Characterization and functional analysis of human Galectin-7 and it's homologue of invertebrate.

Abstract

갈렉틴은 β-galactose에 특이적으로 부착하는 animal lectin의 하나로, 척추동물 및 무척추동물에서도 발견되는 단백질이다. 갈렉틴-7은 인간 피부세포에서 발견된 단일 CRD를 가진 15kDa의 단백질이며, p53에 의해 유도된다고 보고된바 있다. 하지만 p53이 변형된 HaCaT세포에서 UV조사에 의해 p53유전자의 발현과는 상관없이 발현되는 것을 확인하였고, 이는 HaCaT세포에서의 갈렉틴-7은 p53이 아닌 다른 유전자에 의해 발현이 조절되어지는 것으로 생각된다. 그리고 갈렉틴-7의 생물학적 기능에 중요하게 작용할 것으로 추론되는 CRD부위와 Dimer부위를 변형시킨 결과, 갈렉틴-7의 활성이 저해되었다. 또한 무척추동물 바지락으로부터 생체방어/면역에 관련될 것으로 추론되는 갈렉틴을 분리하였으며, Vibrio균에 감염된 바지락에서 갈렉틴이 발현 됨을 확인하였다. 갈렉틴은 척추동물 및 무척추동물에서 생체방어 또는 생존에 관련된 역할을 하며, 갈렉틴의 CRD부위와 Dimer부위가 이러한 역할에 중요하게 작용 할 것이다.

Galectins are a growing family of β-galactose-binding animal lectin. Galectins were initially found in vertebrate, But they have recently been isolated from much lower invertebrates. One member of the galectin family, galectin-7 is a 15kDa protein with a single CRD domain initially identified in human epidermis. It has been identified as one of the p53 inducer genes Invertebrates lack possess an adaptive immune system. Invertebrate galectin acts as body-protection factors in body fluids. I confirmed whether that human galectin-7 and marine invertebrate galectin were expressed against external stimulus. Galectin-7 was controlled p21 after UV irradiation in HaCaT cells. It seems that galectin-7 in HaCaT cells was controlled other gene, not p53. Also galectin was expressed in manila clam infected Vibrio. These means that galectin was importantly associated both vertebrate and invertebrate survival. The carbohydrate recognition of galectin-7 is very important factor at cell adhesion, and carbohydrate binding of galectin-7 is affected by dimerization. A homology analysis based on the correspondence of manila clam galectin and galectin-7 and other organisms showed that carbohydrate-binding sites aligned almost. And galectin-7 and McGal had 25% homology.