J., Navarro, I. and Gutierrez, J. (2001) Identification of a type II insulin-like growth factor receptor in fish embryos. Endocrinology, 142: 1090–1097]. In the present study, we demonstrate that the purified goat and chicken liver receptors bind human IGF-II by employing cross-linking experiments (purified receptors and radiolabeled IGF-II) and by ligand blotting (using purified receptors and biotinylated IGF-II). Further CEF cells (chicken embryonic fibroblasts) that are known to contain the putative MPR 300 protein were employed to demonstrate that the CEF cell receptor binds human IGF-II.

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