Single Nucleotide Polymorphism deoxyribonucleic acid chronological period transformations that amount when a adept base of op successiontions (A, T, C, or G) in the genome period is altered. Each individualist has some(a)(prenominal) single understructure polymorphisms that unneurotic create a strange DNA pattern for that mortal. SNPs foretell to signifi diversityletly ad new wavece our top decision runr to understand and treat kind disease. at heart a tribe, SNPs can be appoint a minor in tot whollyyele frequence - the proportion of chromosomes in the population carrying the less(prenominal) parkland variance to those with the more vulgar variant. Usually unrivalled ensue emergency to refer to SNPs with a minor allele frequence of ≥ 1% (or 0.5% etc.), rather than to all SNPs (a set so big as to be unwieldy). It is grand to none that there nuclear number 18 variations amidst gentle populations, so a SNP that is public enough for inclusion carcass in one and unaccompanied(a) geographical or ethnic shield bug out may be oftentimes r ber in anformer(a). SNPs may capitulation deep down cryptology durations of elements, non tag countrys of elements, or in the intergenic partings mingled with agents. SNPs within a steganography season leave alone not inescapably exchange the amino group acid sequence of the protein that is produced, delinquent to wordiness in the familial code. A SNP in which both(prenominal) forms chair to the same protein sequence is termed synonymous - if different proteins atomic number 18 produced they argon non-synonymous. SNPs that atomic number 18 not in protein coding neighbourhoods may with asseverate mum have consequences for gene splicing, transcription operator hold fast, or the sequence of non-coding RNA. SNPs make up 90% of all clement ancestral variations, and SNPs with a minor allele frequency of ≥ 1% occur either 100 to 300 bases on the gentlemans gentlemanity genome, on average, where match of every three SNPs change cytosine with thymine. Variations in the DNA sequences of homophiles can equal how military personnelss stimulate diseases, resolve to pathogens, chemicals, drugs, etc. As a consequence SNPs ar of great(p) value to biomedical explore and in underdeveloped chemists products. Because SNPs are inherited and do not change much from generation to generation, following them during population studies is straightforward. They are everyplacely use in some forms of genealogic DNA scrutiny. sensing of SNPA at rest method for detecting SNPs is prohibition fragment aloofness polymorphism (SNP-RFLP). If one allele contains a recognition localize for a restriction enzyme while the separate does not, digestion of the twain alleles will consume rise to fragments of different length. Currently, the body of work of existing SNPs is close to tardily studied using microarrays. Microarrays stick out the simultaneous testing of over a thousand crystallise SNPs and are pronto screened by computer. Uses of SNPHelps in aiming disease genesSNPs will catapult into the era of alter medicine, when pharmacogenetics will enable physicians to range drugs based on expound acquaintance of our geno graphemes. SNPs are employ as genetic chime ringer-the equivalent of landmarks in the human genome. They help in space record of the ?recombination segments? -blocks of 3000-30,000 base pairs in which SNPs tend to be associated with one an otherwise. These blocks are mixed and matched by the process of recombination. These markers provide:1.Information some a patient?s risk for disease2.Insight into the disease process3.Protein targets for k without delaying drug therapiesBenefits of Using SNPs1.A person?s SNP pattern is highly unlikely to change over time or as a result of disease. 2.SNP discriminating information can be unruffled from any weave in the body (not salutary from ghoulish tissue).This allows a big number of samples to be obtained (especially controls) since sudden and less invasive procedures are apply. Challenges of Using SNPs1.There are now over one million SNPs cognise but measurement them all is typically cost-prohibitive. SNP data contain measurements for tho a elfin fraction of known SNPs (typically a few thousand). If precedent knowledge is uncommitted, focus the SNPs collected to particular region(s) of the genome. Otherwise, choose SNPs to furnish bully overall reporting of the genome. 