Yoshikazu Takada's research while affiliated with The Scripps Research Institute and other places

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Publications (2)

Figure 1. 
Figure 2. Analysis of ADAM 23 expression in human tissues and cell...
Figure 3. 
Figure 5. 
+3 Figure 6. Analysis of ADAM 23 interaction with cell lines expressing...
ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanism
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  • May 2000
ADAM 23 (a disintegrin and metalloproteinase domain)/MDC3 (metalloprotease, disintegrin, and cysteine-rich domain) is a member of the disintegrin family of proteins expressed in fetal and adult brain. In this work we show that the disintegrin-like domain of ADAM 23 produced in Escherichia coli and immobilized on culture dishes promotes attachment o...
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... Many of them involve formation or disruption of tight connections between somatic cells, gametes, embryos, and reproductive organs, and thus it strongly depends on adhesion abilities. The process of biological adhesion is indispensable for intercellular communication, signal transduction, proliferation, or apoptosis [4]. Cellular connections include: cytoskeleton-involving adherens junctions (AJs), formed by integrins, cadherins, and desmosomes [5]; selective tight junctions, controlling the molecular, and ionic flow, made up of claudins and occludins [6]; and lastly, gap junctions, based on connexins, allowing small substance flow between adjacent cells [7]. ...
Reference: “Biological Adhesion” is a Significantly Regulated Molecular Process during Long-Term Primary In Vitro Culture of Oviductal Epithelial Cells (Oecs): A Transcriptomic and Proteomic Study
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... In addition, studies have confirmed the adhesive and binding propensity/preference of the D domain to integrins on certain membranes and cell surfaces. This is also the case with synthetic peptides carrying the ECD sequence (Kamiguti et al., 1997;Cal et al., 2000;Mariano-Oliveira et al., 2003). It has therefore been postulated that the D domain could possibly bind to a surface receptor (e.g., an integrin), thereby positioning the C domain for target recognition and both domains synergistically positioning the M domain to its protein substrate. ...
Reference: Type-I like metalloproteinase in the venom of the West African saw-scaled carpet viper (Echis ocellatus) has anti-trypanosomal activity against African trypanosomes
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