Andrzej Fertala, PhD
Bluemle Life Sciences Building, Room 430
Philadelphia, PA 19107
Expertise & Research Interests
My primary research activities involve the area of extracellular matrix. In particular, my studies focus on (i) identifying pathomechanisms of heritable diseases of connective tissues caused by mutations in collagen genes, (ii) technologies to produce novel collagen-like proteins for biomedical applications, and (iii) developing novel approaches to limit excessive fibrosis.
In the studies on the molecular basis of the heritable diseases caused by mutations in collagenous proteins, my studies place a main emphasis on (i) osteogenesis imperfecta caused by mutations in collagen I, (ii) spondyloepiphyseal displasias caused by mutations in collagen II, and (iii) on epidermolysis bullosa caused by mutations in collagen VII.
In addition to the studies on pathomechanisms of heritable diseases of connective tissues, my work contributed significantly to developing novel technologies for the production of human recombinant collagens for a number of biomedical applications. As animal-derived collagens and gelatin, at present widely used in biomedical and pharmaceutical fields, have the potential to transmit animal-derived diseases, the ability to produce recombinant human collagens and gelatin is very attractive. The high value and the potential applicability of recombinant human collagens are reflected by an approved patent and its licensing by Thomas Jefferson University to a commercial company. In addition to already established technologies, I continue developing new approaches to the rational engineering of collagenous proteins for biomedical applications.
In response to the need for novel therapies for fibrotic diseases, my laboratory has recently initiated studies on novel approaches to limit excessive fibrosis. These new approaches are built on my discoveries of processes that govern the formation of collagen fibrils. As this process is fundamental for the formation of fibrotic deposits, my concept is that, by inhibiting the formation of collagen fibrils, it will be possible to limit fibrosis. If experimentally confirmed, this novel concept may lead to developing novel inhibitors of fibrotic processes occurring in keloids, hypertrophic scarring, and others.
Patents: 1. Prockop, D.J., L. Ala-Kokko, A. Fertala, A. Sieron, K.I. Kivirikko, A. Geddis, T. Pihlajaniemi, Synthesis of human procollagens and collagens in recombinant DNA systems. U.S. Patent Number 5,405,757, 1995 (Patent licensed by TJU to a biotech company; FibroGen). 2. Prockop, D.J., A. Fertala, Inhibitors of collagen assembly. U.S. Patent Number 6,472,504. 2002. 3. Fertala, A., F. Ko, Collagen or collagen-like peptide containing polymeric matrices. U.S. Patent Number 6,753,311, 2004.
collagen; extracellular matrix; recombinant collagen; fibrosis
Most Recent Peer-Reviewed Publications
- Target-Specific Delivery of an Antibody That Blocks the Formation of Collagen Deposits in Skin and Lung
- P15 peptide stimulates chondrogenic commitment and endochondral ossification
- Patterns of production of collagen-rich deposits in peripheral nerves in response to injury: A pilot study in a rabbit model
- Piezoelectric Tensor of Collagen Fibrils Determined at the Nanoscale
- Blocking collagen fibril formation in injured knees reduces flexion contracture in a rabbit model
- Prospects and limitations of improving skeletal growth in a mouse model of spondyloepiphyseal dysplasia caused by R992C (p.R1192C) substitution in collagen II
- Gingival fibromatosis with significant De Novo formation of fibrotic tissue and a high rate of recurrence
- Auxiliary proteins that facilitate formation of collagen-rich deposits in the posterior knee capsule in a rabbit-based joint contracture model
- Matrix-specific anchors: A new concept for targeted delivery and retention of therapeutic cells
- Mechanisms of aberrant organization of growth plates in conditional transgenic mouse model of spondyloepiphyseal dysplasia associated with the R992C substitution in collagen II
- Piezoelectricity in collagen type II fibrils measured by scanning probe microscopy
- Developmental upregulation of an alternative form of pcp2 with reduced GDI activity
- Testing the anti-fibrotic potential of the single-chain Fv antibody against the α2 C-terminal telopeptide of collagen I
- Kuskokwim syndrome, a recessive congenital contracture disorder, extends the phenotype of FKBP10 mutations
- Engineering and characterization of the chimeric antibody that targets the c-terminal telopeptide of the α2 chain of human collagen I: A next step in the quest to reduce localized fibrosis
- Skeletal diseases caused by mutations that affect collagen structure and function
- Visualizing molecular polar order in tissues via electromechanical coupling
- Remodeling of the dermalepidermal junction in bilayered skin constructs after silencing the expression of the p.R2622Q and p.G2623C collagen VII mutants
- Perlecan Domain V Induces VEGf Secretion in Brain Endothelial Cells through Integrin α
5β 1and ERK-Dependent Signaling Pathways
- Electromechanical properties of dried tendon and isoelectrically focused collagen hydrogels