Carbonic anhydrases are enzymes that catalyze the reversible hydration of carbon dioxide according to the following reaction:
CO2 + H2O ↔ HCO3– + H+
The main function of this protein family is to regulate the acid-base balance, which is of considerable biological importance. In addition, they participate in several other physiological functions including CO2 and HCO3- transport, bone resorption, production of biological fluids, ureagenesis, gluconeogenesis, and lipogenesis. CAs are metalloenzymes containing a zinc-atom in their active site, whereas CARPs do not bind zinc because they lack some of the critical histidine residues which are critical for zinc binding.
The expanding alpha CA gene family includes 13 enzymatically active members with different structural and catalytic properties. Each isoform has a characteristic distribution in tissues.
We have previously shown that CA II, VII, IX and XII are expressed in various malignant tissues. Based on the distribution and functional studies, they may play a role in neoplastic processes such as invasion and increased cell proliferation. We have also demonstrated that Car9 defect in mouse results in a gastric phenotype with significant hyperplasia in the gastric epithelium. More recently, we have produced a novel knockout mouse model for CA VI deficiency.
Recently our studies have extended to cover other gene families of carbonic anhydrase including, importantly, the beta carbonic anhydrases. This family is present in a number of species while absent in mammals, providing a potential therapeutic target for certain diseases.
Our current studies aim to:
- Produce large amounts of recombinant alpha and beta carbonic anhydrases (CAs) and carbonic anhydrase-related proteins (CARPs) for kinetic and structural studies.
- Study the role of CARPs in tissues.
- Continue our studies on tumor-associated CA isozymes, CA II, CA VII, CA IX, and CA XII.
- Develop in-silico tools for transcription factor binding site (TFBS) prediction and analysis.
- Study the role of beta carbonic anhydrases in parasitic organisms, with the goal of impacting human and animal health.
Seppo Parkkila MD PhD University of Tampere
School of Medicine, Department of Anatomy/Tissue Biology
Seppo Parkkila M.D., Ph.D. (born 1966) is a Professor of Anatomy at the University of Tampere, Finland (www.uta.fi). He graduated from the University of Oulu in 1991 (M.D.) and obtained his PhD in 1994 under supervision of Professor Hannu Rajaniemi. From 1996-1998 he worked as a visiting researcher in the laboratory of Professor William S. Sly at Saint Louis University. He became a specialist physician in Clinical Chemistry in 2001. In 2002 he moved to the University of Tampere where he was appointed to the post of Professor of Medical Technology and Biotechnology, and later in 2008 to the post of Professor of Anatomy. His research work focuses on pH-regulation, carbonic anhydrases and regulation of iron homeostasis. Professor Parkkila has published over 200 articles in international journals and has a wide network of research collaborators around the world. He has supervised 13 PhD theses and a number of MSc thesis projects. Professor Parkkila has been actively involved in university administrative bodies. He is currently a vice-chairman of the board of the School of Medicine in Tampere. He is also a director of the MD-PhD program at the School of Medicine. In addition to these academic responsibilities, Professor Parkkila also actively participates in the politics of his home country. During the spring 2015 he is a candidate in the parliamentary elections representing the National Coalition Party of Finland (http://seppoparkkila.fi).
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