Literature DB >> 11162388

Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin.

L Schwettmann1, H Tschesche.   

Abstract

ADAM 9 is a member of the cellular metalloprotease/disintegrin/cysteine-rich (MDC) gene family, related to soluble snake venom metalloproteases (SVMP). ADAMs may play important roles in cell-cell fusion, cell-matrix interaction, and other cellular functions. To investigate catalytic activity of human ADAM 9 we have cloned and expressed the metalloprotease domain of human ADAM 9 in Pichia pastoris. The recombinant protein was purified in a three-step purification procedure and activity was detected against gelatin, beta-casein, and fibronectin. In addition we identified five normal and cancer cell lines expressing mRNA of human ADAM 9. Copyright 2001 Academic Press.

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Year:  2001        PMID： 11162388     DOI： 10.1006/prep.2000.1374

Source DB:  PubMed          Journal:  Protein Expr Purif        ISSN： 1046-5928            Impact factor:   1.650


  12 in total

1.  Variability in melanoma metalloproteinase expression profiling.

Authors:  Orsi Giricz; Janelle L Lauer; Gregg B Fields
Journal:  J Biomol Tech       Date:  2010-12

2.  Characterization of a novel ADAM protease expressed by Pneumocystis carinii.

Authors:  Cassie C Kennedy; Theodore J Kottom; Andrew H Limper
Journal:  Infect Immun       Date:  2009-05-18       Impact factor: 3.441

3.  Inverse regulation of the ADAM-family members, decysin and MADDAM/ADAM19 during monocyte differentiation.

Authors:  Jana Fritsche; Alexandra Müller; Martin Hausmann; Gerhard Rogler; Reinhard Andreesen; Marina Kreutz
Journal:  Immunology       Date:  2003-12       Impact factor: 7.397

4.  Implication of ADAM-8, -9, -10, -12, -15, -17, and ADAMTS-1 in implantational remodeling of a mouse uterus.

Authors:  Jiyoung Kim; Sung Goo Kang; Jong Il Kim; Joo Hyun Park; Sei Kwang Kim; Dong Jae Cho; Haekwon Kim
Journal:  Yonsei Med J       Date:  2006-08-31       Impact factor: 2.759

5.  The cysteine-rich domain regulates ADAM protease function in vivo.

Authors:  Katherine M Smith; Alban Gaultier; Helene Cousin; Dominique Alfandari; Judith M White; Douglas W DeSimone
Journal:  J Cell Biol       Date:  2002-12-02       Impact factor: 10.539

Review 6.  Fine Tuning Cell Migration by a Disintegrin and Metalloproteinases.

Authors:  D Dreymueller; K Theodorou; M Donners; A Ludwig
Journal:  Mediators Inflamm       Date:  2017-02-05       Impact factor: 4.711

7.  Quantitative and dynamic expression profile of premature and active forms of the regional ADAM proteins during chicken brain development.

Authors:  Annett Markus; Xin Yan; Arndt Rolfs; Jiankai Luo
Journal:  Cell Mol Biol Lett       Date:  2011-07-18       Impact factor: 5.787

8.  Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans and retinal degeneration in mice.

Authors:  David A Parry; Carmel Toomes; Lina Bida; Michael Danciger; Katherine V Towns; Martin McKibbin; Samuel G Jacobson; Clare V Logan; Manir Ali; Jacquelyn Bond; Rebecca Chance; Steven Swendeman; Lauren L Daniele; Kelly Springell; Matthew Adams; Colin A Johnson; Adam P Booth; Hussain Jafri; Yasmin Rashid; Eyal Banin; Tim M Strom; Debora B Farber; Dror Sharon; Carl P Blobel; Edward N Pugh; Eric A Pierce; Chris F Inglehearn
Journal:  Am J Hum Genet       Date:  2009-04-30       Impact factor: 11.025

9.  ADAM9 is highly expressed in renal cell cancer and is associated with tumour progression.

Authors:  Florian R Fritzsche; Kirsten Wassermann; Monika Jung; Angelika Tölle; Ilka Kristiansen; Michael Lein; Manfred Johannsen; Manfred Dietel; Klaus Jung; Glen Kristiansen
Journal:  BMC Cancer       Date:  2008-06-26       Impact factor: 4.430

Review 10.  ADAM and ADAMTS family proteins and their role in the colorectal cancer etiopathogenesis.

Authors:  Leszczynski Przemyslaw; Hendrich Andrzej Boguslaw; Szmida Elzbieta; Sasiadek Maria Malgorzata
Journal:  BMB Rep       Date:  2013-03       Impact factor: 4.778
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