Abstract by Blake Nordblad

Personal Infomation

Presenter's Name

Blake Nordblad

Degree Level


Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

Kenneth Christensen


Identifying the Interaction between CMG2 and Collagen VI in Blood Vessel Development and Disease


Capillary Morphogenesis Gene 2 (CMG2) is an important extracellular receptor involved in anthrax intoxication, blood vessel development, and cellular chemotaxis. CMG2 interacts with extracellular matrix proteins such as collagen VI; however, the nature of those interactions is unknown. Moreover, loss of function mutations in CMG2 cause diseases known as Hyaline Fibromatosis Syndromes (HFS) resulting in the accumulation of collagen VI  and other extracellular matrix proteins in subcutaneous nodules in the skin. Primary protein sequence analysis CMG2 and collagen VI has elucidated that both proteins contain von Willebrand factor-like (vWF) domains, which are known for interacting with each other. Here we present a reanalysis of recently published mass spectrometry data showing the prevalence of collagen VI vWF domains in HFS patient samples and data investigating the interaction between vWF domains on collagen VI and CMG2 as a putative mechanism for these protein-protein interactions.