Tel:	617-432-1794
	Fax:	617-432-0471
	E-Mail:	rando@hms.harvard.edu
	Location:	Room LHRRB - 208 45 Shattuck Street Boston MA 02115
	Homepage:	-

My laboratory is focused on the use of chemical approaches to solve basic biological problems. In particular, we are interested in the chemical basis of sensory signal transduction. A long-standing interest has been on the chemical/molecular basis of vertebrate vision. Here a major interest in on understanding the mechanisms of visual pigment (rhodopsin) regeneration and visual adaptation. A group of highly novel molecular processes have been identified. The enzymes and molecular chaperones involved in the biosynthesis of 11- cis -retinal (the visual chromophore) from vitamin A are being identified, cloned, and their mechanisms of action and modes of regulation are being established. These studies have led to novel approaches towards the treatment and prevention of retinal and macular degeneration.

References:

Dok, D., Ruiz, A., Yaron, O., Jahing, W. J., Ray, A., Xue, L. and Rando, R.R.: Purification and characterization of a transmembrane domain-deleted form of lecithin retinol acyl transferase. Biochemistry 42 , 6090-6098 (2003).

Jahng, W. J., David, C., Nesnas, N., Nakanishi, K. and Rando, R. R.: A cleavable affinity biotinylating agent reveals a retinoid binding role for RPE65 Biochemistry 42 , 6159-6168 (2003).

Jahng, W. J., Xue, L., and Rando, R. R.: Lecithin retinol acyltransferase is a founder member of a novel family of enzymes Biochemistry 442 , 12805-12812 (2003).

Gollapalli, D. R., Maiti, P. and Rando, R. R.: RPE65 operates in the vertebrate visual cycle by stereospecifically binding all- trans -retinyl esters Biochemistry 42 , 11824-11830 (2003).

Gollapalli, D. R. and Rando, R. R.: Molecular logic of 11- cis -retinoid biosynthesis in a cone-dominated species Biochemistry 42 , 14921-14929 (2003).

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