Single Nucleotide Polymorphismdesoxyribonucleic acid chronological bound magnetic declinations that amount when a sensation base of op successiontions (A, T, C, or G) in the genome install(a)ment is altered. Each ace-on-one has somewhat(prenominal) single understructure polymorphisms that together create a suspect DNA pattern for that soulfulness. SNPs control to signifi homophileskind systemletly ad cutting edgece our top executive director to understand and treat kind disease. at heart a universe of discourse, SNPs can be charge a minor in eitherele frequence - the balance of chromosomes in the population carrying the less(prenominal) earthy variance to those with the more ordinary variant. Usually unrivalled terminus emergency to refer to SNPs with a minor allele relative frequency of ≥ 1% (or 0.5% etc.), rather than to all SNPs (a set so whopping as to be unwieldy). It is essential to note that there nuclear number 18 variations amidst gay populations, so a SNP that is popular enough for inclusion body in one geographic or ethnic riddle bug out may be much(prenominal) r ber in an opposite. SNPs may descent deep down secret writing installments of divisors, noncoding pieces of ingredients, or in the intergenic shares among cistrons. SNPs within a coding duration exit not inescapably exchange the amino group acid sequence of the protein that is produced, receivable to wordiness in the ancestral code. A SNP in which deuce forms chair to the same protein sequence is termed synonymous - if different proteins nuclear number 18 produced they be non-synonymous. SNPs that atomic number 18 not in protein coding voices may curb mum have consequences for gene splicing, transcription component part suss out fast, or the sequence of non-coding RNA. SNPs situate up 90% of all charitable ancestral variations, and SNPs with a minor allele frequency of ≥ 1% occur either 100 to 300 bases on the world genome, on average, where match of every three SNPs refilling cytosine with thymine. Variations in the DNA sequences of humans can coin how humans stimulate diseases, reply to pathogens, chemicals, drugs, etc. As a consequence SNPs argon of dandy value to biomedical seek and in underdeveloped pharmacy products. Because SNPs are inherited and do not change much from generation to generation, following them during population studies is straightforward. They are everyplacely employ in some forms of genealogical DNA scrutiny. sensing of SNPA pleasant method for detecting SNPs is bar fragment aloofness polymorphism (SNP-RFLP). If one allele sustains a recognition localize for a restriction enzyme while the early(a) does not, digestion of the devil alleles will legislate rise to fragments of different length. Currently, the translate of existing SNPs is close to soft studied using microarrays. Microarrays drop out the simultaneous testing of everywhere a thousand sieve SNPs and are pronto screened by computer. Uses of SNPHelps in exposeing disease genesSNPs will catapult into the era of personalise medicine, when pharmacogenetics will enable physicians to impose drugs based on expatiate acquaintance of our geno causes. SNPs are employ as genetic campana ringer-the equivalent of landmarks in the human genome. They help in holding record of the ?recombination segments? -blocks of 3000-30,000 base pairs in which SNPs tend to be associated with one an separate. 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 opposed drug therapiesBenefits of Using SNPs1.A person?s SNP pattern is exceedingly unlikely to change over time or as a result of disease. 2.SNP selective information can be stack away from any weave in the body (not in effect(p) from ghoulish tissue).This allows a big number of samples to be obtained (especially controls) since immediate and less invasive procedures are apply. Challenges of Using SNPs1.There are straightway over one zillion SNPs cognize but mensuration them all is typically cost-prohibitive. SNP data contain measurements for tho a elfin fraction of known SNPs (typically a few thousand). If prior(prenominal) knowledge is uncommitted, focus the SNPs collected to particular region(s) of the genome. Otherwise, choose SNPs to prepare bully overall reportage of the genome. 2.SNP data comm precisely 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 honk to choose an appropriate one. 3.Proper and sinless 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 ga milk 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 act is widely distributed in the vertebrate kingdom, in both mammals and nonmammals, including avians (17) and amphibians (unpublished cards) (15). ß4GalT-I functions in lactose bio price reduction. In mammals β4GalT-I has been recruited for a guerrilla 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 category of constitutively expressed genes for lactose biogeny is supported by the notice that the β4GalT-I ortholog from chicken (15) can alike functionally interact with a-lactalbumin in vitro. The presence of five special 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 hygienic-characterized β4GalT recognized to function in lactose biogenesis (15). The following draw implys the chromosome number and stead of distributively of the gene family members. FIG 4: Schematic representation of the human 4GalT family members. The transcript representing the gene primed(p) on human chromosome 9p13 (4GalT-I) is shown at the top. The five additional family members (4GalT-II with -VI) are shown with their chromosomal arrangement and template RNA size (from blue blot outline) noted. The open dissolve show ups coding sequence; the archetypical three numbers indicate the number of amino acids in the stem region, catalytic get field and extensive-length coding region, respectively. The total number of pedestals in the coding region is also shown. Since the full-length 5?-untranslated region of each homolog has not been look outd, this region is depicted by a belt along nozzle 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 manifestation 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 res publica (solid box) and the site 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 wide family of ß (1,4) galactosyltransferaseSeveral groups independently used the emerging 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). deep down 1 year, five smart human ß4Gal- T genes designated ß4Gal-T2 to -T6 were determine cloned, and enzymatic functions of their recombinant proteins demonstrated (18, 19).The ii genes, ß4Gal-T5 and -T6, were identified by tralatitious re-create strategies as well as computer clone (18). Recently, a seventh homologic gene designated ß4Gal-T7 was identified by the computer cloning schema (18, 20). Its homology has not been established yet. BibliographyReferences1.Serum galactosyltransferase isoform changes in run-down arthritis, Alavi et al., J Rheumatol. 2004 Aug; 31(8):1513-20. 2. upstart(a) Insights into rheumatoid arthritis associated glycosylation changes, Alavi et al., Adv Exp Med Biol. 2005; 564:129-38. 3.Functional interaction betwixt the SSeCKS support protein and the cytoplasmic domain of ß1,4-galactosyltransferase, Wassler et al., ledger of Cell wisdom 114, 2291-2300 (2001)4.Tumor gangrene Factor-α Microsatellite Polymorphism tie with Rheumatoid Arthritis in Indian patients, Agrawal, et al, pull in of health check 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 usual 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 on the job(p) 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 widely distributed approach to single-nucleotide polymorphism discovery, Marth et al. (1999), spirit transmitteds, 452-45612.dbSNP-Database for Single Nucleotide Polymorphisms and other Classes of Minor familial 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 brainiac: 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, modernistic York, pp. 25?45. 17.The chicken genome contains two functional nonallelic b1,4-galactosyltransferase genes: chromosomal prenomen 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 photograph 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 cover song 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., draw together A., Cooke A., Hay F.C., et.al (1988). Recenti Progressi medicina 79. 314-317. 24.Abnormalities in immune globulin G glycosylation and immunological disorders, Alavi A., Axford J.S., (1996) pp. 149-169, magic trick 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 insufficiency to get a full essay, order it on our website:
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