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Keeping the self-renewal and differentiation of spermatogonial stem cell (SSC) in balance is essential for maintaining spermatogenesis. However, whether the cell death of SSC also plays a vital role in the human being remains unknown. To explore the necroptosis of SSC, the activation marker of necroptosis, phosphorylated mixed lineage kinase domain-like protein (pMLKL) in testes was evaluated by immunofluorescence staining and Western blot. Meanwhile, a total of 81 semen samples were divided based on the sperm concentration (>15, 10-15, 5-10 and 0-5 million/ml) to study the relationships between pMLKL levels and sperm counts. We found that the pMLKL was increased in the ageing human testes (p < 0.05). Moreover, the seminal pMLKL expression was decreased in groups with sperm concentration 0-5 and 5-10 million/ml when compared with normal sperm concentration in young men (p < 0.05). Further analysis revealed that pMLKL showed an age-related increased expression in men aged 22-60 years with normal sperm concentration. These data demonstrated that the necroptosis of SSC was important for the spermatogenic function and would raise in advance on the point of testicular hypofunction. In conclusion, the pMLKL may serve as a potential biologically seminal indicator for the spermatogenic function in men.
This article was published in the following journal.
Lyn kinase (Lck/Yes related novel protein tyrosine kinase) belongs to the family of Src-related non-receptor tyrosine kinases. Consistent with physiological roles in cell growth and proliferation, abe...
Classically activated macrophages (CAMs) play a crucial protective role in the host by killing the invading pathogens. However, excessive activation of CAMs causes chronic inflammation leading to host...
DNA damage response (DDR) pathways form an integral part of the body's repair machinery and Ataxia telangiectasia mutated and Rad-3 related (ATR) is one of the key mediators in DDR pathway. Increasing...
Protein phosphorylation plays a critical role in the regulation of cellular function. Information on protein phosphorylation and the responsible kinases is important for understanding intracellular si...
Co-evolution analysis reveals which amino acids within the protein kinase domain are working together to mediate catalysis, regulation, and substrate binding.
The main task of this study includes analyses of the BCR-ABL1 (breakpoint cluster region/Abelson) gene and mutations in the BCR-ABL1 tyrosine kinase domain within flow-sorted stem cells fr...
In a randomized, cross-over designed study, the investigators examined the effectiveness of the carbohydrate counting method after consumption of mixed meals typical of the Greek cuisine w...
Over the last decade, improvements in the investigators' understanding of the molecular basis of cancer have led to the clinical development of protein kinase inhibitors, which target pivo...
The investigators examined the effects of dietary protein intake in a mixed meal at two levels of protein amount on whole body protein metabolisms in older adults.
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A non-receptor protein tyrosine kinase that is localized to FOCAL ADHESIONS and is a central component of integrin-mediated SIGNAL TRANSDUCTION PATHWAYS. Focal adhesion kinase 1 interacts with PAXILLIN and undergoes PHOSPHORYLATION in response to adhesion of cell surface integrins to the EXTRACELLULAR MATRIX. Phosphorylated p125FAK protein binds to a variety of SH2 DOMAIN and SH3 DOMAIN containing proteins and helps regulate CELL ADHESION and CELL MIGRATION.
A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. The proteins share in common an N-terminal PHOSPHOLIPID-binding domain, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. Upon tyrosine phosphorylation insulin receptor substrate proteins interact with specific SH2 DOMAIN-containing proteins that are involved in insulin receptor signaling.
A cytoskeletal linker protein with a molecular weight of greater than 500 kDa. It binds INTERMEDIATE FILAMENTS; MICROTUBULES; and MICROFILAMENTS and plays a central role in the organization and stability of the CYTOSKELETON. Plectin is phosphorylated by CALMODULIN KINASE; PROTEIN KINASE A; and PROTEIN KINASE C.
A serine-threonine protein kinase family whose members are components in protein kinase cascades activated by diverse stimuli. These MAPK kinases phosphorylate MITOGEN-ACTIVATED PROTEIN KINASES and are themselves phosphorylated by MAP KINASE KINASE KINASES. JNK kinases (also known as SAPK kinases) are a subfamily.
A subclass of receptor-like protein tryosine phosphatases that contain a short extracellular domain, a cytosolic kinase-interaction domain, and single protein tyrosine kinase domain.
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Blood is a specialized bodily fluid that delivers necessary substances to the body's cells (in animals) – such as nutrients and oxygen – and transports waste products away from those same cells. In vertebrates, it is composed of blo...
Track and monitor developments in stem cell research and commercial development. Follow the tabs above to read the latest global news, research, clinical trials on stem cells and follow companies active in the stem cell industry. BioPort...