caa a22 4500 475773152 CHVBK 20180406123623.0 cr unu---uuuuu 170329e20001001xx s 000 0 eng 10.1007/s001250051550 doi (NATIONALLICENCE)springer-10.1007/s001250051550 Genomic structure of mouse IA-2: comparison with its human homologue [Elektronische Daten] [K. Saeki, J. Xie, A. L. Notkins] Aims/hypothesis. IA-2 is a transmembrane protein with a tyrosine phosphatase (PTP)-like structure and a major autoantigen in Type I (insulin-dependent) diabetes mellitus. Because the nucleotide sequence of human and mouse IA-2 cDNA are closely related, it seemed likely that the genomic organization of the two molecules would be similar. To test this possibility the current experiments were initiated to characterize and compare the genomic structure of mouse and human IA-2.¶Methods. IA-2 cDNA was used to screen a 129SVJ mouse genomic library. We selected and mapped 7 overlapping clones. The subcloned inserts were used to determine intron-exon junctions by direct sequencing. Polymerase chain reaction and restriction mapping were used to estimate the size of the introns.¶Results. The mouse IA-2 gene and the 5' upstream regulatory region were isolated and the intron-exon junctions determined. Mouse IA-2 encompasses approximately 20 kb and encodes 23 exons. Both the 3' and 5' ends were mapped by rapid amplification of cDNA ends (RACE) and a 2 kb 5'-upstream region was shown to have functional promoter activity.¶Conclusion/interpretation. Comparison of the genomic structure of mouse and human IA-2 shows that they have the same number of exons and nearly identical intron-exon junctions. The region around the major transcription start site of mouse IA-2 is similar to human IA-2 and other transmembrane protein tyrosine phosphatases. It is concluded that human and mouse IA-2 are highly conserved and derived from a common ancestral gene. [Diabetologia (2000) 43: 1429-1434] Springer-Verlag Berlin Heidelberg, 2000 KeywordsIA-2, insulin-dependent diabetes mellitus, autoantibodies, genomic structure, protein tyrosine phosphatase, intron-exon junctions nationallicence Saeki K. Experimental Medicine Section, Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland, USA, US aut Xie J. Experimental Medicine Section, Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland, USA, US aut Notkins A. L. Experimental Medicine Section, Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland, USA, US aut https://doi.org/10.1007/s001250051550 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s001250051550 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Saeki K. Experimental Medicine Section, Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland, USA, US aut NATIONALLICENCE 700 1- Xie J. Experimental Medicine Section, Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland, USA, US aut NATIONALLICENCE 700 1- Notkins A. L. Experimental Medicine Section, Oral Infection and Immunity Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland, USA, US aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer