HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Faro, C. Articles by Pires, E. Search for Related Content PubMed PubMed Citation Articles by Faro, C. Articles by Pires, E. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 40, 28724-28729, October 1, 1999

Cloning and Characterization of cDNA Encoding Cardosin A, an RGD-containing Plant Aspartic Proteinase

Carlos Faro, Miguel Ramalho-Santos, Margarida Vieira, Alexandra Mendes, Isaura Simões, Rita Andrade, Paula Veríssimo, Xin-li Lin^**, Jordan Tang^**, and Euclides Pires

From the  Departamento de Bioquímica, Faculdade de Ciências e Tecnologia and Departamento Biologia Molecular e Biotecnologia, Centro de Neurociências e Biologia Celular, Universidade de Coimbra, 3000 Coimbra, Portugal and the ^** Protein Studies Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104

Cardosin A is an abundant aspartic proteinase from pistils of Cynara cardunculus L. whose milk-clotting activity has been exploited for the manufacture of cheese. Here we report the cloning and characterization of cardosin A cDNA. The deduced amino acid sequence contains the conserved features of plant aspartic proteinases, including the plant-specific insertion (PSI), and revealed the presence of an Arg-Gly-Asp (RGD) motif, which is known to function in cell surface receptor binding by extracellular proteins. Cardosin A mRNA was detected predominantly in young flower buds but not in mature or senescent pistils, suggesting that its expression is likely to be developmentally regulated. Procardosin A, the single chain precursor, was found associated with microsomal membranes of flower buds, whereas the active two-chain enzyme generated upon removal of PSI is soluble. This result implies a role for PSI in promoting the association of plant aspartic proteinase precursors to cell membranes. To get further insights about cardosin A, the functional relevance of the RGD motif was also investigated. A 100-kDa protein that interacts specifically with the RGD sequence was isolated from octyl glucoside pollen extracts by affinity chromatography on cardosin A-Sepharose. This result suggests that the 100-kDa protein is a cardosin A receptor and indicates that the interaction between these two proteins is apparently mediated through RGD recognition. It is possible therefore that cardosin A may have a role in adhesion-mediated proteolytic mechanisms involved in pollen recognition and growth.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				P. Castanheira, B. Samyn, K. Sergeant, J. C. Clemente, B. M. Dunn, E. Pires, J. Van Beeumen, and C. Faro Activation, Proteolytic Processing, and Peptide Specificity of Recombinant Cardosin A J. Biol. Chem., April 1, 2005; 280(13): 13047 - 13054. [Abstract] [Full Text] [PDF]

				C. L. C. Esteves, J. A. Lucey, T. Wang, and E. M. V. Pires Effect of pH on the Gelation Properties of Skim Milk Gels Made From Plant Coagulants and Chymosin J Dairy Sci, August 1, 2003; 86(8): 2558 - 2567. [Abstract] [Full Text] [PDF]

				C. Egas, N. Lavoura, R. Resende, R. M. M. Brito, E. Pires, M. C. P. de Lima, and C. Faro The Saposin-like Domain of the Plant Aspartic Proteinase Precursor Is a Potent Inducer of Vesicle Leakage J. Biol. Chem., December 1, 2000; 275(49): 38190 - 38196. [Abstract] [Full Text] [PDF]