다중혈관 관상동맥 환자에서 y-문합을 이용하여 양쪽 내흉동맥만을 사용한 우회술의 조기 성적

抗原变异可使得多种致病微生物易于逃避宿主免疫应答。表达在感染红细胞表面的恶性疟原虫红细胞表面蛋白1（PfPMP1）与感染红细胞、内皮细胞、树突状细胞以及胎盘的单个或多个受体作用，在黏附及免疫逃避中起关键的作用。每个单倍体基因组var基因家族编码约60种成员，通过启动转录不同的var基因变异体为抗原变异提供了分子基础。

疟原虫var基因转换速率变化导致抗原变异[英]／Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A

Recent data have expanded the concept that inflammation is a critical component of tumour progression. Many cancers arise from sites of infection, chronic irritation and inflammation. It is now becoming clear that the tumour microenvironment, which is largely orchestrated by inflammatory cells, is an indispensable participant in the neoplastic process, fostering proliferation, survival and migration. In addition, tumour cells have co-opted some of the signalling molecules of the innate immune system, such as selectins, chemokines and their receptors for invasion, migration and metastasis. These insights are fostering new anti-inflammatory therapeutic approaches to cancer development.

Inflammation and cancer

Statistical method for testing the neutral mutation hypothesis by DNA polymorphism.

Integrins: versatility, modulation, and signaling in cell adhesion.

The present invention relates to a method of detecting anti-Neu5Gc specific antibodies in a biological material comprising the steps of: 
(a) determining the amount of anti-Neu5Ac antibodies present in the material using Neu5Ac as an antigen target; 
(b) determining the amount of anti-Neu5Gc antibodies present in the material using anti-Neu5Gc as an antigen target; and 
(c) subtracting the amount of anti-Neu5Ac antibodies from the amount of anti-Neu5Gc antibodies to determine the amount of anti-Neu5Gc specific antibodies.

Methods for detecting and analyzing n-glycolylneuraminic acid (Neu5Gc) specific antibodies in biological materials

Lung Inflammation in Mice Siglec-F Ligand Formation and Eosinophilic Sialyltransferase ST3Gal-III Regulates

The O-GlcNAc modification involves the attachment of single -O-linked N-acetylglucosamine residues to serine and threonine residues of nucleocytoplasmic proteins. Interestingly, previous biochemical and structural studies have shown that O-GlcNAcase (OGA), the enzyme that removes O-GlcNAc from proteins, has an active site pocket that tolerates various N-acyl groups in addition to the N-acetyl group of GlcNAc. The remarkable sequence and structural conservation of residues comprising this pocket suggest functional importance. We hypothesized this pocket enables processing of metabolic variants of O-GlcNAc that could be formed due to inaccuracy within the metabolic machinery of the hexosamine biosynthetic pathway. In the accompanying paper (Bergfeld, A. K., Pearce, O. M., Diaz, S. L., Pham, T., and Varki, A. (2012) J. Biol. Chem. 287, 28865–28881), N-glycolylglucosamine (GlcNGc) was shown to be a catabolite of NeuNGc. Here, we show that the hexosamine salvage pathway can convert GlcNGc to UDP-GlcNGc, which is then used to modify proteins with O-GlcNGc. The kinetics of incorporation and removal of O-GlcNGc in cells occur in a dynamic manner on a time frame similar to that of O-GlcNAc. Enzymatic activity of O-GlcNAcase (OGA) toward a GlcNGc glycoside reveals OGA can process glycolyl-containing substrates fairly efficiently. A bacterial homolog (BtGH84) of OGA, from a human gut symbiont, also processes O-GlcNGc substrates, and the structure of this enzyme bound to a GlcNGcderived species reveals the molecular basis for tolerance and binding of GlcNGc. Together, these results demonstrate that analogs of GlcNAc, such as GlcNGc, are metabolically viable species and that the conserved active site pocket of OGA likely evolved to enable processing of mis-incorporated analogs of O-GlcNAc and thereby prevent their accumulation. Such plasticity in carbohydrate processing enzymes may be a general feature arising from inaccuracy in hexosamine metabolic pathways.

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups-O-LINKEDN-GLYCOLYLGLUCOSAMINE(GlcNGc),UDP-GlcNGc,AND THEBIOCHEMICALANDSTRUCTURALRATIONALEFORTHESUBSTRATETOLERANCEOF -O-LINKED-N-ACETYLGLUCOSAMINIDASE *

of streptococcal SRR glycoproteins

We are very glad to read of Dr. Previc’s enthusiasm for our recent findings on thyroid hormone differences between humans and great apes (Gagneux et al., 2001). We are responding herewith to some of the interesting issues that he has raised. Our paper presented human-ape comparative results on plasma thyroid hormone levels and levels of transthyretin (TTR) in plasma and cerebrospinal fluid (CSF). Given the crucial role of thyroid hormone in brain development, we suggested that developmental studies of humans and great ape thyroid hormone levels are warranted, especially for the CSF/brain side of the blood brain barrier. We did not hypothesize about how such hormonal differences originally came about. Extrapolating from currentday human-ape differences to the series of events that brought about these changes sometime during our evolutionary past is fraught with difficulty. However, we are glad if our results provide potential support to other existing hypotheses. Increased consumption of animal foods and frequent strenuous exercise may indeed have played a crucial role in resetting dopaminergic levels in hominoids, as proposed by Dr. Previc’s extensively researched paper on this subject (Previc, 1999). However, it is also evident that present-day humans can achieve aboveaverage cognitive capacities in the absence of meatrich diets or increased physical activity levels. As far

http://pathology.ucsd.edu/faculty/labs/gagneux/pascal_papers_files/Gagneux%26Varki2002AJPA.pdf

Ajit Varki

Papers

Methods for detecting and analyzing n-glycolylneuraminic acid (Neu5Gc) specific antibodies in biological materials

Lung Inflammation in Mice Siglec-F Ligand Formation and Eosinophilic Sialyltransferase ST3Gal-III Regulates

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups-O-LINKEDN-GLYCOLYLGLUCOSAMINE(GlcNGc),UDP-GlcNGc,AND THEBIOCHEMICALANDSTRUCTURALRATIONALEFORTHESUBSTRATETOLERANCEOF -O-LINKED-N-ACETYLGLUCOSAMINIDASE *

of streptococcal SRR glycoproteins

Reply to comments by Previc: Endocrine differences between humans and great apes—Did environmental factors provide genetic opportunities?