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In the tumor microenvironment, amino acids are important nutrients constituting immune cells and tumor cells. Some proteins or key enzymes in the metabolism process are expected to become tumor diagnostic markers or therapeutic targets. It was found that the contents of some amino acids were obviously different between normal people and gastric cancer patients. Amino acid metabolism has also been confirmed to be involved in the activation of the PI3K/AKT/mTOR pathway, which is one of the main pathways regulating the growth, proliferation, division and autophagy of tumor cells. Amino acid metabolism can be used as a signal molecule to affect the occurrence, development and prognosis of gastric cancer by activating related targets of this pathway. In addition, amino acid metabolism plays an important biological role in the activation and differentiation of immune cells, which can affect the immune function of tumors by regulating immune cells and immune factors.

The 4th edition of WHO Classification of Head and Neck Tumours has been published in Jan. 2017. In Chapter 8‘Odontogenic and maxillofacial bone tumours’, the classification of odontogenic tumors was recomposed from the previous edition in 2005. In this paper, we introduced the modification of odontogenic tumors classification between 2017 and 2005 in a comprehensive discussion.

Objective: To analyze a pathogenic variant of MEFV gene in a family with autosomal dominant-familial Mediterranean fever (AD-FMF)., Methods: A 5-year-old boy presented with recurrent aseptic meningitis and his major symptoms included recurrent fever with headache and vomiting. His family members including his mother, sister and brother also had recurrent fever. A genetic disease was considered. DNAs were extracted from patient and all his family members' blood samples. Whole exome sequencing was performed to identify putative pathogenic variants that can explain this family's condition and Sanger sequencing was conducted. The impact of detected variants were predicted and validated by bioinformatics., Results: A missense variant c.2229C>G (p.Phe743Leu) in MEFV gene was identified in the proband and his family members including his mother, sister and brother. This variant had not been reported in China previously, but the locus of it had already been reported in Arabic patient with AD-FMF (PS1). This variant was absent in major allele frequency databases (PM2) and had been predicted to be pathogenic based on Mutationtaster, PROVEAN and PolyPhen-2. In addition, the change of amino acid, locating in 743 locus of pyrin protein, encoding by MEFV gene, was found to cause SPRY_PRY_TRIM20 and SPRY_superfamily domain destroyed and finally influenced the fuction of pyrin protein. On the other hand, using UCSF chimera software, we find the variant c.2229C>G (p.Phe743Leu) can induce serious influence to the spatial structure of pyrin protein and loss of protein fuction (PP3). According to the ACMG variant classification guideline, the variant c.2229C>G (p.Phe743Leu) in MEFV gene was classified as likely pathogenic (PS1+PM2+PP3)., Conclusion: The condition of this AD-FMF family may be attributed to the missense variant c.2229C>G (p.Phe743Leu) in MEFV gene. The recurrent aseptic meningitis was a very rare manifestation in AD-FMF patients and had not been reported in China previously. The clinical and genetic findings of the present study are helpful for the further understanding of AD-FMF.

Objective: To detect pathogenic variant of ARSA gene in an infant with late infantile metachromatic leukodystrophy (MLD)., Methods: The male proband had an onset of walking dysfunction and seizure at 28 months. Arylsulfatase A activity of his peripheral blood leucocytes was 26.9 nmol/mg.17h, and cranial MRI showed wild symmetrical demyelination. With genomic DNA extracted from his peripheral blood sample, all coding exons and splicing sites of the ARSA gene were subjected to Sanger sequencing. PubMed Protein BLAST system was employed to analyze cross-species conservation of the mutant amino acid. Ucsf chimera software was used to analyze the impact of candidate variants on the secondary structure of the protein product. Impact of potential variants was also analyzed with software including PolyPhen-2, Mutation Taster, SIFT and PROVEAN. Whole-exome sequencing was carried out to identify additional variants which may explain the patient's condition., Results: The proband was found to harbor compound heterozygous variants of the ARSA gene [c.467G>A (p.Gly156Asp) and c.960G>A (p.Trp320*)], neither of which was reported previously. As predicted by Ucsf chimera software, the c.960G>A (p.Trp320*) variant may demolish important secondary structures including α-helix, β-strand and coil of the ARSA protein, causing serious damage to its structure and loss of function. The c.467G>A (p.Gly156Asp) variant was predicted to be "probably damaging" by PolyPhen-2, Mutation Taster and SIFT software., Conclusion: The patient's condition may be attributed to the compound heterozygous c.467G>A (p.Gly156Asp) and c.960G>A (p.Trp320*) variants of the ARSA gene. Above results have facilitated genetic counseling and prenatal diagnosis for this family.

