A secreted protein is an endogenous chemorepellant in Dictyostelium discoideum
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چکیده
منابع مشابه
A secreted protein is an endogenous chemorepellant in Dictyostelium discoideum.
Chemorepellants may play multiple roles in physiological and pathological processes. However, few endogenous chemorepellants have been identified, and how they function is unclear. We found that the autocrine signal AprA, which is produced by growing Dictyostelium discoideum cells and inhibits their proliferation, also functions as a chemorepellant. Wild-type cells at the edge of a colony show ...
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We have previously demonstrated that nitric oxide (NO)-generating compounds inhibit D. discoideum differentiation by preventing the initiation of cAMP pulses (Tao, Y., Howlett, A. and Klein, C. (1996) Cell. Signal. 8, 37-43). In the present study, we demonstrate that cells produce NO at a relatively constant rate during the initial phase of their developmental cycle. The addition of oxyhemoglob...
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When cells of Dictyostelium discoideum are starved they aggregate to form multicellular organisms that eventually can differentiate into fruiting bodies of spores and stalk cells, cAMP plays a dual role in this process: it is the chemotactic agent that allows cells on a moist surface to aggregate to a common point to form the multicellular organism [1], and it is also involved in the process of...
متن کاملDiscoidin 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 کاملDiscoidin I, an endogenous lectin, is externalized from Dictyostelium discoideum in multilamellar bodies
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 ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2012
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1206350109