Int J Biochem Mol Biol 2013;4(3):129-139
Review Article
Biochemical and structural insights into mesotrypsin: an unusual hu-man trypsin
Moh’d A Salameh, Evette S Radisky
Department of Bioscience Technology, Gwinnett Technical College, Lawrenceville, GA, 30043, USA; Department of Cancer Biology, Mayo Clinic
Cancer Center, Jacksonville, FL 32224, USA
Received July 31, 2013; Accepted August 23, 2013; Epub September 13, 2013; Published September 15, 2013
Abstract: Thirty five years ago mesotrypsin was first isolated from the human pancreas. It was described as a minor trypsin isoform with the
remarkable property of near total resistance to biological trypsin inhibitors. Another unusual feature of mesotrypsin was discovered later, when
it was found that mesotrypsin has defective affinity toward many protein substrates of other trypsins. As the younger sibling of the two major
trypsins secreted by the pancreas, cationic and the anionic trypsin, it has been speculated to represent an evolutionary waste with no apparent
function. We know now that mesotrypsin is functionally very different from the other trypsins, with novel substrate specificity that hints at distinct
physiological functions. Recently, evidence has begun to emerge implicating mesotrypsin in direct involvement in cancer progression. This
review will explore the biochemical characteristics of mesotrypsin and structural insights into its specificity, function, and inhibition.
(IJBMB1307010).
Keywords: Trypsin, mesotrypsin, serine protease, protease inhibitors, protein crystallography, substrate specificity, cancer progression
Address correspondence to: Dr. Moh’d A Salameh, Department of Bioscience Technology, Gwinnett Technical College, Lawrenceville, GA,
30043, USA. E-mail: msalameh@gwinnetttech.edu
Review Article
Biochemical and structural insights into mesotrypsin: an unusual hu-man trypsin
Moh’d A Salameh, Evette S Radisky
Department of Bioscience Technology, Gwinnett Technical College, Lawrenceville, GA, 30043, USA; Department of Cancer Biology, Mayo Clinic
Cancer Center, Jacksonville, FL 32224, USA
Received July 31, 2013; Accepted August 23, 2013; Epub September 13, 2013; Published September 15, 2013
Abstract: Thirty five years ago mesotrypsin was first isolated from the human pancreas. It was described as a minor trypsin isoform with the
remarkable property of near total resistance to biological trypsin inhibitors. Another unusual feature of mesotrypsin was discovered later, when
it was found that mesotrypsin has defective affinity toward many protein substrates of other trypsins. As the younger sibling of the two major
trypsins secreted by the pancreas, cationic and the anionic trypsin, it has been speculated to represent an evolutionary waste with no apparent
function. We know now that mesotrypsin is functionally very different from the other trypsins, with novel substrate specificity that hints at distinct
physiological functions. Recently, evidence has begun to emerge implicating mesotrypsin in direct involvement in cancer progression. This
review will explore the biochemical characteristics of mesotrypsin and structural insights into its specificity, function, and inhibition.
(IJBMB1307010).
Keywords: Trypsin, mesotrypsin, serine protease, protease inhibitors, protein crystallography, substrate specificity, cancer progression
Address correspondence to: Dr. Moh’d A Salameh, Department of Bioscience Technology, Gwinnett Technical College, Lawrenceville, GA,
30043, USA. E-mail: msalameh@gwinnetttech.edu
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