Chronic stress affects tyrosine phosphorylated protein expression and secretion of male rat epididymis

Andrologia ◽  
2021 ◽  
Author(s):  
Supatcharee Arun ◽  
Arada Chaiyamoon ◽  
Natthapol Lapyuneyong ◽  
Sudtida Bunsueb ◽  
Alexander Tsang‐Hsien Wu ◽  
...  
Keyword(s):  
Protein Expression ◽  
Chronic Stress ◽  
Male Rat ◽  
Phosphorylated Protein ◽  
Rat Epididymis ◽  
Tyrosine Phosphorylated Protein

scholarly journals Methotrexate Changes the Testicular Tyrosine Phosphorylated Protein Expression and Seminal Vesicle Epithelia of Adult Rats

2018 ◽  
Vol 36 (2) ◽  
pp. 737-742 ◽  
Author(s):  
Sitthichai Iamsaard ◽  
Jariya Umka Welbat ◽  
Wannisa Sukhorum ◽  
Suchada Krutsri ◽  
Supatcharee Arun ◽  
...  
Keyword(s):  
Protein Expression ◽  
Seminal Vesicle ◽  
Adult Rats ◽  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

scholarly journals pp75: A novel tyrosine-phosphorylated protein that heralds differentiation of HL-60 cells

1991 ◽  
Vol 266 (18) ◽  
pp. 11890-11895
Author(s):  
I. Bushkin ◽  
J. Roth ◽  
D. Heffetz ◽  
Y. Zick
Keyword(s):  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

scholarly journals Erythropoietin induces the association of phosphatidylinositol 3'-kinase with a tyrosine-phosphorylated protein complex containing the erythropoietin receptor

1993 ◽  
Vol 216 (3) ◽  
pp. 821-828 ◽  
Author(s):  
Patrick MAYEUX ◽  
Isabelle DUSANTER-FOURT ◽  
Odile MULLER ◽  
Philippe MAUDUIT ◽  
Michele SABBAH ◽  
...  
Keyword(s):  
Protein Complex ◽  
Erythropoietin Receptor ◽  
Phosphatidylinositol 3 Kinase ◽  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein ◽  
Phosphatidylinositol 3

Crkl is constitutively tyrosine phosphorylated in platelets from chronic myelogenous leukemia patients and inducibly phosphorylated in normal platelets stimulated by thrombopoietin

Blood ◽  
1996 ◽  
Vol 88 (11) ◽  
pp. 4304-4313 ◽  
Author(s):  
A Oda ◽  
Y Miyakawa ◽  
BJ Druker ◽  
A Ishida ◽  
K Ozaki ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Tyrosine Phosphorylation ◽  
Molecular Mechanisms ◽  
Genetically Engineered ◽  
Myelogenous Leukemia ◽  
Insoluble Residue ◽  
Consistent Difference ◽  
Clot Retraction ◽  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

Abstract Platelet functions such as aggregation and clot retraction are often abnormal in chronic mylogenous leukemia (CML) patients. However, the molecular mechanisms of these altered functions are unknown. As expression of the p210bcr-abl oncogene product, a constitutively active tyrosine kinase, is known to have an essential role in the pathogenesis of CML and tyrosine phosphorylation is intimately involved in various aspects of platelet activation, we examined the pattern of protein tyrosine phosphorylation in platelets from 15 CML patients by immunoblotting with a monoclonal antiphosphotyrosine antibody (4G10). Before and after stimulation with thrombin, the only consistent difference between normal and CML platelets was the presence of a tyrosine phosphorylated protein with a relative molecular weight of 39 kD. This tyrosine phosphorylated protein was identified as crid, an SH2, SH3 containing adapter protein. Thus, as previously demonstrated for neutrophils from CML patients, tyrosine phosphorylation of p39crkl persists in mature platelets. No tyrosine phosphorylation of crid was detected following stimulation with thrombin in normal platelets. However, crkl became incorporated into the Triton X-100 insoluble residue following thrombin stimulation in a manner dependent on platelet aggregation. Further, we found that crkl is an endogenous substrate for calpain, a protease that may be involved in postaggregation signaling processes. This suggests that crkl may be involved in the reorganization of the cytoskeleton during normal platelet aggregation and its tyrosine phosphorylation in CML platelets may contribute to the abnormal platelet function in CML patients. Finally, we found that thrombopoietin induces tyrosine phosphorylation of crk1 in normal platelets and FDCP cells genetically engineered to express human c-Mpl. This suggests that crk1 can be phosphorylated by a kinase other than p210bcr-abl and that crk1 may have a role in signaling by thrombopoietin.

