Boston University Medical Campus
Biochemistry

Matthew D. Layne

Assistant Professor of Biochemistry
Department of Biochemistry

Education

People:

• Elena Kandror
• William J. Monis
• Robert W. Shine
• Kathleen Tumelty

Former Lab Members BUSM

• Cassandra Patenaude

Research Interests

Dr. Layne established his laboratory in the Biochemistry Department at Boston Univeristy Medical School in the summer of 2007.

Our long-term goals are to understand the transcriptional control of genes, which are upregulated in the vascular smooth muscle cells and fibroblasts in cardiovascular and pulmonary disease. We have identified a secreted protein, aortic carboxypeptidase-like protein (ACLP), which contains a collagen-binding discoidin and a catalytically inactive metallocarboxypeptidase domain. ACLP is expressed in vascular smooth muscle cells and is induced in the diseased blood vessel in vivo. We are defining the mechanisms by which ACLP regulates VSMC proliferation and function using in vitro assays and vascular disease models with transgenic and knockout mice. Additional projects in the lab are investigating the control of myofibroblast gene expression in pulmonary fibrosis. We are exploring the mechanisms of gene expression in de-differentiated VSMC and myofibroblasts and have identified novel transcription factor complexes that may coordinate the expression and subsequent deposition of extracellular matrix proteins in wounded VSMC and fibroblasts.

Current Projects:

1. Investigating the regulation of genes in vascular smooth muscle cells in response to injury
2. Determining the role of aortic carboxypeptidase-like protein in vascular smooth muscle biology
3. Defining mechanism of fibroblast/myofibroblast transitions in fibrotic disease

Opportunities:

Interested graduate students in the Biochemistry, and Cell and Molecular Biology Programs at Boston University School of Medicine should contact Dr. Layne regarding the availability of research rotations.

Representative Publications

PubMed Search

Abstracts & Links

1. Layne MD, Endege WO, Jain MK, Yet S-F, Hsieh C-M, Chin MT, Perrella MA, Blanar MA, Haber E, Lee M-E. Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation. J Biol Chem 1998;273:15654-60.

2. Layne MD, Yet S-F, Hsieh C-M, Maemura K, Bernfield M, Perrella MA, Lee M-E. Impaired abdominal wall development and deficient wound healing in mice lacking aortic carboxypeptidase-like protein. Mol Cell Biol 2001;21:5256-61.

3. Layne MD, Yet S-F, Maemura K, Hsieh C-M, Liu X, Ith B, Lee M-E, Perrella MA. Characterization of the mouse aortic carboxypeptidase-like protein promoter reveals activity in both differentiated and dedifferentiated vascular smooth muscle cells. Circ Res 2002;90:728-36.

4. Ith B, Wei J, Yet S-F, Perrella MA, Layne MD. Aortic carboxypeptidase-like protein is expressed in collagen-rich tissues during mouse embryonic development. Gene Expr Patterns 2005;5(4):533-537.

5. Wei J, Gorman TE, Liu X, Ith B, Chen Z, Simon DI, Layne MD, Yet S-F. Vascular injury increases neointima formation in cysteine-rich protein 2-deficient mice. Circ Res 2005; 97:1323-1331.

6. Lin D-W, Chang I-C, Tseng A, Wu M-L, Chen C-H, Patenaude CA, Layne MD, Yet S-F. Transforming growth factor β up-regulates cysteine-rich protein 2 in vascular smooth muscle cells via activating transcription factor 2. J Biol Chem. 2008;283(22):15003-14.

7. Grant MA, Baron RM, Macias AA, Layne MD, Perrella MA, Rigby AC. Netropsin improves survival from endotoxemia by disrupting HMGA1-binding to the NOS2 promoter. Biochem J. 2009; 418(1):103-12.

8. Liu X, Ramjiganesh T, Chen Y-H, Chung SW, Hall SR, Schissel SL, Padera RF, Liao R, Ackerman KG, Kajstura J, Leri A, Anversa P, Yet S-F, Layne MD, Perrella MA. Disruption of striated preferentially expressed gene locus leads to dilated cardiomyopathy in mice. Circulation, 2009; 119(2)261-8.

9. Schissel SL, Dunsmore SE, Liu X, Shine RW, Perrella MA, Layne MD. Aortic carboxypeptidase-like protein is expressed in fibrotic human lung and its absence protects against bleomycin-induced lung fibrosis. Am J Pathol 2009;174(3):818-828.