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Bruce E. Vogel, PhD

Academic Title:

Assistant Professor

Primary Appointment:



BioMET 307B

Phone (Primary):

(410) 706-4516


(410) 706-8184

Education and Training

B.A.     Biochemistry, Rutgers College, New Brunswick, NJ

Ph.D.    Biochemistry, Rutgers Medical School and Rutgers   University, Piscataway, NJ

Postdoctoral fellow -La Jolla Cancer Research Foundation, La Jolla, CA.  

Postdoctoral fellow  Department of Biology, Johns Hopkins University


My laboratory is interested in how extracellular matrix proteins, transmembrane receptors, and cytoskeletal adapters work together to specify tissue architecture. We primarily use C. elegans as a model organism to study the nematode orthologs of conserved extracellular proteins that are defective in human diseases. In the past we have discovered hemicentin and identified functional interactions between hemicentin and fibulin. These two proteins have been implicated in Age-related Macular Degeneration (AMD), a common human disease that is characterized by progressive degeneration of sensory neurons, called photoreceptors, in the retina. Currently, we are studying how interactions between complement factor H (a secreted protein that is frequently mutated in ARMD patients), transmembrane, and cytoskeletal proteins affect sensory neuron function in C. elegans and asking whether these interactions are conserved in vertebrate photoreceptors.


Highlighted Publications

Acker N, Smith H, Devine C, Oltjen SL, Tsiropoulou S, Smit-McBride Z, Lange K, Blacque OE, Matsubara JA, Gordus A, Golden A, Vogel BE (2021) A complement factor H homolog, heparan sulfation,and syndecan maintain inversin compartment boundaries in C. elegans cilia Proc. Natl. Acad. Sci. 118 (in press)

Muriel JM, Dong C, Vogel BE(2012) Distinct regions within fibulin-1D modulate interactions with hemicentin.  Exp Cell Res. 2012 Dec 10; 318 (20) : 2543-7. doi: 10.1016/j.yexcr.2012.08.007. Epub 2012 Sep 7.  

Xu X and Vogel BE. (2011) A secreted protein promotes cleavage furrow maturation during cytokinesisCurr Biol. 21:114-9.  PMCID: PMC3046554

Vogel BE, Wagner C, Paterson JM, Xu X, Yanowitz JL.  (2011)  An extracellular matrix protein prevents cytokinesis failure and aneuploidy in the C. elegans germline.  Cell Cycle. Jun 15;10(12):1916-20. Epub 2011 Jun 15.  PMCID: PMC3154414

Xu X, Vogel BE.  (2011) A new job for ancient extracellular matrix proteins: Hemicentins stabilize cleavage furrowsCommun Integr Biol. Jul; 4(4):433-5. doi: 10.4161/cib.4.4.15324. Epub 2011 Jul 1.  PMCID: PMC3181513

Xu X, Dong C, Vogel BE. (2007) Hemicentins assemble on diverse epithelia in the mouseJ Histochem Cytochem. 55:119-26.

Dong, C, Muriel, JM, Ramirez, S, Hutter, H, Hedgecock, EM, Breydo, L, Baskakov, IV and Vogel, BE (2006) Hemicentin assembly in the extracellular matrix is mediated by distinct structural modulesJ. Biol. Chem. 281:23606-23610. 

Muriel, JM, Xu, X and Vogel, BE. (2006) Selective assembly of fibulin-1 splice variants reveals distinct extracellular matrix networks and novel functions for Perlecan/UNC-52 splice variantsDev. Dyn. 235:2632-40. 

Vogel BE, Muriel JM, Dong C, Xu X. (2006) Hemicentins: what have we learned from wormsCell Res. 16:872-8. 

Muriel, JM, Dong, C, Hutter, H and Vogel, BE. (2005) Fibulin-1C and Fibulin-1D splice variants have distinct functions in C. elegans development and assemble in a hemicentin dependent manner. Development 132:4223-4234. 

Vogel, BE and Hedgecock, EM. (2001) Hemicentin, a conserved extracellular member of the immunoglobulin superfamily, organizes epithelial and other cell attachments into oriented line-shaped junctionsDevelopment 128:883-894. 



Additional Publication Citations


Ugolino J, Dziki KM, Kim A, Wu JJ, Vogel BE, Monteiro MJ.(2019) Overexpression of human Atp13a2Isoform-1 protein protects cells against manganese and starvation-induced toxicity.    PLoS One.  14:e0220849. doi: 10.1371/journal.pone.0220849. eCollection 2019.PMID: 31393918

Zhong Y, Wang J, Henderson MJ, Yang P, Hagen BM, Siddique T, Vogel BE, Deng HX, Fang S.  (2017) Nuclear export of misfolded SOD1 mediated by a normally buried NES-like sequence reduces proteotoxicity in the nucleus.  Elife. 2;6. pii: e23759. doi: 10.7554/eLife.23759. PMCID: PMC5449186

Research Interests

Research Specialties:  Extracellular matrix, Sensory neuron cell architecture and function

Where is complement factor H (CFH) found in C. elegans?

Age-related Macular Degeneration (AMD) is the leading cause of blindness among the elderly in the developed world. However the mechanism of AMD pathogenesis is poorly understood. Mutations in CFH increase risk for AMD 6-20 fold. The canonical function of CFH is to inhibit inflammation and cytolysis caused by activation of the alternative complement pathway of the innate immune system. Therfore, current thinking suggests that the disease mechanism is likely a result of an increase in inflammation in the retina. However our findings suggest a direct role for CFH in sensory neuron function. Using CRISPR-Cas9, we have constructed a functional fusion between CFH and green fluorescent protein (GFP), enabling us to monitor CFH-GFP localization in live animals during development. CFH-GFP accumulates at the ciliated tips of sensory neurons involved in mechanosensation. Based on this and other data (see Acker et al., 2021), we believe that AMD may result directly from a defect in sensory neuron (i.e. photoreceptor) function.

Our current focus is on using molecular, genetic and biochemical tools to identify the functional significance of CFH on sensory neuron cell surfaces and to identify cell surface receptors and other extracellular proteins that functionally interact with CFH. 

The long-term goal is to understand the mechanism of AMD pathogenesis and to develop therapies to inhibit this mechanism.




Lab Techniques and Equipment

We use a wide variety of Molecular, Genetic, Biochemical and Cell Biology techniques that include (but are not limited to): 
Forward Genetic Screens using random mutagenesis, Reverse Genetic Screens Using RNAi, site directed mutagenesis, GFP tags of proteins, light and electron microscopy, immunohistochemistry, protein purification