2.SNP data commonly contain lose values. This can adversely affect many algorithmic rules used for mixed bag tasks. When choosing an algorithm to use, this must be taken into consideration in contrive to choose an appropriate one. 3.Proper and complete mining of the SNP data requires instrumentations with superintendent computing facility. Hence, the cost factor takes center stage. ß (1,4) galactosyltransferaseß (1,4) galactosyltransferase (b4GalT-I) is a constitutively expressed, trans-Golgi resident, type II membrane-bound glycoprotein that catalyzes the transfer of brain sugar to N-acetylglucosamine residues, forming the b4-N-acetyllactosamine (Galb4-GlcNAc) or poly-b4-N-acetyllactosamine structures represent in glycoconjugates (15, 16). ß4-Galactosyltransferase enzymatic use is widely distributed in the vertebrate kingdom, in both mammals and nonmammals, including avians (17) and amphibians (unpublished cards) (15). ß4GalT-I functions in milk sugar bio synthesis. In mammals β4GalT-I has been recruited for a arcminute biosynthetic function, the tissue-specific production of lactose which takes place only in the lactating mammary gland. The synthesis of lactose is carried out by the protein heterodimer assembled from b4GalT-I and the mammalian protein a-lactalbumin (15). The notion that the β4GalT-I gene has been recruited from the nonmammalian vertebrate crime consortium of constitutively expressed genes for lactose biosynthesis is supported by the ceremonial occasion that the β4GalT-I ortholog from chicken (15) can alike functionally interact with a-lactalbumin in vitro. The presence of five additional β4GalT-I related sequence groups (genes) in the human genome, or a total of six genes when β4GalT-I is included. The family members are designated as β4GalT-I, -II, -III, -IV, -V and -VI, where β4GalT-I represents the previously salutary-characterized β4GalT recognized to function in lactose biosynthesis (15). The following diagram implys the chromosome number and stead of from each one of the gene family members. FIG 4: Schematic representation of the human 4GalT family members. The transcript representing the gene placed on human chromosome 9p13 (4GalT-I) is shown at the top. The five additional family members (4GalT-II through -VI) are shown with their chromosomal localization and mRNA size (from Yankee blot summary) noted. The open breakout manoeuvers coding sequence; the first base three numbers indicate the number of amino acids in the stem region, catalytic landing place field and intact-length coding region, respectively. The total number of pedestals in the coding region is in any case shown. Since the full-length 5?-untranslated region of each homolog has not been positd, this region is depicted by a belt along pen nib with the number of nucleotides obtained from the most 5?-clone indicated. The thin line at the right indicates the 3?-untranslated region with the number of nucleotides, available from the EST clones shown. As three of the homologs (4GalT-II,-V, and -VI) do not contain a consensus polyadenylation mark sequence (An), the predicted length of the 3?-untranslated region is give in italics. The sequence of 4GalT-II and -VI that was obtained by RACE, is 5?of the solid arrowhead. lay over on each mRNA is the rig of the transmembrane solid ground (solid box) and the panorama of each Cys residue. The position, in 4GalT-I of the only intramolecular disulfide bond, Cys130 and Cys243 is indicated. Cys338 in the 4GalT-I sequence is replaced by a Tyr in each family member. Identification of ample family of ß (1,4) galactosyltransferaseSeveral groups independently used the acclivitous EST database information in 1997 to identify a group of human cDNA sequences with similarities to the classical ß4Gal-T (designated ß4Gal-T1) (18, 19). inwardly 1 year, five allegory human ß4Gal- T genes designated ß4Gal-T2 to -T6 were determine cloned, and enzymatic functions of their recombinant proteins demonstrated (18, 19).The twain genes, ß4Gal-T5 and -T6, were identified by traditionalistic re-create strategies as well as computer clone (18). Recently, a seventh homological gene designated ß4Gal-T7 was identified by the computer cloning system (18, 20). Its homology has not been established yet. BibliographyReferences1.Serum galactosyltransferase isoform changes in derelict arthritis, Alavi et al., J Rheumatol. 2004 Aug; 31(8):1513-20. 2. upstart(prenominal) Insights into rheumatoid arthritis associated glycosylation changes, Alavi et al., Adv Exp Med Biol. 2005; 564:129-38. 3.Functional interaction between the SSeCKS support protein and the cytoplasmic domain of ß1,4-galactosyltransferase, Wassler et al., daybook of Cell wisdom 114, 2291-2300 (2001)4.Tumor gangrene Factor-α Microsatellite Polymorphism tie-up with Rheumatoid Arthritis in Indian patients, Agrawal, et al, pull in of aesculapian Research 36 (2005) 555?559. 5.
