One should always indulge in physical activities as it will help them stay fit, energetic and also lead a healthy lifestyle.

Doing regular exercise not only keeps your brain active but also reduces the risk of developing memory loss diseases like dementia.

A new study was conducted on mice and found out that exercise can increase the production of a key protein that helps in keeping the brain active as well as lower the risk of neurological diseases.

The study showed that during the rodents' exercise routine, certain chemicals naturally build up in the brain and kick-start the production of BDNF -- also called "Miracle-Gro" -- for the brain because of its role in enhancing memory and the growth of nerve cells.

Moses Chao, professor at New York University, in the US says, 'We believe that our study shows a precise biological mechanism behind increased BDNF production in mammals due to exercise.'

He added that unravelling the mysteries of BDNF is important as we seek more ways to naturally keep mammalian brains healthy, including those of humans.

Unravelling the mystery of BDNF production to naturally keep mammalian brains healthy, the researchers found that ketone -- a chemical naturally produced in the liver called beta-hydroxybutyrate (DBHB) --, triggers biological reactions that activates the BDNF gene to produce more of its protein.

Also, this DBHB -- which builds up in the body and brain with exercise -- was found to prevent other proteins in the brain known as histone deacetylase complexes, or HDACs, from suppressing BDNF production by altering the environment of the BDNF gene.

For the study, published online in the journal eLife, the team compared the brains of mice that had been allowed to run at will on a cage wheel for a month with the brains of mice that did not run.

"Our findings suggest how we might boost production of BDNF as studies have confirmed that doing so protects the brain," Chao said.

The researchers used commercially available psychiatric drugs already known to stabilize mood and prevent seizures by inhibiting HDACs and "open up" the otherwise "closed" BDNF gene, making it easier to trigger its action and increase BDNF production by as much as 50 percent.

Smokers take note! A new study suggests that people who smoke marijuana for a long time have an increased risk of gum diseases that can lead to tooth loss.

In the study, tobacco users were found to have gum disease as well as reduced lung function, systemic inflammation and indicators of poorer metabolic health.

The study tracked nearly 1,000 New Zealanders from birth to age 38.

"We can see the physical health effects of tobacco smoking in this study, but we don't see similar effects for cannabis smoking," said Madeline Meier, Assistant Professor of Psychology at Arizona State University in the US.

The international research team assessed a dozen measures of physical health, including lung function, systemic inflammation and several measures of metabolic syndrome, including waist circumference, HDL cholesterol (good cholesterol), triglycerides, blood pressure, glucose control and body mass index.

To measure cannabis use, the researchers asked study participants to self-report their use at ages 18, 21, 26, 32 and 38.

However, the study did not find a link between long-term marijuana use and several other health problems associated with cigarette smoking.

"We need to recognise that heavy recreational cannabis use does have some adverse consequences, but overall damage to physical health is not apparent in this study," study co-author Avshalom Caspi, Professor at Duke University in Durham, said.

"Physicians should certainly explain to their patients that long-term marijuana use can put them at risk for losing some teeth," Terrie Moffitt, who is also from Duke University said.

The findings were published in the journal JAMA Psychiatry.

A pinch of poison is good for a body, at least if it is heme, and researchers, including one of Indian-origin, have now found how the body turns this toxin into a nutrient know for its role at the core of hemoglobin, the component of red blood cells responsible for transporting oxygen.

In minuscule amounts, heme works in cells as an essential catalyst called a cofactor and as a signaling molecule to trigger other processes.

"Poor heme management can cause things like Alzheimer's, heart disease, and some types of cancers, so cells have to do a good job of managing how much heme is available," said Amit Reddi, Assistant Professor at Georgia Institute of Technology in the US.

The labile heme serves as a nutrient instead of a poison. But to make sure things stay that way, heme needs to be carefully trafficked through the cell, Reddi said.

"By having biosensors that can monitor heme in cells, we have this new window into how cells make this essential toxin available in carefully sparse concentrations," he said.

The researchers used ratiometric sensor to illuminate heme's movements.

People may recognise heme from its role at the core of hemoglobin, the component of red blood cells responsible for transporting oxygen.

The ionic iron in the heme molecule is what the oxygen molecule sticks to.

In hemoglobin, the heme is embedded tightly in protein, rendering it non-toxic.

For the research, published in the journal Proceedings of the National Academy of Sciences. the team designed a fluorescent sensor molecule to keep tabs on how hem is carefully trafficked through the cell

With heme at very low baseline levels, the sensor lit up bright green and as heme concentration increased, it caused the light to fade out.

Using the heme sensors, the researchers found an enzyme, GAPDH, known for its involvement in breaking down sugar, got tied up in proteins, leaving only a limited amount free for biochemical reactions.

When more labile heme is needed, nitric oxide, a signaling molecule, rapidly released heme from entangling proteins, so it could do jobs such as regulating gene expression.

"Ratiometric fluorescent techniques have been around for a while, but our technique is new, because it specifically senses heme," Reddi said.

"We took a heme binding protein from bacteria and clipped it onto to green fluorescent protein," he explained.