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Story ideas from the Journal of Biological Chemistry

American Society for Biochemistry and Molecular Biology

Articles to be published in the June 1, 2007 issue of the Journal of Biological Chemistry (Vol. 282, No. 22)

ARTICLE HIGHLIGHTS

  • New Insight into Cell Division

  • How Curry Spice Helps Fight Cancer

  • Role of Tau Proteins in Alzheimer's Disease

  • New Insight into Cause of Amyotrophic Lateral Sclerosis


New Insight into Cell Division

This article was featured as a "Paper of the Week" by the Journal of Biological Chemistry's Editors, meaning that it belongs to the top one percent of papers reviewed in significance and overall importance.

Researchers provide new details about how proteins orchestrate cell division.

Cells can divide only when certain key proteins are activated and others inhibited. A protein called NIPA and a set of two proteins called cyclin B1 and Cdk1 are some of these key proteins. Until now, scientists had shown that the cyclin B1/Cdk1 complex is needed to initiate and maintain cell division but is destroyed before and after this process. Also, NIPA was shown to regulate the abundance of cyclin B1/Cdk1 before cell division.

Justus Duyster, Florian Bassermann, and their colleagues revealed that cyclin B1/Cdk1 also regulates NIPA during cell division, which indicates that both proteins regulate each other. The scientists suggest that NIPA is inhibited twice: directly before cell division, to activate cyclin B1/Cdk1, and at the beginning of cell division, when NIPA is further inhibited by cyclin B1/Cdk1. At the end of cell division, cyclin B1/Cdk1 is destroyed and NIPA becomes active again.

Article: "Multisite phosphorylation of Nuclear Interaction Partner of ALK (NIPA) at G2/M Involves Cyclin B1/Cdk1" by Florian Bassermann, Christine von Klitzing, Anna Lena Illert, Silvia Muench, Stephan W. Morris, Michele Pagano, Christian Peschel, and Justus Duyster

MEDIA CONTACT: Justus Duyster, Technical University of Munich, Germany; tel: +49-89-41-40-41-04; e-mail: justus.duyster@lrz.tum.de

MEDIA CONTACT: Florian Bassermann, New York University School of Medicine; tel: 212-263-5129; e-mail: florian.bassermann@med.nyu.edu


How Curry Spice Helps Fight Cancer

Scientists showed that curcumin, the main ingredient of the Indian herb turmeric, restores key immune cells that fight off cancer.

The immune system of patients with advanced cancer is significantly weakened, mostly because the main cells that fight off tumors either cannot proliferate anymore or have died off. Curcumin was previously shown to have anti-tumor activity but its effects on the immune system were unknown - until now.

Gaurisankar Sa and colleagues showed that curcumin boosts the immune system of tumor-bearing mice by restoring key immune cells called CD4 and CD8 T cells. The scientists also showed that curcumin increases the production of proteins that cause immune cells to proliferate and reduces the production of proteins that destroy immune cells.

Article: "Curcumin Prevents Tumor-Induced T Cell Apoptosis through Stat-5a-mediated Bcl-2 Induction" by Sankar Bhattacharyya, Debaprasad Mandal, Baisakhi Saha, Gouri Sankar Sen, Tanya Das, and Gaurisankar Sa

MEDIA CONTACT: Gaurisankar Sa, Bose Institute, Kolkata, India.; tel: +91-33-2355-9416; e-mail: gauri@bic.boseinst.ernet.in


Role of Tau Proteins in Alzheimer's Disease

Scientists have provided new details about how proteins involved in the origin and development of Alzheimer's Disease (AD) form harmful aggregates.

AD, the most common type of dementia, is characterized by progressive cognitive deterioration and declining daily activities. One of AD's pathological hallmarks is the abnormal aggregation of a protein called tau within nerve cells. Scientists have long suspected that this process contributes to the progressive damage or death of neurons but, until now, they have had difficulty testing this hypothesis in cultured cells because tau proteins do not aggregate easily under normal conditions.

To address this problem, Jeff Kuret and colleagues have developed drug-like chemicals that cross cell membranes and drive efficient tau aggregation over a period of days. They noticed that when tau proteins within cells were treated with this chemical, they separated from other proteins - called microtubules - to which they naturally attach and then started aggregating.

The scientists then showed that cells in which tau proteins aggregated could not grow and function properly. These results suggest that tau aggregation is toxic to cells and could directly contribute to the progressive damage or death of neurons in AD. The results also show that by further understanding the toxic effects of tau aggregation, scientists may be able to devise treatments to prevent or slow down AD in the future.

Article: "Tau Aggregation and Toxicity in a Cell Culture Model of Tauopathy" by Bhaswati Bandyopadhyay, Guibin Li, Haishan Yin, and Jeff Kuret

MEDIA CONTACT: Jeff Kuret, The Ohio State University, Columbus; tel: 614-688-5899; e-mail: kuret.3@osu.edu


New Insight into Cause of Amyotrophic Lateral Sclerosis

Researchers have discovered a new cellular mechanism that may better explain what causes amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig's Disease.

ALS is characterized by the death of neurons that control voluntary muscles, leading to muscle weakness and atrophy. Around 25 percent of the familial forms of the disease - forms that occurs repeatedly in family members but is not necessarily inherited - have been linked to mutation in a gene that makes a protein called superoxide dismutase 1 (SOD1). But how the defective variants of the SOD1 protein might interact with other cellular components to cause the disease has remained unclear.

Haining Zhu and colleagues looked at the components of proteins that interact with SOD1 and identified a protein involved in the intracellular transport of molecules in neurons. Previous studies had shown that such transport processes were slowed down in ALS patients and related animal models, but how such deficiency was connected with defective SOD1 has remained unknown. The new results show that this slower transport of molecules is probably due to an abnormal interaction between the newly-identified transport protein and defective components of SOD1, thus providing new insight into ways to prevent or slow down the disease.

Article: "Interaction between Familial Amyotrophic Lateral Sclerosis (ALS)-linked SOD1 Mutants and the Dynein Complex" by Fujian Zhang, Anna-Lena Strom, Kei Fukada, Sangmook Lee, Lawrence J. Hayward, and Haining Zhu

MEDIA CONTACT: Haining Zhu, University of Kentucky, Lexington; tel: 859-323-3643; e-mail: haining@uky.edu

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