Hudson Freeze, Ph.D.

Hudson Freeze's Research Focus

Related Diseases > Congenital Disorders of Glycosylation, Glycosylation-Related Disorders, Crohn’s Disease (Colitis), Cancer

Dr. Freeze’s research focuses on the pathology resulting from faulty glycosylation, the process of adding carbohydrate (sugar) chains to proteins and lipids. Carbohydrates are required for proper secretion and targeting of thousands of proteins – an often overlooked fact of biology. He is driven by the search for novel therapeutics to treat patients with mutations leading to glycosylation defects called Congenital Disorders of Glycosylation (CDG). 

Hudson Freeze's Research Report

Glycosylation: An Essential Function

The entire cell surface is coated with sugars in complex chains that promote (or sometimes interfere) with cell-to-cell communication. These sugar chains are first attached to proteins deep inside the cell where they help them get into shape for their jobs. As the proteins percolate toward to cell surface, the sugar chains are sculpted for specific needs. This entire process, called glycosylation, recruits a force of more than 500 genes for this job. The Freeze lab works on several facets of glycosylation, all of them with an eye toward therapeutic applications for diseases that impair the functions of these critical genes. 


Human Glycosylation Disorders

One of our major areas is a group of inherited diseases is called Congenital Disorders of Glycosylation (CDG). Today we know of defects in over 50 genes compared to just 3, only 15 years ago. Patients with these diseases have highly variable mental and motor developmental delay, seizures, failure to grow, hypoglycemia (low blood sugar), clotting and digestion abnormalities, to name just a few. These are rare disorders have over 1,000 known patients worldwide, but it is likely that many remain undiagnosed. Physicians are becoming more aware of glycosylation disorders in general, and basic scientists continue to discover sugar chains at the helm of many basic metabolic processes. Defective glycosylation is also known to cause several types of muscular dystrophy. Figure 1 shows the explosive growth in the number of different diseases caused by defective glycosylation. In Figure 2 and the film clip, Harrison Ford poses a few questions for us. Rocket Williams reaches out to us in Figure 3. 

Inherited Glycosylation Disorders

Figure 1

Harrison Ford Knows a lot abuot CDG
Figure 2

The Rocket Fund
Figure 3

The Freeze lab identifies new glycosylation disorders and tries to understand how these defects cause the disease manifestations. Defects occur in genes that activate and transport sugars, assemble them into glycans an remodel them. Some also traffic and distribute the glycosylation machinery within cells. Ongoing collaborations with academic physicians provide a steady flow of new patients for analysis. Since very few laboratories in the United States work on CDG, we are developing new molecular diagnostic methods to handle the increasing number of patients. With the help of generous philanthropic support, we are seeking ways to supplement the depleted glycosylation pathways in patients. 

Hudson Freeze's Bio

Dr. Freeze earned his Ph.D. from the University of California, San Diego in 1976. Subsequently he held fellowships in Biology, Medicine and Neurosciences later joined the faculty at the same institution. In 1988 Dr. Freeze was recruited to Sanford-Burnham Medical Research Institute.

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Srikrishna G
J Innate Immun 2012;4(1):31-40
Jones MA, Bhide S, Chin E, Ng BG, Rhodenizer D, Zhang VW, Sun JJ, Tanner A, Freeze HH, Hegde MR
Genet Med 2011 Nov;13(11):921-32
Freeze HH, Ng BG
Cold Spring Harb Perspect Biol 2011 Sep 1;3(9):a005371
Chan B, Clasquin M, Smolen GA, Histen G, Powe J, Chen Y, Lin Z, Lu C, Liu Y, Cang Y, Yan Z, Xia Y, Thompson R, Singleton C, Dorsch M, Silverman L, Su SM, Freeze HH, Jin S
Hum Mol Genet 2016 Jun 1;25(11):2182-2193
Wheeler PG, Ng BG, Sanford L, Sutton VR, Bartholomew DW, Pastore MT, Bamshad MJ, Kircher M, Buckingham KJ, Nickerson DA, Shendure J, Freeze HH
Am J Med Genet A 2016 Dec;170(12):3165-3171
Freeze HH
Nat Genet 2016 Jun 28;48(7):705-7