OBJECTIVETo examine the expression of the tau protein and microtubule-associated proteins in the testis interstitium of aged and young rats.

METHODSSprague-Dawley male rats were divided into a young group(6 months, n = 10) and an aged group(28 months, n = 10). The two steps immunohistochemistry method with the antibody against tau protein and MAP alpha was performed on the testis tissues of the rats.

RESULTSThe results showed that the immunoreactive cells of tau protein of the testis interstilial of the aged rats obviously increased(P < 0.001) than those of the young, while the immunoreactive cells of the microtubule-associated proteins decreased(P < 0.01) in the aged.

CONCLUSIONThe changes in the expression of the tau protein and microtubule-associated proteins may be related to the aging process of the testis.

Aging ; metabolism ; Animals ; Immunohistochemistry ; Male ; Microtubule-Associated Proteins ; analysis ; Rats ; Rats, Sprague-Dawley ; Testis ; chemistry ; tau Proteins ; analysis

Cell Cycle Proteins ; Microtubule-Associated Proteins

Intracellular organelle transport is essential for morphogenesis and functioning of the cell. Kinesins and kinesin-related proteins make up a large superfamily of molecular motors that transport cargoes such as vesicles, organelles (e.g. mitochondria, peroxisomes, lysosomes), protein complexes (e.g. elements of the cytoskeleton, virus particles), and mRNAs in a microtubule- and ATP-dependent manner in neuronal and non-neuronal cells. Until now, more than 45 kinesin superfamily proteins (KIFs) have been identified in the mouse and human genomes. Elucidating the transport pathways mediated by kinesins, the identities of the cargoes moved, and the nature of the proteins that link kinesin motors to cargoes are areas of intense investigation. This review focuses on the structure, the binding partners of kinesins and kinesin-based human diseases.
Adenosine Triphosphate/metabolism ; Alzheimer Disease/metabolism ; Animals ; Biological Transport ; Cytoplasm/metabolism ; Diabetes Mellitus/metabolism ; Human ; Kinesin/*chemistry/*metabolism ; Mice ; Microtubule-Associated Proteins/chemistry ; Microtubules/metabolism ; Models, Biological ; Neurons/metabolism ; Protein Binding ; Support, Non-U.S. Gov't

Adenomatous Polyposis Coli Protein ; chemistry ; metabolism ; Amino Acid Sequence ; Chromatography, High Pressure Liquid ; HeLa Cells ; Humans ; Kinesin ; chemistry ; metabolism ; Microtubule-Associated Proteins ; chemistry ; metabolism ; Microtubules ; metabolism ; Molecular Sequence Data ; Phosphopeptides ; analysis ; Phosphorylation ; Protein Multimerization ; Tandem Mass Spectrometry

A growing body of evidence has indicated the important role of autophagy receptors in directing ubiquitinated or non-ubiquitinated cargos towards autophagy. Autophagy receptors bind to LC3 (microtubule-associated protein 1 light chain 3) on phagophore and autophagosome membranes, and recognize signals on cargoes in the delivery system of autophagy. However, the diverse domains in the receptor structures determine that their roles would never be limited to autophagy. Up to date, increasing numbers of the receptor proteins have been demonstrated to serve as a molecular link or switch participating in autophagic degradation, apoptosis or cell survival signals. Here, we highlight the non-autophagic roles of these receptor proteins to draw attention to this growing research topic.
Apoptosis ; Autophagy ; Humans ; Microtubule-Associated Proteins ; physiology ; Signal Transduction ; Ubiquitination

The present study involves a chronological and comparative analysis of both microtubule-associated protein 1A (MAP1A) and microtubule-associated protein 2 (MAP2) immunoreactivities in the striatum of both seizure resistant (SR) and seizure sensitive (SS) gerbil. The MAP1A immunoreactivity is weakly detected in perikarya of SR gerbils. However, MAP1A immunoreactivity is more accumulated in perikarya and dendrites in the pre-seizure group. At 30 min postictal, MAP1A immunoreactivity in the perikarya is decreased. At 3 hr postictal, MAP1A immunoreactivity in perikarya and dendrites is similarly decreased to the level of SR gerbils. The MAP2 immunoreactivity is weakly detected in the perikarya and dendrites of SR gerbils. However, MAP2 immunoreactivity is more accumulated in perikarya and dendrites. In particular, the neuropil between unstained fiber tracts obviously contains strong MAP2 immunoreactivity. At 30 min postictal, MAP2 immunoreactivity isn't almost observed in striatum. At 3 hr postictal, the MAP2 immunoreactivity is not different in the 30 min post -seizure groups but is only observed in the neuropil. However, at 12 hr postictal, the decrease of both MAP1A and MAP2 immunoreactivities had recovered to the pre -seizure level of SS gerbils. These results suggest that MAPs immunoreactivity in the striatum is different in SR and SS gerbils, and that this difference may be the results of seizure activity in this animal.
Animals ; Dendrites ; Epilepsy ; Gerbillinae* ; Microtubule-Associated Proteins* ; Microtubules* ; Neuropil ; Seizures*

