PH.D. University of Alberta
B. Chemistry Universidad Autonoma del Estado de Mexico
Professor, Department of Physiology and Pharmacology
Children's Health Research Institute
Scientist, Developmental Biology Program
Lawson Health Research Institute
Scientist, Children's Health Research Institute
Dr. Dagnino’s research focus is on skin biology and stem cells. Her expertise includes cellular and molecular biology, as well as developmental genetics.
The skin is the largest organ in the body. It weighs 6-9 pounds and, if one could take it off and lay it flat, it would cover an area of about 20 ft2 (2 m2). The skin fulfills myriad functions. It serves as a barrier between the body and the outside environment, protecting it from chemicals, physical damage, and entry of infectious organisms. It also prevents dehydration and heat loss, and allows perception of touch, a quintessential source of sensory stimulation. Three layers form the skin. The uppermost layer is the epidermis, which is formed by epithelial cells called keratinocytes.
These cells also form hair, nails, teeth and sebaceous glands. Keratinocyte stem cells constantly differentiate and migrate from the base of the epidermis towards the outer surface of the skin, where they are sloughed off. This process normally takes about a month, but in people suffering from skin disorders, such as psoriasis, it can be accelerated, sometimes occurring in a few days. Over 30,000 cells are shed from the skin every minute, and the skin can be maintained only because it has a large reservoir of keratinocyte stem cells.
Dr. Dagnino’s laboratory works on the mechanisms that are involved in cellular decisions to maintain an undifferentiated, stem-cell phenotype or follow a pathway of terminal differentiation in the keratinocytes of the epidermis. Her group is currently investigating how those mechanisms regulate normal regeneration after wounding, abnormal proliferation and cancer, as well as how they contribute to block microbial invasion.
L Vi, C de Lasa, G DiGuglielmo and L Dagnino. Integrin-linked kinase is essential for transforming growth factor-beta induced myofibroblast differentiation. J Invest Dermatol 131:586-593, 2011
L Dagnino. Integrin-linked kinase: A scaffold protein unique among its ilk. J Cell Commun Signal, 5:81-83, 2011
KA Nakrieko, A Rudkouskaya, TS Irvine, SJA D’Souza and L Dagnino. Targeted inactivation of integrin-linked kinase in hair follicle stem cells reveals an important modulatory role in skin repair after injury. Mol Biol Cell, 14:2532-2540, 2011
E Ho and L Dagnino. Epidermal growth factor induction of front-rear polarity and migration in keratinocytes is mediated by integrin-linked kinase and ELMO2. Mol Biol Cell 23: 492-502, 2012
D Judah, A Rudkouskaya, R Wilson, D. E. Carter and L Dagnino. Multiple roles of integrin-linked kinase inepidermal development, maturation and pigmentation revealed by molecular profiling. PLOS One, 7(5):e36704, 2012
E Ho and L Dagnino. Emerging role of ILK and ELMO2 in the integration of adhesion and migration pathways. Cell Adhesion and Migration 6 (3): 168-172, 2012
S Sayedyahossein, L Nini, TS Irvine, and L Dagnino. Essential role of integrin-linked kinase in regulation of phagocytosis in keratinocytes. FASEB J, 26:4218-4229, 2012
S Sayedyahossein, and L Dagnino. Integrins and small GTPases as modulators of phagocytosis. Int Rev Cell Mol Biol 302: 319-352, 2013.
S Boo and L Dagnino. Integrins as modulators of TGF-signaling in skin regeneration after injury. Adv Wound Care 2:225-237, 2013.
A Rudkouskaya, I Welch, L Dagnino. ILK modulates epithelial polarity and matrix formation in hair follicles. Mol Biol Cell 25(5): 620-632, 2014 (E pub ahead of print Dec 2013)
L Vi, HS Boo, S Sayedyahossein, RK Singh, S McLean, GM Di Guglielmo, and L Dagnino. Modulation of type II TGF- receptor degradation by integrin-linked kinase. J Invest Dermatol 135(3): 885-894, 2015; Epub Sep 30, 2014, doi: 10.1038/jid.2014.427
S Sayedyahossein, SX Xu, A Rudkouskaya, MJ McGavin, JK McCormick, L Dagnino. Staphylococcus aureus keratinocyte invasion is mediated by integrin-linked kinase and Rac1. FASEB J 29(2): 711-723, 2015; Epub Nov 21, 2014