Advanced search×

The structural requirements of matriptase in its ectodomain release in polarized epithelial cells.

Satoshi S Tsuzuki, Nobuhito N Murai, Yuka Y Miyake, Kuniyo K Inouye, and Tohru T Fushiki

Biosci Biotechnol Biochem 74(6):1295-7 (2010) PMID 20530886

Matriptase is a type-II transmembrane serine protease abundantly expressed in polarized epithelia. The ectodomain of matriptase is released from the cell surface. In the present study, we found that the post-translational cleavage between Gly149 and Ser150 and the existence of catalytic domain are critical for the ectodomain release of matriptase in stable transfection experiments using the polarized Madin-Darby canine kidney epithelial cell line.

Version: za2963e q8zae q8zb0 q8zc7 q8zdf q8ze7 q8zf2 q8zg7
View PDF

Similar articles you may find interesting…

  1. Identification of the matriptase second CUB domain as the secondary site for interaction with hepatocyte growth factor activator inhibitor t...
    Kuniyo K Inouye, Satoshi S Tsuzuki, ... Tohru T Fushiki

    Audio, Transactions of the IRE Profe... 285(43):33394-403 (2010) PMID 20682770 PMCID PMC2963394

    We also found that MAT undergoes cleavage between Lys(379) and Val(380) within CUB domain II and that the C-terminal residues after Val(380) are responsible for facilitating the interaction with HAI-1-58K. A synthetic peptide corresponding to Val(380)-Asp(390) markedly increased the matriptase-inhib...
    View PDF
  2. Effects of organic solvents on the reverse transcription reaction catalyzed by reverse transcriptases from avian myeloblastosis virus and Mo...
    Kiyoshi K Yasukawa, Atsushi A Konishi, and Kuniyo K Inouye

    Audio, Transactions of the IRE Professio... 74(9):1925-30 (2010) PMID 20834159

    We examined the effects of dimethyl sulfoxide (DMSO), formamide, and glycerol on the reverse transcription reaction catalyzed by reverse transcriptases (RTs) from avian myeloblastosis virus (AMV) and Moloney murine leukemia virus (MMLV). At 42 °C, DMSO at 24% v/v and formamide at 12-14% inhibited t...
    View PDF
  3. Structure-function analysis of vitamin D 24-hydroxylase (CYP24A1) by site-directed mutagenesis: amino acid residues responsible for species-...
    Hiromi Hamamoto, Tatsuya Kusudo, ... Toshiyuki Sakaki

    Mol Pharmacol 70(1):120-8 (2006) PMID 16617161

    We tried to identify amino acid residues that cause the species-based difference by site-directed mutagenesis. In the putative substrate-binding regions, amino acid residue of rat CYP24A1 was converted to the corresponding residue of human CYP24A1. Among eight mutants examined, T416M and I500T showe...