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This profile was last updated on 2/13/14  and contains information from public web pages and contributions from the ZoomInfo community.

Adam D. Linstedt

Wrong Adam D. Linstedt?

Professor of Biological Sciences

Phone: (412) ***-****  HQ Phone
Email: l***@***.edu
Local Address:  Pennsylvania , United States
Carnegie Mellon University
5000 Forbes Ave.
Pittsburgh , Pennsylvania 15213
United States

Company Description: Carnegie Mellon,, is a private, internationally ranked research university with programs in areas ranging from science, technology and business, to...   more

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11 Total References
Web References
New results published in the Jan. ..., 21 Jan 2012 [cached]
New results published in the Jan. 20 issue of Science by Carnegie Mellon biologists Adam Linstedt and Somshuvra Mukhopadhyay show that manganese completely protects against Shiga toxicosis in animal models.
It would be neutralized if it were to get degraded, so it had to find some way to get out of being sent to the lysosome," said Linstedt, professor of biological sciences at Carnegie Mellon.
Serendipitous Discovery Based on Phone Call and a Protein
Linstedt and Mukhopadhyay discovered exactly how Shiga toxin avoided the lysosome as they were doing basic biological research to understand how components of the cell function. "If we weren't focused on answering fundamental biological questions, we wouldn't have made this discovery," Linstedt said.
Fifteen years ago Linstedt discovered GPP130, a protein found in the Golgi apparatus, a kind of post office for the cell that sorts and packages molecules made in the endoplasmic reticulum and delivers them to their final destinations within the cell. GPP130, Linstedt found, didn't behave like most Golgi proteins. Rather than remaining in the Golgi, GPP130 constantly cycles to the endosomes and back to the Golgi. As it returns, it avoids the pathway that takes a substance to the lysosome to be degraded.
In Science, Linstedt and Mukhopadhyay report that Shiga toxin exploits this unique quality of GPP130 to its advantage.
What I didn't realize was how profoundly dependent Shiga toxin was on GPP130," Linstedt said.
Because Shiga toxin was dependent on GPP130 and manganese caused loss of GPP130, Linstedt and Mukhopadhyay decided to see whether manganese would protect against Shiga toxin infection. In cell cultures, manganese treatment yielded an almost 4,000-fold increase in the amount of Shiga toxin required to induce cell death. In a mouse model, mice exposed to a high dose of Shiga toxin and treated with non-toxic doses of manganese were 100 percent resistant to the toxin.
By introducing manganese, Linstedt and Mukhopadhyay were able to remove Shiga toxin's vehicle for avoiding degradation -- GPP130. The researchers feel that this could be a promising treatment for neutralizing the effects of Shiga toxin in humans.
"Manganese is inexpensive. While Shiga toxin infection affects people in the developed world, it affects far more people in the developing world. An inexpensive, accessible treatment -- not a designer drug -- is the ideal solution," Linstedt said.
Linstedt believes that they can use manganese to block the toxin and an antibiotic to kill the bacteria, making for an extremely effective therapy.
S. Mukhopadhyay, A. D. Linstedt. Manganese Blocks Intracellular Trafficking of Shiga Toxin and Protects Against Shiga Toxicosis. Science, 2012; 335 (6066): 332 DOI: 10.1126/science.1215930
The new finding "is a classic ..., 20 Jan 2012 [cached]
The new finding "is a classic example of serendipity in science," says coauthor Adam Linstedt, a cell biologist at Carnegie Mellon. His team has been exploring the somewhat mysterious cellular role of a protein called GPP130.
Linstedt and Somshuvra Mukhopadhyay, also of Carnegie Mellon, now show that it's GPP130 that Shiga toxin hijacks.
Blog: Dan E. Linstedt: Nanotechnology Archives, 8 Mar 2006 [cached]
My cousin, Adam Linstedt is a microbiologist professor at Carnegie Mellon University, he's suggested to me that when conditions are right, the man-made atoms (nanotech) can actually be separated from the combined chemicals.In other words, he said: making conditions favorable to binding, allows the "walkers" to bind to the target molecules, making conditions unfavorable can have the chemicals self-separate from their target molecules.
So what about the power of computing at this level?
Gordon Research Conferences - 2008 Program (Molecular Cell Biology), 25 Sept 2008 [cached]
Adam Linsdtedt (Carnegie Mellon University)
MBC Editorial Board, 9 Jan 2011 [cached]
Adam Linstedt Carnegie Mellon University
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