Aims: The common subtypes of renal tumours are conventional, papillary, chromophobe carcinoma and oncocytoma. The morphological differentiation between chromophobe carcinoma and oncocytoma may be difficult. The aim was to evaluate S100A1 as a new marker for the differentiation of the two subtypes.
Methods And Results: Thirty-nine tumour samples [nine clear cell renal cell carcinomas (RCCs), six papillary RCCs, nine chromophobe RCCs and 15 oncocytomas] were studied. The protein expression of S100A1 was evaluated by immunohistochemistry. The gene expression of S100A1 was analysed by reverse transcriptase-polymerase chain reaction. Nine oncocytomas showed strong immunoreactivity for S100A1. Four oncocytomas were scored as moderate and one as weak reactivity. In total, 14/15 (93%) of oncocytomas were considered to be immunopositive. In contrast, all nine chromophobe RCCs were considered to be immunonegative. There was a significant difference in the positive percentages of staining of S100A1 between these two subtypes (P < 0.01). S100A1 immunoreactivity was observed in 6/9 clear cell and 4/6 papillary carcinomas. The results of S100A1 gene expression corresponded well with the results of immunohistochemistry.
Conclusion: S100A1 may be a potentially powerful marker to differentiate the chromophobe RCC from renal oncocytoma.
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http://dx.doi.org/10.1111/j.1365-2559.2007.02655.x | DOI Listing |
Cell Tissue Res
January 2025
Department of Animal Science, Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia.
Traditional transcriptomic studies often overlook the complex heterogeneity of skeletal muscle, as they typically isolate RNA from mixed muscle fibre and cell populations, resulting in an averaged transcriptomic profile that obscures fibre type-specific differences. This study assessed the potential of the recently developed Xenium platform for high-resolution spatial transcriptomic analysis of human skeletal muscle histological sections. Human vastus lateralis muscle samples from two individuals were analysed using the Xenium platform and Human Multi-Tissue and Cancer Panel targeting 377 genes complemented by staining of successive sections for Myosin Heavy Chain isoforms to differentiate between type 1 and type 2 muscle fibres.
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January 2025
Department of Pathology, Honghui Hospital, Xi'an Jiaotong University College of Medicine, Xi'an, Shaanxi, China.
Introduction: Osteosarcoma (OS) is a malignancy of the bone that mainly afflicts younger individuals. Despite existing treatment approaches, patients with metastatic or recurrent disease generally face poor prognoses. A greater understanding of the tumor microenvironment (TME) is critical for enhancing outcomes in OS patients.
View Article and Find Full Text PDFJ Gen Physiol
January 2025
Chemistry Department, University of Massachusetts Lowell, Lowell, MA, USA.
Titin is the third contractile filament in the sarcomere, and it plays a critical role in sarcomere integrity and both passive and active tension. Unlike the thick and thin filaments, which are polymers of myosin and actin, respectively, titin is a single protein that spans from Z-disk to M-line. The N2A region within titin has been identified as a signaling hub for the muscle and is shown to be involved in multiple interactions.
View Article and Find Full Text PDFFish Shellfish Immunol
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Jiangsu Province Engineering Research Center for Marine Bio-resources Sustainable Utilization, College of Oceanography, Hohai University, Nanjing, 210024, China.
The S100 proteins are highly conserved EF-hand calcium-binding proteins found only in vertebrates. In the current study, two S100 genes (S100A1 and S100A10) were successfully identified and characterized from hybrid grouper Epinephelus lanceolatus♂ × Epinephelus fuscoguttatus♀. The deduced S100A10 protein contained two EF-hand domains, and S100A1 only possessed the N-terminal EF-hand.
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November 2024
Molecular and Translational Cardiology, Heidelberg University Hospital (UKHD), Germany. (D.K., J.R., K.S., K.V., J.B., M.E., A.J., C.B., M.B., P.M.).
Background: The EF-hand Ca sensor protein S100A1 has been identified as a molecular regulator and enhancer of cardiac performance. The ability of S100A1 to recognize and modulate the activity of targets such as SERCA2a (sarcoplasmic reticulum Ca ATPase) and RyR2 (ryanodine receptor 2) in cardiomyocytes has mostly been ascribed to its hydrophobic C-terminal α-helix (residues 75-94). We hypothesized that a synthetic peptide consisting of residues 75 through 94 of S100A1 and an N-terminal solubilization tag (S100A1ct) could mimic the performance-enhancing effects of S100A1 and may be suitable as a peptide therapeutic to improve the function of diseased hearts.
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