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Denise C. Hocking, Ph.D.

Contact Information

Phone Numbers

Fax: (585) 273-2652

Office: (585) 273-1770

Research Labs

Biography

Research

Research in the Hocking lab focuses on understanding the mechanisms by which the extracellular matrix protein, fibronectin, affects cell and tissue functions that are critical for wound repair. We study both the structural mechanisms and intracellular signaling events that mediate cell and tissue responses to matrix fibronectin. In turn, we are using this information to develop novel technologies for tissue engineering, and therapeutic approaches to promote tissue regeneration in chronic wounds. The Extracellular Matrix: What is it? The extracellular matrix (ECM) is a complex, three-dimensional network comprised of collagens, glycoproteins, and proteoglycans that provides an adhesive substrate for the organization of cells into tissues. In the adult, dynamic interactions between cells and their surrounding ECM proteins regulate most, if not all, cell and tissue functions. ECM proteins also contribute to the mechanical and permeability properties of the skin, vasculature, lungs, and other organs. Fibronectin is a principal component of the ECM, where it is organized into elongated, branching fibrils. Mechanical forces influence the deposition, organization, and structure of ECM fibronectin fibrils, which in turn, affect cell function, ECM organization and stability, vascular perfusion, blood vessel permeability, and tissue strength. Fibronectin is initially secreted by cells in a soluble, protomeric form. Soluble fibronectins are then polymerized into ECM fibrils by means of a tightly-regulated, cell-dependent mechanism that can be rapidly up- or down-regulated. Fibronectin matrix polymerization is increased in response to tissue injury; altered fibronectin matrix deposition is associated with abnormal tissue repair in a number of chronic inflammatory states, including non-healing wounds, asthma, pulmonary fibrosis, and atherosclerosis. In the body, fibronectin polymerization is a continuous process, with as much as 50% of the fibronectin matrix undergoing turnover every 24 hours. In spite of this remarkable information, the mechanisms of fibronectin matrix polymerization and the function of ECM fibronectin fibrils in vivo is not well understood. Studies from the Hocking Lab: What have we learned about fibronectin? Research in the Hocking lab has been directed at determining whether and how this three-dimensional fibronectin matrix regulates cell behaviors that are essential to tissue repair. Our studies have firmly established that cells respond differently to soluble versus ECM fibronectin, and that the ECM form is the primary functional form of fibronectin. We have shown that the conversion of fibronectin into the ECM form specifically stimulates cell spreading, cell migration, and collagen matrix contraction – all cellular events critical to tissue regeneration. We have also shown that the assembly of a fibronectin matrix promotes the co-polymerization of collagen I and enhances the tensile strength of model tissue, thus demonstrating that the organization and functional properties of the ECM are also dependent on fibronectin matrix polymerization. We have localized several of the ECM-specific effects of fibronectin to a single, cryptic heparin-binding site in the first type III module of fibronectin (FNIII-1). This conformation-dependent, or "matricryptic" site is not exposed in soluble fibronectin, but becomes unmasked during fibronectin matrix formation or as cells and tissues exert tension on ECM fibronectin fibrils. Our exciting new studies, conducted in collaboration with the laboratory of Dr. Ingrid Sarelius, demonstrate that exposure of this matricryptic site in vivo mechanically couples skeletal muscle contraction with local vasodilation. These were the first studies to demonstrate a role for fibronectin fibrils in adult connective tissue in vivo.

Credentials

Faculty Appointments

Education

1983
BS | Hartwick College
Medical Technology

1992
PhD | Albany Medical College
Physiology

1990
MS | Albany Medical College
Physiology

Awards

1990
Proctor and Gamble Career Opportunity Award, American Physiological Society.

Patents

Title: Chimeric Fibronectin Matrix Mimetics and Uses Thereof
U.S. Serial #: 14/743,485
Filed: Jun 18, 2015
Invented By: DeniseHocking, DanielRoy

Title: Controlling Collagen Microstructure with Ultrasound
U.S. Serial #: 14/389,283
Filed: Mar 14, 2013
Invented By: DianeDalecki, KelleyGarvin, DeniseHocking

Title: Chimeric Fibronectin Matrix Mimetics and Uses Thereof
U.S. Serial #: 13/994,179
Filed: Dec 14, 2011
Invented By: DeniseHocking, DanielRoy

Title: Ultrasound Technology to Control the Spatial Organization of Cells and Proteins in Engineered Tissues
U.S. Serial #: 13/321,218
Filed: Apr 15, 2010
Invented By: DianeDalecki, KelleyGarvin, DeniseHocking

Title: Ultrasound Technology to Control the Spatial Organization of Cells and Proteins in Engineered Tissues
U.S. Serial #:
Filed: Jan 01, 1899
Invented By: DianeDalecki, KelleyGarvin, DeniseHocking

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Publications

Journal Articles

1/1/2017
Comeau ES, Hocking DC, Dalecki D. "Ultrasound patterning technologies for studying vascular morphogenesis in 3D." Journal of cell science.. 2017 Jan 1; 130(1):232-242. Epub 2016 Oct 27.

11/1/2016
Hocking DC, Brennan JR, Raeman CH. "A Small Chimeric Fibronectin Fragment Accelerates Dermal Wound Repair in Diabetic Mice." Advances in wound care.. 2016 Nov 1; 5(11):495-506.

10/1/2016
Okech W, Abberton KM, Kuebel JM, Hocking DC, Sarelius IH. "Extracellular matrix fibronectin mediates an endothelial cell response to shear stress via the heparin-binding, matricryptic RWRPK sequence of FNIII1H." American journal of physiology. Heart and circulatory physiology.. 2016 Oct 1; 311(4):H1063-H1071. Epub 2016 Aug 12.

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