Animals ; Cardiovascular System ; metabolism ; GTPase-Activating Proteins ; metabolism ; Humans ; Nerve Tissue Proteins ; metabolism ; Signal Transduction

OBJECTIVETo investigate the role of microtubule-associated protein 2 (MAP-2) and nestin in gastric development in human embryos and fetuses.

METHODSImmunohistochemistry was used to detect the expressions of MAP-2 and nestin proteins in the gastric cardia, pyloric and gastric tissues of human embryos and fetuses during the second, third and fourth month of development.

RESULTSIn the second to fourth months of gestation, MAP-2 and nestin expressions were detected in the neural cells and neural fibers of the intermuscular nerve plexus and submucosal plexus in the gastric cardia, pyloric and gastric tissues. As the gestational age increased, the number of MAP-2- and nestin-positive cells and the expression intensity all increased in the myenteric plexus, but MAP-2 and nestin expressions were negative in the glandular and mucosal tissues of human embryonic and fetal gastric cardia, pylorus or gastric walls.

CONCLUSIONMAP-2 and nestin participate in the regulation of the development of gastric tissues in human embryos.

Fetus ; metabolism ; Humans ; Intermediate Filament Proteins ; metabolism ; Microtubule-Associated Proteins ; metabolism ; Nerve Tissue Proteins ; metabolism ; Nestin ; Stomach ; embryology ; metabolism

Plexins and semaphorins are a large family of proteins that are involved in cell movement and response. The importance of plexins and semaphorins has been emphasized by their discovery in many organ systems including the nervous (Nkyimbeng-Takwi and Chapoval, 2011; McCormick and Leipzig, 2012; Yaron and Sprinzak, 2012), epithelial (Miao et al., 1999; Fujii et al., 2002), and immune systems (Takamatsu and Kumanogoh, 2012) as well as diverse cell processes including angiogenesis (Serini et al., 2009; Sakurai et al., 2012), embryogenesis (Perala et al., 2012), and cancer (Potiron et al., 2009; Micucci et al., 2010). Plexins and semaphorins are transmembrane proteins that share a conserved extracellular semaphorin domain (Hota and Buck, 2012). The plexins and semaphorins are divided into four and eight subfamilies respectively based on their structural homology. Semaphorins are relatively small proteins containing the extracellular semaphorin domain and short intracellular tails. Plexins contain the semaphorin domain and long intracellular tails (Hota and Buck, 2012). The majority of plexin and semaphorin research has focused on the nervous system, particularly the developing nervous system, where these proteins are found to mediate many common neuronal cell processes including cell movement, cytoskeletal rearrangement, and signal transduction (Choi et al., 2008; Takamatsu et al., 2010). Their roles in the immune system are the focus of this review.
Animals ; Cell Adhesion Molecules ; immunology ; metabolism ; Humans ; Immunity ; Nerve Tissue Proteins ; immunology ; metabolism ; Semaphorins ; immunology ; metabolism

This study was designed to elucidate the existence of PSD95 in the rat sciatic nerve. Immunohistochemical stains of cryosection and teased fiber of sciatic nerves were performed with goat polyclonal antibody against PSD95. Western blot analysis was also accomplished with the same antibody. We got an interesting result that the rat sciatic nerve obviously showed PSD95 immunoreactivity especially in the nodal and paranodal regions, and we also identified a distinct band of PSD95 by western blot. These results suggest PSD95 exists in the sciatic nerve as well as it does in the central nervous system. We suppose PSD95 may have some important roles in ion channel clustering, junctional plasticity and signal transduction in the peripheral nerves as well.
Animals ; Blotting, Western ; Cerebellum/cytology/metabolism ; Immunohistochemistry ; Nerve Fibers/metabolism/ultrastructure ; Nerve Tissue Proteins/*metabolism ; Rats ; Rats, Sprague-Dawley ; Sciatic Nerve/*metabolism

A strong animal survival instinct is to approach objects and situations that are of benefit and to avoid risk. In humans, a large proportion of mental disorders are accompanied by impairments in risk avoidance. One of the most important genes involved in mental disorders is disrupted-in-schizophrenia-1 (DISC1), and animal models in which this gene has some level of dysfunction show emotion-related impairments. However, it is not known whether DISC1 mouse models have an impairment in avoiding potential risks. In the present study, we used DISC1-N terminal truncation (DISC1-N
Animals ; Interneurons/metabolism* ; Mice ; Mice, Transgenic ; Nerve Tissue Proteins/metabolism* ; Neurons/metabolism* ; Nucleus Accumbens/metabolism* ; Parvalbumins/metabolism*

OBJECTIVETo investigate the role of autophagy on the pathogenesis of spinocerebellar ataxia 3/Machado-Joseph disease (SCA3/MJD).

METHODSHEK293 cells expressing polyglutamine-expanded ataxin-3 were used as cell model for SCA3/MJD. The level of polyglutamine-expanded ataxin-3 was detected after cells were treated with different inhibitors or inducer of autophagy.

RESULTSInhibition of autophagy increased aggregate formation and cell death in HEK293 cells expressing mutated ataxin-3, and vice versa.

CONCLUSIONThe data suggested that autophagy is involved in the degradation of mutant ataxin-3, resulting in a decrease in the proportions of aggregate-containing cells and cell death in HEK293 cells expressing polyglutamine-expanded ataxin-3. It is possible that autophagy may be applied as a potential therapeutic approach for SCA3/MJD.