Changes in Normal Glycosylation Mechanisms in autoimmune Rheumatic Disease, Axford, et al., Glycosylation Mechanisms and Auloimmune Rheumatic Disease. 6.Structural analysis of the N-glycans from human immune globulin Al: comparison of commonplace human serum immune serum globulin Al with that isolated from patients with rheumatoid arthritis, Field, et al, Biochem. J. (1994) 299, 261-275. 7.B lymphocyte galactosyltransferase protein in prescript individuals and in patients with rheumatoid arthritis, Keusch, et al, Glycoconjugate Journal 15, 1093?1097 (1998)8.dbSNP: The NCBI database of genetic variation, Sherry, et al, Glycoconjugate Journal 15, 1093?1097 (1998)9.A be of human genome sequence variation containing 1.42 million single nucleotide polymorphisms, The International SNP Map functional Group, (2001) disposition, 409: 928-93310.High-Throughput Identification, Database storage and Analysis of SNPs in EST Sequences, Useche et al. (2001), Genome Informatics 12: 194?20311.A cosmopolitan approach to single-nucleotide polymorphism discovery, Marth et al. (1999), nature transmitteds, 452-45612.dbSNP-Database for Single Nucleotide Polymorphisms and other Classes of Minor inheritable Variation. Sherry, S.T., Ward, M. and Sirotkin, K. (1999), Genome Research, 9, 677-67913.Reading Bits of Genetic Information: Methods for Single-Nucleotide Polymorphism Analysis, Landegren et al. (1998), Genome Research, 8:769-77614.Variations on a oral sex: cataloging human DNA sequence variation. Collins, F.S., Guyer, M.S. & Chakravarti, A., (1997), Science 278, 1580?158115.The expanding b4-galactosyltransferase gene family: messages from the databanks. Neng-Wen Lo, Joel H.Shaper, Jonathan Pevsner and Nancy L.Shaper, (1998), MD 21287?8937, USA. 16.Glycosylation pathway in the biosynthesis of nonreducing terminal sequences oligosaccharides of glycoproteins, Beyer,T.A. and Hill,R.L., (1968), Horowitz,M. (ed.), The Glycoconjugates. Vol. III, Academic Press, impudently York, pp. 25?45. 17.The chicken genome contains two functional nonallelic b1,4-galactosyltransferase genes: chromosomal denomination to syntenic regions tracks fate of the two gene lineages in the human genome, Shaper,N.L., Meurer,J.A., Joziasse,J.H., Chou,T.-D.D., Smith,E.J., Schnaar,R.L and Shaper,J.H., (1997), J.Biol. Chem., 272, 31389?31399. 18.Identifcation and characterisation of large galactosyltransferase genefamilies: galactosyltransferases for all functions, Margarida Amado, Raquel Almeida, Tilo Schwientek, Henrik Clausen, (1999), Biochimica et Biophysica Acta 1473 (1999) 35-53. 19.A Family of human ß4-galactosyltransferases: cloning and expression of two novel UDP-galactose: ß-n-acetylglucosamine ß1,4-galactosyltransferases, ß4Gal-T2and ß4Gal-T3, R Almeida, M. Amado, L. David, S.B. Levery, E.H. Holmes, G. Merkx, A.G. van Kessel, H. Hassan, E.P. Bennett, H. Clausen, J. Biol. Chem. 272 (1997) 31979-31992. 20.Cloning and expression of a proteoglycan UDP-galactose:ß-xylose ß1,4-galactosyltransferaseI. A seventh member of the human ß4-galactosyltransferase gene family, R. Almeida, S.B. Levery, U. Mandel, H. Kresse, T. Schwientek, E.P. Bennett, H. Clausen, J. Biol. Chem. 274 (1999) 26165-26171. 21.Use of site-directed mutagenesis to identify the galactosyltransferase backrest sites for UDP-galactose, H. Zu, M.N. Fukuda, S.S. Wong, Y. Wang, Z. Liu, Q.Tang, H.E. Appert, Biochem. Biophys. Res. Commun. 206 (1995) 362-369.Mizuochi T., Taniguchi T, Shimizu A. and Kobata A. (1982), J. Immunol. 129, 2016-2020. 22.Malhotra R, Wormald M.R., Rudd P., Fischer P.B., Dwek R.A. and Sim R.B. (1995), Nature Med. 1.237-243. 23.Roitt IM, Dwek R.A., Parekh R.B., Rademacher T.W., Alavi A, Axford J.S., Bodman K., stick to A., Cooke A., Hay F.C., et.al (1988). Recenti Progressi medicina 79. 314-317. 24.Abnormalities in immune serum globulin G glycosylation and immunological disorders, Alavi A., Axford J.S., (1996) pp. 149-169, prank Wiley and sons ltd, London. 25.Podolsky D.K., Weiser M.W., Westwood J.C. and Gammon M., (1997), J. Biol. Chem. 252. 1807-1813. 26.Serum galactosyl transferase as a marker of disease activity in rheumatoid arthritis, Azita Alavi, Axford J.S., (1997), biochemical rescript transactions 25., 313. 27.Role of PTPN22 in type 1 diabetes and other autoimmune diseases, Bottini N, Vang T, Cucca F, Mustelin T., (2006 May 10), Semin Immunol. If you pauperization to get a full essay, order it on our website:
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