OBJECTIVE: To show evidence of the autophagy in hippocampal nerve cells from rats with sepsis-associated encephalopathy (SAE) in vivo and to investigate the expression of microtubule-associated protein 1 light chain 3 (LC3). 
 METHODS: A rat model of sepsis was established by the cecal ligation and puncture (CLP). A total of 60 male Wistar rats (30 days old) were randomly divided into a sham group (n=10) and a CLP group (n=50). At 12 hours after CLP, the electroencephalogram (EEG) and somatosensory evoked potential (SEP) changes in rats were monitored and the neurobehavioral score was measured. According to the occurrence of SAE, the CLP group was further divided into an SAE(+) group and an SAE(-) group. Histopathological changes in hippocampus were observed by hematoxylin-eosin staining. An electron microscope was used to observe autophagosome formation and lysosome activation in the hippocampal nerve cells. Expressions of LC3-I and LC3-II protein were measured by Western blot. 
 RESULTS: Five of 50 rats in CLP group died in 12 hours after CLP. According to the low neurobehavioral score and abnormal EEG and SEP, 16 rats were diagnosed as SAE. The incidence of SAE was 35.56% (16/45). Compared with the sham group or the SAE(-) group, the frequency of α wave in SAE(+) group was significantly decreased at 12 hours after CLP, the δ wave increased, the P1 amplitude decreased, and the latency of SEP waves (P1 and N1) was prolonged (P<0.05). The morphology of hippocampal nerve cells was obvious in a status of edema. Pyramidal cells decreased significantly, even dissolved, and cell arrangement was in disorder in the SAE(+) group. But these cells were normal in the sham group and the SAE(-) group. The structure of hippocampal nerve cells was disordered, and the autophagy, granular matrix and square or rectangular crystals were found in the SAE(+) group. However, there was no autophagy both in the sham group and the SAE(-) group. LC3-II/LC3-I ratio in the hippocampal nerve cells was increased significantly at 12 hours after CLP in the SAE(+) group when compared with that in the sham or the SAE(-) group (P<0.05). 
 CONCLUSION There is autophagy in hippocampal nerve cells from rats with SAE and the LC3-II/LC3-I ratio is increased significantly.
Animals ; Autophagy ; Hippocampus ; Male ; Microtubule-Associated Proteins ; Neurons ; Rats ; Rats, Wistar ; Sepsis-Associated Encephalopathy

Cells selectively scavenge redundant or damaged mitochondria by mitophagy, which is an important mechanism of mitochondrial quality control. Recent studies have shown that mitophagy is mainly regulated by autophagy-related genes (Atgs) in yeast cells, while mitochondrial membrane associated proteins such as PTEN-induced putative kinase 1 (PINK1), NIX/BNIP3L, BNIP3, FUN14 domain containing 1 (FUNDC1), FKBP8/FKBP38, Bcl-2-like protein 13 (Bcl2L13), nucleotide binding domain and leucine-rich-repeat-containing proteins X1 (NLRX1), prohibitin 2 (PHB2) and lipids such as cardiolipin (CL) are the key mitophagic receptors in mammalian cells, which can selectively recognize damaged mitochondria, recruit them into isolation membranes by binding to microtubule-associated protein 1 light chain 3 (LC3) or γ-aminobutyric acid receptor-associated protein (GABARAP), and then fuse with lysosomes to eliminate the trapped mitochondria. This article reviews recent research progress of mitophagy-related receptor proteins.
Animals ; Apoptosis Regulatory Proteins ; Autophagy ; Microtubule-Associated Proteins ; Mitochondria ; Mitochondrial Proteins/genetics* ; Mitophagy ; Prohibitins

Humans ; Hypertension, Pulmonary ; metabolism ; Inhibitor of Apoptosis Proteins ; Microtubule-Associated Proteins ; metabolism

OBJECTIVETo investigate the effects of arsenic trioxide (As2O3) on the proliferation, differentiation and apoptosis of HL-60 cells in vitro and explore the underlying mechanisms.

METHODSAfter HL-60 cells were treated with different concentration of As2O3, the cell proliferation was determined by MTS/PES method, the differentiation state was detected by the nitroblue tetrazolium (NBT) reduction test; flow cytometry was used to analyze the apoptosis and expression of CD11b. In addition, SYBR Green real-time RT-PCR was used to measure the mRNA levels of C-FES, BCL-2, BAX, survivin , P21 and P27.

RESULTSAs2O3 could obviously inhibit the proliferation of HL-60 cells, and the effect was in dose- and time-dependent manners (r=-0.967; r=-0.954). Low concentration (0.1, 0.5 and 1.0 µmol/L) of As2O3 could significantly promote the differentiation of HL-60 cells, the cells exhibited a higher NBT-reducing ability and expressed far more CD11b antigens. High concentration (2.5 and 5.0 µmol/L) of As2O3 induced HL-60 cell apoptosis, but the ability of promoting differentiation decreased. The expression of C-FES mRNA significantly increased after being treated with As2O3 at the concentrations 1.0 and 5.0 µmol/L, and the former is more obvious, which confirmed that C-FES mRNA level paralleled the cell differentiation degree. Also, the expression of BCL-2 and survivin significantly decreased, while the expression of BAX, P21 and P27 was significantly upregulated in HL-60 cells after being treated with 5.0 µmol/L As2O3.

CONCLUSIONAs2O3 can significantly suppress cell proliferation, promote the differentiation and induce the apoptosis in HL-60 cells, and the mechanism of As2O3 anti-tumor activity may be involved in the regulation of C-FES, cell cycle and apoptosis-related genes.

Apoptosis ; Arsenicals ; Cell Differentiation ; Cell Proliferation ; HL-60 Cells ; Humans ; Microtubule-Associated Proteins ; Oxides