Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function
-
Ying Dong
Abstract
Tissue kallikrein (kallikrein 1) was first identified in pancreas and is the namesake of the kallikrein-related peptidase (KLK) family. KLK1 and the other 14 members of the human KLK family are encoded by 15 serine protease genes clustered at chromosome 19q13.4. Our Northern blot analysis of 19 normal human tissues for expression of KLK4 to KLK15 identified pancreas as a common expression site for the gene cluster spanning KLK5 to KLK13, as well as for KLK15 which is located adjacent to KLK1. Consistent with previous reports detailing the ability of KLK genes to generate organ- and disease-specific transcripts, detailed molecular and in silico analyses indicated that KLK5 and KLK7 generate transcripts in pancreas variant from those in skin or ovary. Consistently, we identified in the promoters of these KLK genes motifs which conform with consensus binding sites for transcription factors conferring pancreatic expression. In addition, immunohistochemical analysis revealed predominant localisation of KLK5 and KLK7 in acinar cells of the exocrine pancreas, suggesting roles for these enzymes in digestion. Our data also support expression patterns derived from gene duplication events in the human KLK cluster. These findings suggest that, in addition to KLK1, other related KLK enzymes will function in the exocrine pancreas.
©2008 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function
- Transcriptional responses of Plasmodium falciparum to α-difluoromethylornithine-induced polyamine depletion
- Secondary structures and functional requirements for thiM riboswitches from Desulfovibrio vulgaris, Erwinia carotovora and Rhodobacter spheroides
- Secreted human apolipoprotein(a) kringle IV-10 and kringle V inhibit angiogenesis and xenografted tumor growth
- Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue
- Evaluation of the ‘side door’ in carboxylesterase-mediated catalysis and inhibition
- Functional tyrosine residue in the active center of human dipeptidyl peptidase III
- Development of a human adipocyte model derived from human mesenchymal stem cells (hMSC) as a tool for toxicological studies on the action of TCDD
- HNF4α orchestrates a set of 14 genes to down-regulate cell proliferation in kidney cells
- Effects of gastric inhibitory polypeptide (GIP) and related analogues on glucagon release at normo- and hyperglycaemia in Wistar rats and isolated islets
- Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen
Articles in the same Issue
- Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function
- Transcriptional responses of Plasmodium falciparum to α-difluoromethylornithine-induced polyamine depletion
- Secondary structures and functional requirements for thiM riboswitches from Desulfovibrio vulgaris, Erwinia carotovora and Rhodobacter spheroides
- Secreted human apolipoprotein(a) kringle IV-10 and kringle V inhibit angiogenesis and xenografted tumor growth
- Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue
- Evaluation of the ‘side door’ in carboxylesterase-mediated catalysis and inhibition
- Functional tyrosine residue in the active center of human dipeptidyl peptidase III
- Development of a human adipocyte model derived from human mesenchymal stem cells (hMSC) as a tool for toxicological studies on the action of TCDD
- HNF4α orchestrates a set of 14 genes to down-regulate cell proliferation in kidney cells
- Effects of gastric inhibitory polypeptide (GIP) and related analogues on glucagon release at normo- and hyperglycaemia in Wistar rats and isolated islets
- Cathepsin V, but not cathepsins L, B and K, may release angiostatin-like fragments from plasminogen
