Dr. Andrzej Fertala |
|
Thomas Jefferson University Jefferson Medical College Dermatology & Cutaneous Biology ProfessorAppointed: 2000 |
Mailing AddressDepartment of Dermatology and Cutaneous Biology, BLSB/424 Thomas Jefferson University BLSB/Room 424 233 South 10th Street Philadelphia, Pennsylvania 19107-5587United States | Contact InformationPhone: (215) 503-0113 Andrzej.Fertala@jefferson.edu |
Qualifications
Ph.D..
Expertise and Research Interests
Dr. Fertala's research is focused on the structure and function of the extracellular matrix in health and disease. The extracellular matrix consists of a number of macromolecules that form well-organized complexes. These complexes are part of a continuous framework, which provides support for cells and is critical for mechanical functions of various connective tissues.
Dr. Fertala is particularly interested in studies on mechanisms of the self-assembly of the extracellular matrix. Specifically, his laboratory is involved in studies on self-assembly of fibrillar collagens. Because human procollagens are difficult to isolate from tissues or cell cultures, studies on human collagen fibril formation present a number of challenges. To circumvent these problems, Dr. Fertala's laboratory developed an experimental system that utilizes recombinant human procollagens. Dr. Fertala has pioneered work on the self-assembly of recombinant human collagen II. These studies led to an understanding of the molecular mechanism of altering collagen fibril structure because of mutations in collagen genes found in patients with early onset osteoarthritis. Recently, Dr. Fertala's group synthesized a number of mutant collagens that are used to determine general the mechanism of the alteration of collagen fibrils in some heritable diseases of connective tissues. In addition to the studies on self-assembly of fibrillar collagens, Dr. Fertala is involved in research on the formation of collagen VII anchoring fibrils present in skin. His group has discovered that assembly of these fibrils depends on site-specific interactions and is promoted by enzymatic cleavage of the NC2 domain present in procollagen VII.
Recombinant procollagen technology used in Dr. Fertala's laboratory resulted in the creation of unique gene engineered collagen II variants that are used in studies on the collagen fibril formation. These studies resulted in defining specific regions in collagen molecules that are critical for fibril assembly. Currently, the team led by Dr. Fertala is investigating the possibility of blocking these sites to inhibit process of fibrosis.
Dr. Fertala is also interested in the interaction between cells and collagenous proteins. Using a unique experimental system, his group identified specific sites in collagen II critical for interaction with chondrocytes. This information is used to engineer "smart super-collagens," in which most important domains were multiplied. These results provide a basis for the rational design of collagen-like proteins for tissue engineering.
Because of changes in metabolism and the structure of connective tissues occurring during space flights, Dr. Fertala is interested in studies on designing gene-engineered collagens for promoting regeneration of bone and cartilage. The recombinant collagen-like proteins he designed and successfully expressed are under investigation structurally and biologically.
Dr. Fertala is particularly interested in studies on mechanisms of the self-assembly of the extracellular matrix. Specifically, his laboratory is involved in studies on self-assembly of fibrillar collagens. Because human procollagens are difficult to isolate from tissues or cell cultures, studies on human collagen fibril formation present a number of challenges. To circumvent these problems, Dr. Fertala's laboratory developed an experimental system that utilizes recombinant human procollagens. Dr. Fertala has pioneered work on the self-assembly of recombinant human collagen II. These studies led to an understanding of the molecular mechanism of altering collagen fibril structure because of mutations in collagen genes found in patients with early onset osteoarthritis. Recently, Dr. Fertala's group synthesized a number of mutant collagens that are used to determine general the mechanism of the alteration of collagen fibrils in some heritable diseases of connective tissues. In addition to the studies on self-assembly of fibrillar collagens, Dr. Fertala is involved in research on the formation of collagen VII anchoring fibrils present in skin. His group has discovered that assembly of these fibrils depends on site-specific interactions and is promoted by enzymatic cleavage of the NC2 domain present in procollagen VII.
Recombinant procollagen technology used in Dr. Fertala's laboratory resulted in the creation of unique gene engineered collagen II variants that are used in studies on the collagen fibril formation. These studies resulted in defining specific regions in collagen molecules that are critical for fibril assembly. Currently, the team led by Dr. Fertala is investigating the possibility of blocking these sites to inhibit process of fibrosis.
Dr. Fertala is also interested in the interaction between cells and collagenous proteins. Using a unique experimental system, his group identified specific sites in collagen II critical for interaction with chondrocytes. This information is used to engineer "smart super-collagens," in which most important domains were multiplied. These results provide a basis for the rational design of collagen-like proteins for tissue engineering.
