Discoidin I, an endogenous lectin, is externalized from Dictyostelium discoideum in multilamellar bodies
نویسندگان
چکیده
Discoidin I, a soluble lectin synthesized by aggregating Dictyostelium discoideum and implicated in their adhesion to the substratum, is localized in multilamellar bodies both intracellularly and upon externalization. These structures also contain a glycoconjugate that binds discoidin I. The multilamellar bodies apparently serve to package the lectin for externalization, and may then gradually release it to function extracellularly.
منابع مشابه
Discoidin I , an Endogenous Dictyostelium discoideum in Lectin , Is Externalized Multilamellar Bodies from
Discoidin I, a soluble lectin synthesized by aggregating Dictyostelium discoideum and implicated in their adhesion to the substratum, is localized in multilamellar bodies both intracellularly and upon externalization. These structures also contain a glycoconjugate that binds discoidin I. The multilamellar bodies apparently serve to package the lectin for externalization, and may then gradually ...
متن کاملIdentification of endogenous binding proteins for the lectin discoidin-I in Dictyostelium discoideum.
Recent biochemical and genetic evidence has shown that the endogenous lectin discoidin-I is involved in intercellular adhesion during development of the cellular slime mold Dictyostelium discoideum. We have prepared discoidin-I affinity columns and used them to isolate the lectin receptors. By using the cell surface radioiodination method, 11 discoidin-I binding proteins were identified in wild...
متن کاملDiscoidin-binding polysaccharide from Dictyostelium discoideum.
Extracts of Dictyostelium discoideum grown axenically in a chemically defined medium were evaluated for binding to discoidin I and discoidin II, endogenous lectins of this slime mold. Binding activity was measured by competitive inhibition of 125I-lactosyl-bovine serum albumin binding to the immobilized lectins. With the solubilization procedure used extracts of vegetative cells and of early ag...
متن کاملCell surface species-specific high affinity receptors for discoidin: developmental regulation in Dictyostelium discoideum.
Vegetative (noncohesive) D. discoideum cells and cells at several stages during the development of cohesiveness were fixed with glutaraldehyde, and their agglutinability by purified carbohydrate-binding proteins (lectins) from slime molds and plants was determined. The two purified lectins from D. discoideum, called discoidin I and II, were poor agglutinins of fixed vegetative D. discoideum ce...
متن کاملInhibition of Dictyostelium discoideum differentiation in monolayers in vitro by endogenous and exogenous lectins.
Spore-cell differentiation in monolayers in vitro of two sporagenous mutants of Dictyostelium discoideum, HM18 and HM15, is markedly inhibited by relatively low concentrations of the exogenous lectins, Concanavalin A (ConA) and wheat germ agglutinin (WGA) and by somewhat higher concentrations of the endogenous lectin, discoidin. The selective inhibition of spore cell formation by ConA occurs to...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of Cell Biology
دوره 100 شماره
صفحات -
تاریخ انتشار 1985