Ataxin-3 ; Autophagy ; Cell Line ; Humans ; Machado-Joseph Disease ; genetics ; metabolism ; physiopathology ; Mutation ; Nerve Tissue Proteins ; genetics ; metabolism ; Nuclear Proteins ; genetics ; metabolism ; Peptides ; metabolism ; Repressor Proteins ; genetics ; metabolism

OBJECTIVEMachado-Joseph disease (MJD)/Spinocerebellar ataxia type 3 (SCA3) is an autosomal dominant neurodegenerative disorder caused by an expansion of polyglutamine tract near the C-terminus of the MJD1 gene product, ataxin-3. The precise mechanism of the MJD/SCA3 pathogenesis remains unclear. A growing body of evidence demonstrates that phosphorylation plays an important role in the pathogenesis of many neurodegenerative diseases. However, few kinases are known to phosphorylate ataxin-3. The present study is to explore whether ataxin-3 is a substrate of casein kinase 2 (CK2).

METHODSThe interaction between ataxin-3 and CK2 was identified by glutathione S-transferase (GST) pull-down assay and co-immunoprecipition assay. The phosphorylation of ataxin-3 by CK2 was measured by in vitro phosphorylation assays. Results (1) Both wild type and expanded ataxin-3 interacted with CK2alpha and CK2beta in vitro. (2) In 293 cells, both wild type and expanded ataxin-3 interacted with CK2beta, but not CK2alpha. (3) CK2 phosphorylated wild type and expanded ataxin-3.

CONCLUSIONAtaxin-3 is a substrate of protein kinase CK2.

Ataxin-3 ; Casein Kinase II ; metabolism ; Cell Line, Transformed ; Glutathione Transferase ; metabolism ; Humans ; Immunoprecipitation ; methods ; Nerve Tissue Proteins ; metabolism ; Nuclear Proteins ; metabolism ; Phosphorylation ; Repressor Proteins ; metabolism ; Transfection ; methods

Biomarkers ; Heart Diseases ; diagnosis ; metabolism ; Humans ; Natriuretic Peptide, Brain ; metabolism ; physiology ; Nerve Tissue Proteins ; metabolism ; physiology ; Peptide Fragments ; metabolism ; physiology

OBJECTIVE: To investigate the regulatory role of Musashi-1 (MSI1) in the proliferation and growth of hepatocellular carcinoma (HCC) cells. METHODS: We examined the expression of MSI1 in HCC and paired adjacent tissues from 24 patients using immunohistochemistry and Western blotting. A MSI1-expressing vector was constructed and stably transfected into HepG2 cells, and short hairpin RNAs (shRNAs) that targeted MSI1 mRNA were ligated into the vector and stably transfected in Huh7 cells. The effects of MSI1 overexpression and silencing on the proliferation, viability and cell cycle of HepG2 cells were investigated using flow cytometry or MTT assay. The expressions of PCNA, cyclin D1, APC and β-catenin in the HCC cells were detected with Western blotting. RESULTS: MSI1 expression was significantly up-regulated in HCC tissues as compared with that in the adjacent tissues. Overexpression of MSI1 in HepG2 cells resulted in significantly enhanced cell growth ( < 0.01) and significantly reduced G0/G1 phase cells from (58.42±3.18)% to (40.67±1.22)% and increased S phase cells from (28.51± 1.93)% to (40.06±1.92)% ( < 0.01), causing also increases in the expressions of PCNA and Cyclin D1. Knockdown of MSI1 in Huh7 cells obviously inhibited the cell growth and caused cell cycle arrest at the G1/S phase ( < 0.01) with reduced protein expressions of PCNA and cyclin D1. Overexpression of MSI1 in HepG2 cells also down-regulated the expression of APC and up-regulated the expression of β-catenin protein, while MSI1 knockdown caused reverse changes in Huh7 cells. CONCLUSIONS MSI1 promotes the progression of HCC through positive modulation of cell growth and cell cycle the Wnt/β-catenin pathway.
Carcinoma, Hepatocellular ; Cell Cycle ; Cell Proliferation ; Hep G2 Cells ; Humans ; Liver Neoplasms ; Nerve Tissue Proteins ; metabolism ; RNA-Binding Proteins ; metabolism

OBJECTIVE: To study the expression of PCNA and LNGFr in olfactory epithelium of patients suffering from dysosmia caused by chronic sinusitis, and the function of LNGFr. METHOD: Forty-six patients undergoing FESS were chosen. Before operation, their olfactory functions were examined with CCCRC. According to their CCCRC scores, they were divided into three groups. Group A: Patients with chronic sinusitis and dysosmia 25 cases; Group B: Patients with chronic sinusitis and a normal olfactory function 10 cases; Group C: Patients with deviation of nasal septum and a normal olfactory function 11 cases. The expressions of PCNA and LNGFr were measured in olfactory mucosas of the three groups by immunohistochemistry. RESULT: In basal cells, the expression of PCNA and LNGFr in group A was higher than that in group B (P < 0.01). and in group C (P < 0.01). There was negative correlation between positive cells of PCNA and CCCRC score in basal cells of group A (r = -0.7441, P < 0.01); There was negative correlation between integral optical density of LNGFr and CCCRC score in basal cells of group A (r = -0.4407, P < 0.05). There was positive correlation between positive cells of PCNA and integral optical density of LNGFr in basal cells of group A (r = 0.5317, P < 0.01). CONCLUSION Basal cells proliferated dramatically in patients suffering from dysosmia caused by chronic sinusitis. The proliferating capacity of basal cells was related to up-regulation of LNGFr expression.
Chronic Disease ; Humans ; Immunohistochemistry ; Nerve Tissue Proteins ; metabolism ; Olfaction Disorders ; metabolism ; Olfactory Mucosa ; metabolism ; Proliferating Cell Nuclear Antigen ; metabolism ; Receptors, Nerve Growth Factor ; metabolism ; Sinusitis ; complications