Because of changes in metabolism and the structure of connective tissues occurring during space flights, Dr. Fertala is interested in studies on designing gene-engineered collagens for promoting regeneration of bone and cartilage. The recombinant collagen-like proteins he designed and successfully expressed are under investigation structurally and biologically.
Keywords
COS Keywords:
Bone, Collagen, Connective Tissue, Dermatology, Diseases and Disorders, Extracellular Matrix.Additional Terms:
Collagen Fibril, Collagen Mutations, Extracellular Matrix, Recombinant Collagen.Languages
(Reading, Writing, Speaking)
Polish: (Fluent, Fluent, Fluent)
Memberships
American Society for Matrix Biology
Protein Society
Society of Investigative Dermatology
Patents
Inhibitors of collagen assembly,
Patent Number: 6472504,
2002,
Institution-owned,
United States.
Synthesis of human procollagens and collagens in recombinant DNA systems,
Patent Number: 5593859,
1997,
Institution-owned,
United States.
Synthesis of human procollagens and collagens in recombinant DNA systems,
Patent Number: 5405757,
1995,
United States.
Funding Received
- National Institutes of Health (NIH): , to .
- National Aeronautics and Space Administration (NASA): , to .
Publications
- Chung HJ, Steplewski A, Chung KY, Uitto J, Fertala A (Sep 2008) Collagen fibril formation. A new target to limit fibrosis., The Journal of biological chemistry, 283 (38), 25879-86
- Sweeney SM, Orgel JP, Fertala A, McAuliffe JD, Turner KR, Di Lullo GA, Chen S, Antipova O, Perumal S, Ala-Kokko L, Forlino A, Cabral WA, Barnes AM, Marini JC, San Antonio JD (Jul 2008) Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates., The Journal of biological chemistry, 283 (30), 21187-97
- Hintze V, Steplewski A, Ito H, Jensen DA, Rodeck U, Fertala A (Jun 2008) Cells expressing partially unfolded R789C/p.R989C type II procollagen mutant associated with spondyloepiphyseal dysplasia undergo apoptosis., Human mutation, 29 (6), 841-51
- Rodeck U, Fertala A, Uitto J (Jun 2007) Anchorless keratinocyte survival: an emerging pathogenic mechanism for squamous cell carcinoma in recessive dystrophic epidermolysis bullosa., Experimental dermatology, 16 (6), 465-7
- Cabral WA, Makareeva E, Letocha AD, Scribanu N, Fertala A, Steplewski A, Keene DR, Persikov AV, Leikin S, Marini JC (Apr 2007) Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype., Human mutation, 28 (4), 396-405
- Steplewski A, Hintze V, Fertala A (Feb 2007) Molecular basis of organization of collagen fibrils., Journal of structural biology, 157 (2), 297-307
- Twardowski T, Fertala A, Orgel JP, San Antonio JD (2007) Type I collagen and collagen mimetics as angiogenesis promoting superpolymers., Current pharmaceutical design, 13 (35), 3608-21
- Brittingham R, Uitto J, Fertala A (May 2006) High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV., Biochemical and biophysical research communications, 343 (3), 692-9
- Fujimoto N, Terlizzi J, Aho S, Brittingham R, Fertala A, Oyama N, McGrath JA, Uitto J (Apr 2006) Extracellular matrix protein 1 inhibits the activity of matrix metalloproteinase 9 through high-affinity protein/protein interactions., Experimental dermatology, 15 (4), 300-7
- Wang H, Fertala A, Ratner BD, Sage EH, Jiang S (Nov 2005) Identifying the SPARC binding sites on collagen I and procollagen I by atomic force microscopy., Analytical chemistry, 77 (21), 6765-71
- Ito H, Rucker E, Steplewski A, McAdams E, Brittingham RJ, Alabyeva T, Fertala A (Sep 2005) Guilty by association: some collagen II mutants alter the formation of ECM as a result of atypical interaction with fibronectin., Journal of molecular biology, 352 (2), 382-95
- Steplewski A, Brittingham R, Jimenez SA, Fertala A (Sep 2005) Single amino acid substitutions in the C-terminus of collagen II alter its affinity for collagen IX., Biochemical and biophysical research communications, 335 (3), 749-55
Profile Details
Last Verified: 4/3/2009
COS Expertise ID #959722
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Individual Expertise profile of Andrzej Fertala, Copyright Andrzej Fertala.
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