Objective: To detect potential mutations of HEXB gene in an infant with Sandhoff disease (SD)., Methods: Genomic DNA was extracted from peripheral blood sample of the infant. All coding exons (exons 1 to 14) and splicing sites of the HEXB gene were subjected to PCR amplification and direct sequencing.PubMed Protein BLAST system was employed to analyze cross-species conservation of the mutant amino acid. PubMed BLAST CD-search was performed to identify functional domains destroyed by thecandidate mutations. Impact of the mutations was analyzed with software including PolyPhen-2, Mutation Taster and SIFT. Whole-exome sequencing was carried out to identify additional mutations., Results: The infant was found to carry compound heterozygous mutations c.1652G>A(p.Cys551Tyr) and c.1389C>G (p.Tyr463*) of the HEXB gene. The c.1389C>G (p.Tyr463*) mutation may lead to destruction of two functional domains in β subunit of the Hex protein. The c.1652G>A(p.Cys551Tyr) mutation, unreported previously,was predicted to be probably damaging by Bioinformatic analysis., Conclusion: Compound heterozygous mutations c.1652G>A(p.Cys551Tyr) and c.1389C>G (p.Tyr463*) in the HEXB gene probably underlie the disease in this patient.

Objective: To identify potential mutation of PMM2 gene in an infant with congenital disorders of glycosylation type 1a (CDG-1a)., Methods: Genomic DNA was extracted from peripheral blood sample of the patient. All coding exons (exons 1-8) and splicing sites of the PMM2 gene were amplified with PCR. Potential variants were detected by direct sequencing of the PCR products and comparing the results against the ESP and SNP human gene databases. A protein BLAST system was employed to analyze cross-species conservation of the variants amino acid. A PubMed BLAST CD-search system was employed to identify functional domains damaged by variants of the PMM2 gene. Impact of potential variants was analyzed using software including PolyPhen-2 SIFT and Mutation Taster. Whole exome sequencing was used to identify additional variants of the PMM2 gene which may explain the condition of the patient., Results: The child was found to carry compound heterozygous variants (c.458_462delTAAGA and c.395T>C) of the PMM2 gene, which were inherited respectively from his father and mother. The c.458_462delTAAGA has not been reported previously and may result in disruption of 10 functional domains within the PMM2 protein. The c.395T>C mutation has been recorded by a SNP database with frequency unknown. Both mutations were predicted as "probably damaging". Whole exome sequencing has identified no additional disease-causing variant which can explain the patient's condition., Conclusion: The patient's condition may be attributed to the compound heterozygous variants c.458_462delTAAGA and c.395T>C of the PMM2 gene. Above results has facilitated molecular diagnosis for the patient.

Objective: To explore the effectiveness and operation method of the superficial branch of radial artery wrist crease flap for repair of ring tissue defect of the fingers., Methods: Between June 2013 and March 2016, the superficial branch of radial artery wrist crease flap was used to repair ring finger tissue defect in 20 cases (21 fingers). There were 14 males and 6 females with an average age of 39.3 years (range, 12-61 years). The causes included machine injury in 9 cases, traffic accident injury in 6 cases, heat inury in 2 cases, and avulsed injury in 3 cases. The index finger was involved in 6 cases, middle finger in 6 cases, ring finger in 3 cases, and little finger in 6 cases. Combined injuries included exposure of bone, tendon, vessel, and nerve. The mean time of injury to operation was 3 hours (range, 0.5-5.5 hours) in 17 patients undergoing emergency operation, and was 8.5 days (range, 7-10 days) in 3 patients undergoing selective operation. The superficial palmar branch of the radial artery from the flap was used for bridging proper digital artery. The donor site was directly sutured in 19 cases and was repaired by skin grafting in 1 case., Results: One case had blood blister at distal flap, which was cured after dressing change; the other flaps survived, and primary healing was obtained. Healing of incision at the donor site healed by first intention. The patients were followed up 6-24 months (mean, 12 months). The appearance, texture, and color of the flaps were satisfactory. The two-point discrimination ranged from 6 to 13 mm (mean, 9 mm) at 6 months after operation. According to the Chinese Medical Association Society of hand surgery of thumb and finger reconstruction function evaluation standard, the results were excellent in 13 cases, good in 4 cases, and fair in 3 cases; the excellent and good rate was 85%., Conclusion: The superficial branch of radial artery wrist crease flap is an ideal choice for the repair of ring tissue defect of the fingers.

Since its invention in 1970s, nucleic acid sequencing technology has contributed tremendously to the genomics advances. The next-generation sequencing technologies, represented by HiSeq 2000 from Illumina, SOLiD from Applied Biosystems and 454 from Roche, re-energized the application of genomics. In this review, we first introduced the next-generation sequencing technologies, then, described their potential applications in the field of microbiology.

Objective: To discover the etiology of allergic rhinitis(AR) at the genomic level., Methods: Microarray analysis on a genomic scale was used to find changes in genes expression in AR. The total RNAs were isolated from nasal mucosa of AR and normal, then purified to mRNAs and were reversely transcribed to cDNAs with the incorporation of fluorescent-labeled dUTP to prepare for the hybridization probes. The genes differential expressed in AR were screened with the gene chip which contained 12,800 human genes in all 8 samples., Result: 734 genes were shown in differential expressed profile with 430 upregulated genes and 304 downregulated genes, and all 8 samples were 15 genes upregulated and 6 genes downregulated. The differential expressed genes involved in the functions of inflammation, immunology, neuroendocrine and signal conduct, and they had potential value in AR study., Conclusion: The investigation based on gene chip in researching related genes in AR afforded a new idea in studying pathogenesis of nasal allergic diseases.