• 검색어에 아래의 연산자를 사용하시면 더 정확한 검색결과를 얻을 수 있습니다.
  • 검색연산자
검색연산자 기능 검색시 예
() 우선순위가 가장 높은 연산자 예1) (나노 (기계 | machine))
공백 두 개의 검색어(식)을 모두 포함하고 있는 문서 검색 예1) (나노 기계)
예2) 나노 장영실
| 두 개의 검색어(식) 중 하나 이상 포함하고 있는 문서 검색 예1) (줄기세포 | 면역)
예2) 줄기세포 | 장영실
! NOT 이후에 있는 검색어가 포함된 문서는 제외 예1) (황금 !백금)
예2) !image
* 검색어의 *란에 0개 이상의 임의의 문자가 포함된 문서 검색 예) semi*
"" 따옴표 내의 구문과 완전히 일치하는 문서만 검색 예) "Transform and Quantization"
쳇봇 이모티콘
ScienceON 챗봇입니다.
궁금한 것은 저에게 물어봐주세요.

논문 상세정보

Molecular divergence of the fish somatomedins: the single family of insulin­like growth factor (IGF)-I and -II from the teleost, flounder


The teleosts represent ancient real-bony vertebrates in phylogeny and resemble major genetic patterns to higher vertebrates. In the present study, we have defined the single family of insulin-like growth factors (IGFs) from flounder (Paralichthys olivaceus), compared to the prototype of IGFs observed in the Agnathan hagfish. In flounder, IGFs are clearly diverged into two major types including type I and II, and they are structurally similar by displaying a multidomain structure consisting of five functional regions as previously found in other vertebrates. However, flIGF-I appears to be more basic (pI 8.03) than the flIGF-II (pI 5.34) in the fully processed form for the B to D domain region. The flIGF-I seems to contain an evolutionary conserved Asn-linked glycosylation in E domain, which is not found in flIGF­II. The most interesting feature is that flIGF-II appeared to be structurally close to hagfish IGF in secondary structures, particularly in Band D domains. This could tell us an idea on the molecular divergence of IGFs from the Agnatha to teleosts during the vertebrate phylogeny. It also support, in part, a notion regarding on how IGF-II is appeared as more embryonic during development. Nonetheless, the biologically active B to D domain region of flIGF-II shows significant sequence homology of $65.6\%$ to flIGF-Is and contains the evolutionary conserved insulin-family signature, as well as a reserved recognition site (Lys) in D domain, necessary to generate proteolytic cleavage for E-peptide. A significant structural difference was found in E domain in which flIGF-I possesses two potential alternative splicing donor site at $Val^{17,\;24}$ of E domain. Therefore, it seems so far that IGF-I sorely produces spliced variants due to the spliced E-peptide moiety while IGF-II appears to be maintained in a single type during evolution. IGF-II, however, may be also possible to transcribe unidentified variants, depending on the physiological conditions of tissues in vertebrates in vivo.

참고문헌 (0)

  1. 이 논문의 참고문헌 없음

이 논문을 인용한 문헌 (0)

  1. 이 논문을 인용한 문헌 없음


원문 PDF 다운로드

  • ScienceON :

원문 URL 링크

원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다. (원문복사서비스 안내 바로 가기)

상세조회 0건 원문조회 0건

DOI 인용 스타일