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Wrong Adam Linstedt?

Adam D. Linstedt

Professor of Biological Sciences

Carnegie Mellon University

HQ Phone:  (412) 268-2000

Email: l***@***.edu

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Carnegie Mellon University

5000 Forbes Avenue

Pittsburgh, Pennsylvania, 15213

United States

Company Description

Carnegie Mellon (www.cmu.edu) is a private, internationally ranked research university with programs in areas ranging from science, technology and business, to public policy, the humanities and the arts. More than 13,000 students in the university's seven scho...more

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Background Information

Employment History

Associate Editor

Mol Biol Cell


Affiliations

Gordon Research Conferences incorporated

Board of Trustees Member


Education

Ph.D.


Web References(10 Total References)


Gordon Research Conferences - 2013 Program - Cell Biology of Metals

Adam Linstedt (Carnegie Mellon University)


http://www.biomedicalblog.com/manganese-may-provide-the-first-known-treatment-for-shiga-toxin/141400/

An inexpensive, accessible treatment- not a designer drug - is the ideal solution," says Adam Linstedt, professor of biological sciences at Carnegie Mellon.


http://www.sciencedaily.com/releases/2012/01/120119143330.htm

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


http://www.sciencenews.org/view/generic/id/337775/title/Mineral_quashes_deadly_bacterial_poisons

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.


http://telecominnovation.ulitzer.com/node/2135288

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.


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