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Kim, Ek-Yune,Kim, Young-Hyun,Ryu, Chung-Hun,Lee, Jae-Woong,Kim, Sang-Hyun,Lee, Sang-Rae,Kim, Myeong-Su,Kim, Wan-Jun,Lim, Jeong-Mook,Chang, Kyu-Tae The Korean Society of Animal Reproduction 2008 Reproductive & developmental biology Vol.32 No.1
Members of the Vps (Vacuolar protein sorting) protein family involved in the formation of the retromer complex have been discovered in a variety of species such as yeast, mouse, and human. A mammalian retromer complex is composed of Vps26, Vps29, and Vps35 proteins and plays and important role in cation-independent mannose-6-phosphate receptor retrieval from the endosome to the trans-Golgi network. In this study, we have identified the full-length sequences of the retromer components of Vps26, Vps29, and Vps35 in micro pigs. The cDNA sequences of these retromer components have been determined and the result showed there is 99% homology among the component counterparts from mouse, micro pigs, and humans. In addition, the retromer complexes formed with hetero-components were found in the brain of micro pigs. Based on above results, we suggest mammalian Vps components are well conserved in micro pigs.
Kim, Ek-Yune,Lee, Young-Jeon,Kim, Ji-Su,Song, Bong-Seok,Kim, Sun-Uk,Huh, Jae-Won,Lee, Sang-Rae,Kim, Sang-Hyun,Hong, Yong-Geun,Chang, Kyu-Tae Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.30 No.5
V-set and immunoglobulin domain containing 1 (VSIG1) is a newly discovered member of the junctional adhesion molecule (JAM) family; it is encoded by a gene located on human chromosome X and preferentially expressed in a variety of cancers in humans. Little is known about its physiological function. To determine the role(s) of VSIG1 in mammalian spermatogenesis, we first generated a specific antibody against mouse VSIG1 and examined the presence and localization of the protein in tissues. RT-RCR and Western blot analysis of the mouse tissues indicated that VSIG1 was specifically expressed in the testis. Furthermore, the results of our trypsinization and biotinylation assays strongly support the assumption that VSIG1 is localized on the testicular germ cell surface. In order to determine whether VSIG1 is capable of participation in homotypic interactions, we performed a GST-pull down assay by using recombinant GST-fusion and Histagging proteins. The pull-down assay revealed that each GST-fusion Ig-like domain shows homotypic binding. We further show that mVSIG1 can adhere to the Sertoli cells through its first Ig-like domain. To identify the protein that interacted with cytoplasmic domain, we next performed co-immunoprecipitation analysis. This analysis showed that ZO-1, which is the central structural protein of the tight junction, is the binding partner of the cytoplasmic domain of mouse VSIG1. Our findings suggest that mouse VSIG1 interacts with Sertoli cells by heterophilic adhesion via its first Ig-like domain. In addition, its cytoplasmic domain is critical for binding to ZO-1.
Cystein-Aβ42 폴리펩티드가 β-아밀로이드의 응집력에 미치는 영향
김익균 ( Ek Yune Kim ) 대구가톨릭대학교 자연과학연구소 2013 자연과학연구논문집 Vol.11 No.1
Alzheimer``s disease (AD) is a neurodegenerative disease caused by the deposition of Ab plaque in the brain. β-secretase known as BACE-1 and g-secretase have been identified as the key proteases responsible for processing the Amyloid Precurs or Protein(APP) to the 40 or 42 residue β-amyloid peptide(Aβ). Albeit the deposition of Aβ is a crucial role in AD, but little is known about regarding of its accumulation process. In this study, we have produced recombinant cystein- A β 42 polypeptide and demonstrated its possible role in deposition of Aβ plaque in invitro level. The cystein- Aβ 42 subject showed two high molecules bands compare to control subject. These results might imply that the aggregated forms of cysteine coupled Aβ 42 may use development of amyloid β-protein yields novel therapies for Alzheimer disease.
Alu-Derived Old World Monkeys Exonization Event and Experimental Validation of the LEPR Gene
Huh, Jae-Won,Kim, Young-Hyun,Kim, Dae-Soo,Park, Sang-Je,Lee, Sang-Rae,Kim, Sang-Hyun,Kim, Ek-Yune,Kim, Sun-Uk,Kim, Myeong-Su,Kim, Heui-Soo,Chang, Kyu-Tae Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.30 No.3
The leptin receptor (LEPR) is a crucial regulatory protein that interacts with Leptin. In our analysis of LEPR, novel AluJb-derived alternative transcripts were identified in the genome of the rhesus monkey. In order to investigate the occurrence of AluJb-derived alternative transcripts and the mechanism underlying exonization events, we conducted analyses using a number of primate genomic DNAs and adipose RNAs of tissue and primary cells derived from the crab-eating monkey. Our results demonstrate that the AluJb element has been integrated into our common ancestor genome prior to the divergence of simians and prosimians. The lineage-specific exonization event of the LEPR gene in chimpanzees, orangutans, and Old World monkeys appear to have been accomplished via transition mutations of the 5' splicing site (second position of C to T). However, in New World monkeys and prosimians, the AluJb-related LEPR transcript should be silenced by the additional transversion mutation (fourth position of T to G). The AluJb-related transcript of human LEPR should also be silenced by a mutation of the 5' splicing site (first position of G to A) and the insertion of one nucleotide sequence (minus fourth position of A). Our data suggests that lineage-specific exonization events should be determined by the combination event of the formation of splicing sites and protection against site-specific mutation pressures. These evolutionary mechanisms could be major sources for primate diversification.