Bcl‐2 Regulates the Levels of the Cysteine Proteases ICH and CPP32/Yama in Human Neuronal Precursor Cells

Korhonen, Laura; Hamnér, Susanne; Olsson, Per-Anders; Lindholm, Dan

doi:10.1111/j.1460-9568.1997.tb01666.x

Cited by 15 publications

(10 citation statements)

References 33 publications

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“…RNA was electrophoresed through a 1.2% agarose formaldehyde gel, transfered onto Hybond‐N membranes and hybridized as described earlier (Leingärtner et al . 1994; Korhonen et al . 1997).…”

Section: Methodsmentioning

confidence: 99%

Pituitary adenylate cyclase‐activating polypeptide promotes the survival of basal forebrain cholinergic neurons in vitro and in vivo: comparison with effects of nerve growth factor

Takei

Torres

Yuhara

et al. 2000

Eur J of Neuroscience

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Pituitary adenylate cyclase-activating polypeptide (PACAP) is a member of the vasointestinal polypeptide gene family for which neurotrophic activity has been postulated. PACAP mRNA is expressed in the developing and adult hippocampus, which is the principal target region of septal cholinergic neurons. We therefore studied the effects of PACAP on septal cholinergic neurons. In primary cultures from septum of embryonic and postnatal rats, PACAP increased the number of neurons immunohistochemically stained for the low-affinity nerve growth factor (NGF) receptor p75 and for the enzyme choline acetyltransferase (ChAT). PACAP also caused a corresponding increase in ChAT activity. In comparison, NGF had a greater effect than PACAP on the number of p75- and ChAT-positive neurons in these cultures. In vivo, following fimbria fornix transection, the number of immunohistochemically stained septal cholinergic neurons fell significantly to 18% in rats given continuous intracerebroventricular infusion of vehicle, whereas in rats given NGF the number of these neurons did not differ significantly from unoperated controls. In PACAP-treated rats the number was 48% of unoperated values, which represented a significant increase compared with vehicle-treated rats and a significant decrease compared with NGF-treated rats or unoperated controls. Double-staining experiments revealed that most ChAT-positive neurons in rat medial septum also express PACAP receptor 1. Together the results show that PACAP promotes the survival of septal cholinergic neurons in vitro, and after injury in vivo, suggesting that PACAP acts as a neurotrophic factor influencing the development and maintenance of these neurons.

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Section: Methodsmentioning

confidence: 99%

Pituitary adenylate cyclase‐activating polypeptide promotes the survival of basal forebrain cholinergic neurons in vitro and in vivo: comparison with effects of nerve growth factor

Takei

Torres

Yuhara

et al. 2000

Eur J of Neuroscience

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“…The experiments were repeated three times. Western blots for analysis of TH protein levels were performed as described previously (Korhonen et al, 1997); 60 µg of total protein was applied to each lane and the blotting was done using the anti-TH antibody.…”

Section: Dopamine Uptake and Western Blotsmentioning

confidence: 99%

Neurotrophic and neuroprotective effects of pituitary adenylate cyclase-activating polypeptide (pACAP) on mesencephalic dopaminergic neurons

1998

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The neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP) is present in many regions of the adult and developing brain as are receptors for PACAP. PACAP stimulates different signalling cascades in neurons, involving cAMP, MAP kinase, and calcium. These characteristics suggest that PACAP may influence neuronal development. Here we have studied the effects of PACAP on mesencephalic dopaminergic neurons using primary cultures from embryonic rats. PACAP increased the number of tyrosine hydroxylase (TH)-immunoreactive neurons, elevated TH protein, and enhanced tritiated dopamine uptake in these cultures. Moreover, PACAP counteracted the effects of 6-hydroxydopamine treatments, which induce cell death of dopaminergic neurons. In situ hybridisation showed that both PACAP and PACAP receptor type 1 are present in developing and adult rat mesencephalon. These results show that PACAP has a neurotrophic action on dopaminergic neurons and partially protects them against 6-OHDA induced neurotoxicity.

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“…The purified antibody recognized recombinant MIR in Western blots (data not shown). Cells were fixed for 10 min using 4% paraformaldehyde, washed with phosphate-buffered saline, and blocked overnight with skim milk (18). The MIR antibody, diluted 1:100, was added and incubated overnight at 4°C.…”

Section: Cloning Of Mir-a Search In Genbankmentioning

confidence: 99%

“…The antibody-protein complex formed was bound to protein A-Sepharose (Amersham Pharmacia Biotech, Uppsala) and washed three times with RIPA buffer. The beads were suspended and boiled in SDS-loading buffer, and the eluate loaded onto a 12% SDS acrylamide gel (18). The gel was blotted onto a polyvinylidene difluoride membrane (Amersham Pharmacia Biotech) and incubated with anti-His (CLON-TECH) and anti-HA antibodies (Boehringer-Mannheim).…”

Section: Cloning Of Mir-a Search In Genbankmentioning

confidence: 99%

MIR Is a Novel ERM-like Protein That Interacts with Myosin Regulatory Light Chain and Inhibits Neurite Outgrowth

Olsson

Korhonen

Mercer

et al. 1999

Journal of Biological Chemistry

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The ERM protein family members ezrin, radixin, and moesin are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. Here we report on the cloning of myosin regulatory light chain interacting protein (MIR), a protein with an ERMhomology domain and a carboxyl-terminal RING finger, that is expressed, among other tissues, in brain. MIR is distributed in cultured COS cells, in a punctated manner as shown using enhanced green fluorescent protein (EGFP)-tagged MIR and by staining with a specific antibody for MIR. In the yeast two-hybrid system and in transfected COS cells, MIR interacts with myosin regulatory light chain B, which in turn regulates the activity of the actomyosin complex. Overexpression of MIR cDNA in PC12 cells abrogated neurite outgrowth induced by nerve growth factor (NGF) without affecting TrkA signaling. The results show that MIR, a novel ERMlike protein, affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth.Dynamic changes in cell shape and movements involve interactions between proteins in the cytoskeleton and the plasma membrane. Ezrin, radixin, moesin, and the related tumor suppressor merlin link the actin cytoskeleton to membrane-bound proteins located at membrane extension sites, such as microvilli, membrane rufflings, and at cell-cell contacts (1-3). ERM 1 proteins are also involved in cell adhesion, influencing the redistribution of various cell adhesion molecules, such as ICAM-1 (4, 5). The amino-terminal domain of ERM proteins, comprising about 300 amino acids, is conserved among the different proteins and merlin and exhibits a high degree of sequence similarity (1-3). This amino terminus is related to proteins in the large band 4.1 protein superfamily (6), including some protein tyrosine phosphatases (7) and talin (8), and it is thought to bind to membrane proteins. In contrast, the interaction of ERM proteins with F-actin seems to involve both the amino-and carboxyl-terminal region (5). Merlin, however, lacks the F-actin binding site in the carboxyl terminus, but binds it in a different manner (9).ERM proteins are present in a wide variety of tissues, notably in epithelial cells in culture (10). In contrast to other tissues, less is known about the function of ERM proteins in the nervous system. During development and regeneration, neurons grow over large distances in a process controlled by extrinsic factors and cytoskeleton interactions. Some ERM proteins have been found in the growth cones of neuronal cells (11,12), suggesting an effect on neurite outgrowth. Indeed, recently it was shown by an antisense approach, that radixin and moesin are important for growth cone morphology and motility (13). Although important for dynamic interactions between cytoskeleton and membranes, the mechanism by which ERM proteins mediate their effects on cell motility is not fully understood (5). In this study, we have identified a novel ERM-like protein, called myosin regulatory light chain interacting protein (MIR), that binds to the...

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Bcl‐2 Regulates the Levels of the Cysteine Proteases ICH and CPP32/Yama in Human Neuronal Precursor Cells

Cited by 15 publications

References 33 publications

Pituitary adenylate cyclase‐activating polypeptide promotes the survival of basal forebrain cholinergic neurons in vitro and in vivo: comparison with effects of nerve growth factor

Pituitary adenylate cyclase‐activating polypeptide promotes the survival of basal forebrain cholinergic neurons in vitro and in vivo: comparison with effects of nerve growth factor

Neurotrophic and neuroprotective effects of pituitary adenylate cyclase-activating polypeptide (pACAP) on mesencephalic dopaminergic neurons

MIR Is a Novel ERM-like Protein That Interacts with Myosin Regulatory Light Chain and Inhibits Neurite Outgrowth

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