While federal judges feuded over whether jailed nuclear physicist Wen Ho Lee should be released to home detention before his trial in November, the country's scientific establishment attacked Attorney General Janet Reno over the way Lee is being treated.

On 31 August the presidents of the nation's preeminent science academies released an open letter that blasts Reno. Lee has been "a victim of unjust treatment," say the presidents, since he was jailed in December following a yearlong investigation into possible spying at Los Alamos. The letter--signed by Bruce Alberts of the National Academy of Sciences, William Wulf of the National Academy of Engineering, and Kenneth Shine of the Institute of Medicine--also complained that Reno had failed to respond to two earlier letters inquiring about his treatment, including alleged restrictions on contact with his family and the use of shackles while in solitary confinement. A one-page letter that they received in May from a Department of Justice (DOJ) official "was not a satisfactory response," they said. Noting the academies' efforts on behalf of political prisoners in other countries, Wulf told Science that even some repressive foreign regimes "had done a far better job" of answering routine letters protesting the treatment of jailed scientists.

But Wulf says the trio might not have publicly raked Reno over the coals had they known about another letter that DOJ sent to a workers' advocacy group at Lawrence Livermore National Laboratory in California. Two weeks before the academies released their letter, the DOJ sent the Society of Professional Scientists and Engineers (SPSE) a three-page discussion of Lee's treatment, including assurances that he was shackled only when being moved and was allowed visits from his family.

DOJ will have another chance to respond to the academies. Wulf and his colleagues also want to know how the government plans to punish an FBI agent who apparently gave misleading testimony at a May court hearing that led a judge to jail Lee pending his trial.

Scientists have found a new member of a gang of proteins that attack the brain to cause Alzheimer's disease. The new protein helps prepare one of the raw materials that builds up in amyloid plaques. Identifying it, researchers say, opens up a new target for drugs that stop the disease.

Alzheimer's afflicts about 4 million people in the United States, leaving them disoriented, forgetful, and increasingly unable to take care of themselves. The neurological damage seems to result from deposits in the brain called amyloid plaques. One of the main ingredients in these plaques, a peptide called beta amyloid, is created when enzymes cut up a protein called APP. Some of the cellular scissors that snip out beta amyloid are a group of enzymes called the presenilins (see Science, 22 October 1999, p. 650), but scientists know the presenilins have help.

To find one of these accomplices, a research team led by neurobiologist Gang Yu of the University of Toronto looked for proteins that hang out with presenilins. The researchers isolated presenilin-1 from Alzheimer's-like cells and discovered a new protein they dubbed nicastrin. It appeared to have the strong grip necessary for a cutting enzyme: When Yu and his team grabbed onto nicastrin, APP came along for the ride. And more direct evidence for its role in making plaques is the fact that cells produced more beta amyloid if they contained certain mutated forms of nicastrin, the researchers report in the 7 September issue of Nature. They suggest that nicastrin and presenilin-1 are members of a large complex they call a secretosome in which many proteins collaborate to make beta amyloid.

Nicastrin is "an important piece of the puzzle" says molecular neurologist Sangram Sisodia of the University of Chicago. Though it's clear that nicastrin is part of the machine that makes the beta amyloid peptide, he says, it's not clear what it does. It might cut APP itself, or it might assist presenilin or other proteins in the task. Figuring out these details, says Sisodia, will guide the design of drugs that might slow the progression of Alzheimer's.

--R. JOHN DAVENPORT

Related sites
The Alzheimer Research Forum

--DAVID MALAKOFF