[The expression and clinical progression of androgen, estrogen and prolactin receptor in laryngeal squamous cell carcinoma].

Objective:The aim of this study is to analyze the different expression and function of androgen receptors (AR) and estrogen receptor (ER-α) in laryngeal squamous cell carcinoma (LSCC). In combination with the expression of prolactin receptor (PRLR), we analyzed the prognostic impact of three receptors on the laryngeal carcinoma. Method:In this study, immunohistochemistry and reverse transcription polymerase chain reaction (RT-PC) analysis were performed on the tumor tissues and adjacent normal tissues in 112 LSCC patients (95 males and 17 females). We found that hormone receptor expression is closely related to the clinical tumor lesions and overall survival data. Result:The expression of AR, ER-α and PRLR in tumor tissues were much higher than those in adjacent normal tissues (P>0.05) at both protein and mRNA levels. The higher PRLR level indicate poor survival in LSCC patients (P=0.02), while higher ER-α expression could influence the survival with considerable trend toward significance (P=0.06). Furthermore, the higher expression of ER-α in tumours were corresponding with PRLR cytoplasmic higher level expression (r=0.802, P=0.04). This mutual promoted effect between ER-α and PRLR possibly suggests potential mechanisms among those sex related hormone receptors in laryngeal cancer. Conclusion:It has become increasingly credible that the sex related hormone receptors play an important role in the development of LSCC.

[Preliminary findings for metabolite profiles of papillary thyroid carcinoma and laryngeal squamous cell carcinoma].

Objective:To identify distinct metabolite profiles of papillary thyroid cancer (PTC) and laryngeal squamous cell carcinoma (LSCC).Method:Tumor and adjacent non-tumor specimens were collected from 57 PTC and 33 LSCC patients. Distinct metabolite profiles of tissues were examined using a combination of gas chromatography-time-of-flight mass spectrometry and ultra-performance liquid chromatography-quadrupole-time-of-flight mass spectrometry. The data were analyzed with multivariate statistical analysis to compare the distinct metabolite profiles and related pathways of these three tumors.Result:A panel of 46 and 41 differentially expressed metabolites were identified in tumor and adjacent non-tumor tissues of PTC and LSCC, respectively. Increased glycolysis, amino acids metabolism, one carbon metabolism and tryptophan metabolism were found in these two types of tumor tissues compared to adjacent non tumor tissues. Purine and pyrimidine metabolism was significantly elevated in PTC and LSCC tumor tissues, while taurine and hypotaurine were only higher in PTC tumor tissues. The fatty acid metabolism was detected at lower level in both PTC and LSCC tumor tissue.Conclusion:PTC and LSCC tumor tissues not only have common metabolic signatures characterized by increased glycolysis, amino acids metabolism, one carbon metabolism and tryptophan metabolism, but also have distinct metabolic signatures. It is helpful to understand the nature of these two tumors.

[The characteristic of metabolics of female papillary thyroid carcinoma and its relationship with primary tumor size and cervical lymph node metastases].

OBJECTIVE: To analyze the metabolic profiles of the female papillary thyroid carcinoma (PTC) and the relationship between the metabolic profiles and primary tumor size and cervical lymph node metastasis using a metabolomics approach. METHODS: Forty-three cases of female PTC were enrolled in this study. Gas chromatography-time-of-flight mass spectrometry and ultra performance liquid chromatography-time of flight-mass spectrometry were employed for analyzing metabolic profiles of tumor tissues and adjacent normal tissues in the female PTC. Cases were divided into Group T1 (tumor size≤2.0 cm) and Group T2 (tumor size>2.0 cm) according to the tumor size, and divided into Group N- (with negative cervical lymph node) and Group N+ (with positive cervical lymph node) according to the cervical lymph node conditions. We compared the metabolomic profiles between these groups. RESULTS: A panel of 46 differentially expressed metabolites was identified in the PTC specimens, compared with normal tissues. Increased metabolism of amino acid, purine and pyrimidine, tryptophan acid, one carbon, glycolysis, taurine and hypotaurine, and fatty acid were found in PTC tumors tissues. Amino acids, purine and pyridine, tryptophan, and carbon metabolism increased significantly in the tumor tissues of Group T2 compared with Group T1, while glycolysis, amino acid, purine and pyridine, tryptophan, and carbon metabolism increased significantly in the specimens of Group N+ . CONCLUSION: Distinct metabolic profiles were identified in the female PTC tissues, which were related to the primary tumor size and cervical lymph node metastases.

X-ray structure of azide-bound fully oxidized cytochrome c oxidase from bovine heart at 2.9 A resolution.

Two azide ions were identified, one between the Fe and Cu atoms in the O(2)-reduction site and the other at the transmembrane surface of the enzyme, in the crystal structure of the azide-bound form of bovine heart cytochrome c oxidase at 2.9 A resolution. Two geometries, a mu-1,3 type geometry between the Fe and Cu atoms and a terminal geometry on the Fe atom, are equally possible for an azide ion in the O(2)--reduction site. The other azide molecule was hydrogen bonded to an amide group of an asparagine and a hydroxyl group of tyrosine in a mu-1,1 type geometry. The antisymmetric infrared bands arising from these azide ions, which show essentially identical intensity [Yoshikawa & Caughey (1992), J. Biol. Chem. 267, 9757-9766], strongly suggest terminal binding of the azide to Fe. The electron density of all three imidazole ligands to Cu(B) was clearly seen in the electron-density map of the azide-bound form of bovine heart enzyme, in contrast to the crystal structure of the azide-bound form of the bacterial enzyme [Iwata et al. (1995), Nature (London), 376, 660-669], which lacks one of the three imidazole ligands to Cu(B).

Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.

Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme.