Bovine Pancreatic Preproelastases I and II: Comparison of Nucleotide and Amino Acid Sequences and Tissue Specific Expression

• Published in: Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology Vol. 118; no. 1; pp. 181 - 187
• Main Authors: Gestin, Martine, Le Huërou-Luron, Isabelle, Wicker-Planquart, Catherine, Le Dréan, Gwenola, Chaix, Jean-Claude, Puigserver, Antoine, Guilloteau, Paul
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.09.1997; Elsevier
• Subjects: Amino Acid Sequence; Animals; Base Sequence; calf; Cattle; Cloning, Molecular; DNA Primers - genetics; DNA, Complementary - genetics; elastases I and II; Enzyme Precursors - chemistry; Enzyme Precursors - genetics; Enzyme Precursors - metabolism; Food and Nutrition; Gene Expression; Human health and pathology; Life Sciences; Molecular Sequence Data; nucleotide and amino acid sequences; Pancreas; Pancreas - enzymology; Pancreatic Elastase - chemistry; Pancreatic Elastase - genetics; Pancreatic Elastase - metabolism; Polymerase Chain Reaction; RNA, Messenger - genetics; RNA, Messenger - metabolism; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Tissue Distribution; Tissues and Organs; tissular expression; elastases I and II; nucleotide and amino acid sequences; tissular expression; Pancreas; calf; Pancreas/enzymology; Pancreatic Elastase/chemistry; DNA, Complementary/genetics; RNA, Messenger/metabolism; Polymerase Chain Reaction
• ISSN: 1096-4959; 1879-1107
• DOI: 10.1016/S0305-0491(97)00031-X

Clones encoding bovine preproelastases I and II were isolated from a pancreatic cDNA library and were sequenced in order to define the structural characteristics of these enzymes. The bovine 947- and 884- nucleotide preproelastase I and II cDNAs encode proteins containing a signal peptide of the same length (16 amino acids), but with a slightly different number of amino acids for the activation peptide (10 and 12, respectively) and the mature enzyme (240 and 241, respectively). Considering amino acid sequences, each enzyme shares a high degree of identity (76–86%) within species. In contrast, only 55.3% identity is found between bovine elastases I and II. This difference could explain partly their own specificity. Analysis of the expression of the elastases in various bovine tissues demonstrated that they are specifically expressed in high levels in the pancreatic gland. These two approaches (structure and expression) allowed us to characterize the bovine pancreatic elastases I and II.