Felix Grissom, Ph.D.
Associate Professor


Contact Information:
Office: Numa P. G. Adams Bldg., Suite: 2305
Office Telephone: 202-806-6346


BS., Shaw University (1965)
MS., NC State University (1971)
Ph.D., NC State University (1976)
Public Health Service Fellow, Duke University and Univ. Of Iowa (1976-9)

Dental Physiology
Advances in Endocrinology

Research Interests
Insulin-like growth factor binding  protein (IGFBP)regulation of bone cell growth.                    
Extracellular matrix regulation of IGF axis activity in normal and disease states (prostate cancer metastasis to bone, suppressed diabetic wound healing, suppressed cartilage regeneration in arthritic joints).

Research Details

Characterization of aggrecan-related peptides associated with suppression of chrondrocyte activity in arthritic knee joints.
This project is focused on the generation, structure and activity of five aggrecan-related peptides found in synovial fluid of arthritic knee joints.  The study proposes to determine if the fragments are generated by cleavage of intact aggrecan and , if so, what conditions are required for this selective degradation.  Additionally, an examination of the mechanism(s) whereby these fragments suppress both growth and secretory activity of chrondrocytes including extracellular availability of IGF for chrondrocyte stimulation and the role of a putative chrondrocyte binding site for two of these peptides on intracellular second messenger cascades associated with chrondrocyte growth and secretory activity.

Roles of IGFBP-3 and IGFBP-5 on the inhibition and stimulation, respectively, of diabetic wound fibroblasts fibroblasts. 
This project examines the actions of IGFBP-3 and IGFBP-5 which are elevated in non-healing and healing areas, respectively, of diabetic and other slow healing wounds.  The mechanism of the induction of increased IGFBP-3 binding to plasma membrane of fibroblasts and its effect on growth and ECM protein secretion are one focus of this study.  A second focus is the mechanism associated with increased IGFBP-5 production by fibroblasts which occurs simultaneous with a reduction of the IGFBP-3 inhibition and a return to near normal of fibroblasts healing regions of slow-healing wounds.       

Selected Publications
Grissom, F.E., Watson-Hampton, S.N., Rust, C. F., Austin, K. and Anderson, W.A. Measurement of insulin-like growth factor binding protein (IGFBP) binding characteristics on nitrocellulose. Under Review Anal Biochem.

Watson-Hampton, S.N., Rust C. F., Austin, K., Green, W. And Grissom, F.E.  Unique high molecular weight forms of insulin-like growth factor binding proteins are found in synovial fluid from the joints of arthritic subjects.   Under Review Bone Research.

Macias, C.L., Williams, K., Baccetti, B., Renieri, T., Reddi, H., Asseffa, A., Hollis, V., Grissom, F and Anderson, W. Culture and co-culture of DU145 prostate carcinoma, osteoblasts, and HT-29 colon carcinoma cells on a fabricated type III collagen matrix. J. Submicrosc. Cytol Pathol. 82, 241-53 2002.

Grissom, F.E., Carlsson-Skwirut, C., Laurenzi, M.A., Collins, V.P., and Sara. V.R.  Characterization of insulin-like growth factor binding proteins from a glioblastoma cell line.  Acta Endocrinol. 143,238-45 1996.

Tham, A., Nordberg, A., Grissom, F.E., Carlsson-Swirut, C., Vitanen, M. and Sara, V.R.  Insulin-like growth factors and insulin-like growth factor binding proteins in cerebrospinal fluid and serum of patients with dementia of the Alzheimer's type. J. Neural. [P-D Sect.]  5, 165-176, 1993.                           

Sandberg-Nordqvist, A-C., Carlson-Skirut, C., Ehrenborg, E., Grissom, F.E. and Sara, V.R. Comparison of Insulin-like growth factors and their binding proteins in glioblastoma and  neuroblastoma cells. Ann NY Acad Sci., 692, 297-299, 1993  

Grissom, F.E., Rivero-Crespo, F., Lindgren, B. and Hall, K. Quantitative ligand blot analysis: Validation and utilization for measurement of truncated insulin-like growth factor regulation of Hep-G2 cell insulin-like growth factor binding protein-1 (IGFBP-1) secretion.  Anal. Biochem. 212, 412420, 1993.