'Y’ a Protein Unicorn Might Matter in Glaucoma

First Discovery – Encoded By Gene – Protein Linked with Glaucoma

Recent discovery has been done on Y-shape towards the base of myoclin linking together four popular proteins forms known as olfactomedins or propellers in segments of four. To get some insight on myocilin is essential in definite types of hereditary glaucoma.

Raquel Lieberman, the artist behind this interpretation is said to be the main investigator of the group which has set a Y-shaped structure, considered to be the first ever discovery which had been encoded by a gene and not built from protein component parts. This amazing discovery had been done by researcher regarding protein linked with glaucoma which for more than two years had gone through a tough lab test.

A new research paper had been published regarding the same and what was observed had been certified. It was a Y-shape which had made it peculiarly significant to science and probably to medicine, especially in the treatment of certain kind of blindness.

Raquel Lieberman leading the study had commented that a protein of this kind had not been reported earlier and there seems to be very few Y-shapes in protein at all. Lieberman is a structural biologist at the Georgia Institute of Technology and expert on myocilin that is a protein which at times is associated in a form of hereditary glaucoma.

Common Cause of Blindness Glaucoma 

Universally the second most common cause of blindness is glaucoma and hereditary glaucoma is said to be one type of the ailment. Major cause of hereditary glaucoma is genetic mutation in myocilin that tends to strike especially at a tender age particularly in childhood. It is said that there are other forms in protein that tend to look same to the Y, although with significant variances.

Lieberman had commented that the antibodies appear somewhat like this though in antibodies, separate proteins, which are the various genes of the product that fit together making it a type of Y-shape. This Y is encoded by an individual gene sequence which makes it completely exclusive. Besides being apparent unicorn of protein structure, it seems to be the essential binding component of myocilin.

The Y ties along with major components in nailing down the overall form of myocilin over turning the earlier conception regarding the appearance of protein. However the Y has not been associated in particular in glaucoma, its presence could change the way the researchers would comprehend myocilin and how it tends to function in the eye. It make fibrils when mycolin inclines to go wrong or misfolds, damaging tissue known as trabecular meshwork which have a tendency to generally permit the fluid in the eye to drain and relieve the pressure within.

 

Myocilin Common in Body

Lieberman, an associate professor in Georgia Tech’s School of chemistry and Biochemistry, had commented that if one destroys the cells responsible for draining the fluid, it would clog and the pressure within the eye would increase.

Moreover that pressure could destroy areas of the retina or optic nerve which would cause irreversible partial or complete blindness. In spite of the fact that myocilin tends to be common in several areas of our body, its usual healthy function in the eye and what functions the protein tends to have in the body seems to be yet a mystery.

Lieberman had further commented that he thinks that if they were aware of what this protein could be doing in the trabecular meshwork then they would comprehend more regarding glaucoma in general. This study has enabled them to get more insight with regards to myocilin. The results had been published by Lieberman on October 19, 2017, in the journal Structure.

The research had been financed by the National Eye Institute together with the National Institute of General Medical Science, both at the National Institutes of Health by the National Science Foundation as well as by the U.S. Department of Energy Office of Science.

Stingy Abnormal Proteins 

The purpose of the study so far had been on area of myocilin which tends to be the main issue by way of hereditary glaucoma, which is considered to be protein structure known as the olfactomedin domain. This had been extensively researched by Lieberman. It appeared like a protein propeller having five blades surrounding a hole towards its centre.

Lieberman had also stated that when a myocilin propeller tends to misfolds, it unravels forming amyloid fibrils – stingy abnormal proteins. This damaged the cells which maintain the trabecular network. Till then their work had led them to assume that the propellers floated around exclusively as liberated units and not bound together in groups.

 He further added that they were aware that in solutions, those olfactomedins had been just monomers. They did not make much of a higher order with the exception that when they had untied into amyloid fibres, they stuck together and blocked the flow of fluid.

 The Y tends to change the image and anchors the propellers in cluster of four. Two of the propellers – olfactomedin domains, each seem to be linked probably to the tip of the Y’s branches possibly by amino acid strings.

Super Sticky

The overall myocilin with the Y tends to appear like fur pinwheels on strings linked to a slingshot. Additional new discoveries – The Y tends to be sticky like glue and seems to be bothersome while handling in the lab. He informed that it was sticking to the plastic, to the glass as well as to the membrane, to beads and is super sticky. This could serve a biological function. The Y could perhaps fasten the propellers to surface though it is not known.

Lieberman is of the opinion that the main function would be to pair and separate out these olfactomedin domains. Mutations in the Y are not knowingly linked with glaucoma. Lieberman has stated that when it mutates, it tends to misfold though not in a manner which would cause cell death.

However in usual role the Y could promote the speed of misfolding of the propeller protein which is associated with hereditary glaucoma. When the misfolded proteins tends to come in contact with good proteins it is said that the misfolded one make the ones which are good to misfold also.