@article {468,
	title = {Purification of a cysteine protease inhibitor from larval hemolymph of the tobacco hornworm (Manduca sexta) and functional expression of the recombinant protein},
	volume = {37},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalLaboratory of Food Molecular Functionality, College of Agriculture, Ibaraki University, 3-21-1 Chuo, Ami-machi, Inashiki-gun, Ibaraki 300-0393, Japan.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=17681235},
	pages = {960 - 968},
	abstract = {A cysteine protease inhibitor (CPI) with an apparent molecular mass of 11.5kDa was purified from larval hemolymph of the tobacco hornworm (Manduca sexta) by gel filtration on Sephadex G-50 followed by hydrophobic and ion-exchange column chromatographies. The purified cysteine proteinase inhibitor, denoted as MsCPI, strongly inhibited the plant cysteine protease, papain, with a K(i) value of 5.5 x 10(-9)M. Nucleotide sequence analysis of a partial cDNA encoding MsCPI indicated that MsCPI consists of 105 amino acid residues in a sequence that is similar to sarcocystatin A from Sarcophaga peregrina. However, northern blotting and PCR analyses using the specific primers of MsCPI suggested that the mRNA encoding MsCPI had a size of more than 12 kilobases, which included at least six tandemly repeated MsCPI segments. MsCPI was expressed in Escherichia coli and the recombinant protein effectively inhibited cysteine proteases from plants as well as from animals such as cathepsins B (K(i), 6.8 nM), H (3.0 nM), and L (0.87 nM). There was no inhibition exhibited toward trypsin, chymotrypsin, subtilisin, pepsin or themolysin.},
	keywords = {Amino Acid Sequence, Animals, Cathepsins/drug effects/isolation \&amp, Cloning, Molecular, Conserved Sequence, Cysteine Proteinase Inhibitors/genetics/*isolation \&amp, development, DNA Primers, Escherichia coli/genetics, Hemolymph/*chemistry, Humans, inhibitors, Larva, Manduca/*growth \&amp, Molecular Sequence Data, Papain/antagonists \&amp, Polymerase Chain Reaction, purification/metabolism, purification/pharmacology, Recombinant Proteins/isolation \&amp, Sequence Alignment, Sequence Homology, Amino Acid},
	author = {Miyaji, T. and Kouzuma, Y. and Yaguchi, J. and Matsumoto, R. and Kanost, M. R. and Kramer, K. J. and Yonekura, M.}
}
@article {38,
	title = {Contact angioedema and rhinoconjunctivitis caused by Dendrobaena species and Sarcophaga carnaria used as fishing bait},
	volume = {21},
	year = {Submitted},
	note = {28-12-201106-02-2012Department of Allergology, Hospital Puerta de Hierro, Majadahonda, Madrid, Spain.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=21721377},
	pages = {305 - 309},
	abstract = {The flesh fly Sarcophaga carnaria is commonly used as fishing bait. Immunoglobulin (Ig) E-mediated reactions caused by the handling of this bait have been reported. The earthworm Dendrobaena species is increasingly being used as fishing bait but there have been no reported cases of allergy to this species to date. We studied a 26-year-old amateur angler who presented rhinoconjunctivitis, urticaria, and angioedema on handling S carnaria. He started to use Dendrobaena species instead but developed the same symptoms. The aim of this study was to identify the allergens involved in the patient{\textquoteright}s clinical reactions. The study was performed using immunoglobulin (Ig) E immunoblotting and immunoblotting inhibition assays.The patient{\textquoteright}s serum detected allergens from Dendrobaena species (of an apparent molecular weight of approximately 150, 60, 37, 24, 21 and 19 kDa) and S. carnaria (approximately 70 kDa and a smear ranging from 50 to 40 kDa). The patient was diagnosed with allergy to both Dendrobaena species and 5 carnaria. This is the first case describing Dendrobaena species as an allergic agent.},
	keywords = {Adult, Allergens/immunology, Animals, Conjunctivitis, Allergic/*etiology/immunology, Dermatitis, Allergic Contact/*etiology/immunology, Hand Dermatoses/etiology/immunology, Hobbies, Humans, Immunoglobulin E/immunology, Larva, Male, Oligochaeta/*immunology, Rhinitis, Allergic, Perennial/*etiology/immunology, Sarcophagidae/*immunology, Skin Tests},
	author = {Garcia-Loria, J. and Rodriguez-Perez, R. and Iglesias, A. and Moneo, I. and Caballero, M. L.}
}
