Aiping M Zhao

Publication Detail

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Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes.

John P Hobson; Sarah Netzel-Arnett; Roman Szabo; Sophie M Réhault; Frank C Church; Dudley K Strickland; Daniel A Lawrence; Toni M Antalis; Thomas H Bugge (Profiled Authors: Toni Antalis; Dudley K Strickland)

Proteases and Tissue Remodeling Unit, NIDCR, National Institutes of Health, Bethesda, Maryland 20892, USA.
The Journal of biological chemistry 2004;279(45):46981-94.

We report the identification and functional analysis of a type II transmembrane serine protease encoded by the mouse differentially expressed in squamous cell carcinoma (DESC) 1 gene, and the definition of a cluster of seven homologous DESC1-like genes within a 0.5-Mb region of mouse chromosome 5E1. This locus is syntenic to a region of human chromosome 4q13.3 containing the human orthologues of four of the mouse DESC1-like genes. Bioinformatic analysis indicated that all seven DESC1-like genes encode functional proteases. Direct cDNA cloning showed that mouse DESC1 encodes a multidomain serine protease with an N-terminal signal anchor, a SEA (sea urchin sperm protein, enterokinase, and agrin) domain, and a C-terminal serine protease domain. The mouse DESC1 mRNA was present in epidermal, oral, and male reproductive tissues and directed the translation of a membrane-associated 60-kDa N-glycosylated protein with type II topology. Mouse DESC1 was synthesized in insect cells as a zymogen that could be activated by exposure to trypsin. The purified activated DESC1 hydrolyzed synthetic peptide substrates, showing a preference for Arg in the P1 position. DESC1 proteolytic activity was abolished by generic inhibitors of serine proteases but not by other classes of protease inhibitors. Most interestingly, DESC1 formed stable inhibitory complexes with both plasminogen activator inhibitor-1 and protein C inhibitor that are expressed in the same tissues with DESC1, suggesting that type II transmembrane serine proteases may be novel targets for serpin inhibition. Together, these data show that mouse DESC1 encodes a functional cell surface serine protease that may have important functions in the epidermis, oral, and reproductive epithelium.

5 Originating Grant

• 1.

  Antalis, Toni M

  New Function for the Serpin PAI-2 as a Regular of pRb

  1 August 2003 - 31 May 2009

  NATIONAL CANCER INSTITUTE

• 2.

  Antalis, Toni M

  NEW FUNCTION SERPIN PAI 2 AS A REGULAR OF RB

  1 July 2002 - 30 June 2010

  NATIONAL CANCER INSTITUTE

• 3.

  STRICKLAND, DUDLEY K.

  Information Signaling Pathways in the Vasculature

  1 May 1997 - 31 March 2012

  NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

• 4.

  STRICKLAND, DUDLEY K.

  Regulation of Surface Receptors by LRP

  30 September 1993 - 30 June 2012

  NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

• 5.

  STRICKLAND, DUDLEY K.

  Vascular Biology Training Program

  1 July 1991 - 31 August 2014

  NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

Scientific Context

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