Endogenous cleavage of annexin I generates a truncated protein with a reduced calcium requirement for binding to neutrophil secretory vesicles and plasma membrane
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 1468, Issue: 1, Page: 231-238
2000
- 9Citations
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations9
- Citation Indexes9
- CrossRef8
Article Description
We have earlier shown that an N-terminal truncated annexin I molecule, annexin I des1–8, is generated in human neutrophils through cleavage by a membrane localized metalloprotease. The truncated protein showed differences in membrane binding among the neutrophil granule populations as compared to full-length annexin I. In this study, we investigated the cleavage capabilities of isolated neutrophil secretory vesicles and plasma membrane, and the binding of full-length annexin I and annexin I des1–8 to these membrane fractions. Translocations were performed in vitro to secretory vesicles and plasma membrane, respectively, at different Ca 2+ concentrations. We show that the annexin I-cleaving membrane localized metalloprotease is present both in the secretory vesicles and the plasma membrane. The N-terminal truncation of annexin I gives rise to a molecule with a decreased Ca 2+ requirement for binding, both to secretory vesicles and plasma membrane. There was, thus, no difference in binding of either full-length annexin I or annexin I des1–8 to the secretory vesicles as compared to the plasma membrane.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0005273600002613; http://dx.doi.org/10.1016/s0005-2736(00)00261-3; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0034730437&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11018667; https://linkinghub.elsevier.com/retrieve/pii/S0005273600002613; http://linkinghub.elsevier.com/retrieve/pii/S0005273600002613; http://api.elsevier.com/content/article/PII:S0005273600002613?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0005273600002613?httpAccept=text/plain; http://dx.doi.org/10.1016/s0005-2736%2800%2900261-3; https://dx.doi.org/10.1016/s0005-2736%2800%2900261-3
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know