scholarly journals Characterization of GABAergic Marker Expression in the Chronic Unpredictable Stress Model of Depression

2017 ◽  
Vol 1 ◽  
pp. 247054701772045 ◽  
Author(s):  
Mounira Banasr ◽  
Ashley Lepack ◽  
Corey Fee ◽  
Vanja Duric ◽  
Jaime Maldonado-Aviles ◽  
...  
Keyword(s):  
Major Depressive Disorder ◽  
Prefrontal Cortex ◽  
Depressive Disorder ◽  
Protein Expression ◽  
Neuropeptide Y ◽  
Chronic Stress ◽  
Gabaergic Interneurons ◽  
Chronic Unpredictable Stress ◽  
Major Depressive

Background Evidence continues to build suggesting that the GABAergic neurotransmitter system is altered in brains of patients with major depressive disorder. However, there is little information available related to the extent of these changes or the potential mechanisms associated with these alterations. As stress is a well-established precipitant to depressive episodes, we sought to explore the impact of chronic stress on GABAergic interneurons. Methods Using western blot analyses and quantitative real-time polymerase chain reaction, we assessed the effects of five-weeks of chronic unpredictable stress exposure on the expression of GABA-synthesizing enzymes (GAD65 and GAD67), calcium-binding proteins (calbindin, parvalbumin, and calretinin), and neuropeptides co-expressed in GABAergic neurons (somatostatin, neuropeptide Y, vasoactive intestinal peptide, and cholecystokinin) in the prefrontal cortex and hippocampus of rats. We also investigated the effects of corticosterone and dexamethasone exposure on these markers in vitro in primary cortical and hippocampal cultures. Results We found that chronic unpredictable stress induced significant reductions of GAD67 protein levels in both the prefrontal cortex and hippocampus of chronic unpredictable stress-exposed rats but did not detect changes in GAD65 protein expression. Similar protein expression changes were found in vitro in cortical neurons. In addition, our results provide clear evidence of reduced markers of interneuron population(s), namely somatostatin and neuropeptide Y, in the prefrontal cortex, suggesting these cell types may be selectively vulnerable to chronic stress. Conclusion Together, this work highlights that chronic stress induces regional and cell type-selective effects on GABAergic interneurons in rats. These findings provide additional supporting evidence that stress-induced GABA neuron dysfunction and cell vulnerability play critical roles in the pathophysiology of stress-related illnesses, including major depressive disorder.

Localization of a 215-kDa tyrosine-phosphorylated protein that cross-reacts with tensin antibodies

1992 ◽  
Vol 203 (1) ◽  
pp. 39-46 ◽  
Author(s):  
Susanne M. Bockholt ◽  
Carol A. Otey ◽  
John R. Glenney ◽  
Keith Burridge
Keyword(s):  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein

An avian cDNA encoding a tyrosine-phosphorylated protein with PDZ, coiled-coil, and SAM domains

Gene ◽  
1998 ◽  
Vol 219 (1-2) ◽  
pp. 111-123 ◽  
Author(s):  
Kwang Sun Suh ◽  
Yuan-Tsang Ting ◽  
John G. Burr
Keyword(s):  
Coiled Coil ◽  
Phosphorylated Protein ◽  
Tyrosine Phosphorylated Protein
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