Proteinase Inhibitors and Resistance of Transgenic Plants to Insects

2010 ◽  
pp. 157-184 ◽  
Author(s):  
GERALD R REECK ◽  
KARL J KRAMER ◽  
JAMES E BAKER ◽  
MICHAEL R KANOST ◽  
JEFFREY A FABRICK ◽  
...  
2014 ◽  
Vol 185 ◽  
pp. S116
Author(s):  
Beibutgul Akimalieva Zhumabayeva ◽  
Erika Dimashevna Djangalina ◽  
Zaure Gaynetdinovna Aytasheva

HortScience ◽  
1994 ◽  
Vol 29 (4) ◽  
pp. 249e-249
Author(s):  
Dominique Michaud ◽  
Serge Overney ◽  
Binh Nguyen-Quoc ◽  
Serge Yelle

In the past few years, transformation of plant genomes with proteinase inhibitor (PI) genes has been proposed as an effective way to produce insect-tolerant plants. For such a control approach, however, biochemical studies are necessary to assess the effect of PIs on not only insect digestive proteinases (target enzymes) but also plant endogenous proteinases (nontarget enzymes). As an example, transformation of potato (Solanum tuberosum L.) with oryzacystatin (OC) genes, two cysteine PIs, was considered for controlling Colorado potato beetle (CPB; Leptinotarsa decemlineata Say). The use of electrophoretic approaches and standard assays showed that CPB uses at least 14 cysteine proteinases for protein digestion throughout its development. Proteinases of the same class were also detected in sprouting potato tuber extracts, suggesting a potential interference of cPIs in transgenic plants. While OCs inhibit a significant fraction of CPB digestive proteinases, no inactivation of potato proteinases was detected. This apparent absence of direct interference suggests the real potential of OCs for producing CPB-tolerant transgenic potato plants.


Author(s):  
James Baker ◽  
Jeffrey Fabrick ◽  
Michael Kanost ◽  
Gerald Reeck ◽  
Karl Kramer ◽  
...  

1987 ◽  
Vol 58 (02) ◽  
pp. 753-757 ◽  
Author(s):  
M F López-Fernández ◽  
C López-Berges ◽  
R Martín ◽  
A Pardo ◽  
F J Ramos ◽  
...  

SummaryThe multimeric and subunit patterns of plasma von Willebrand factor (vWF) were analyzed in eight patients with myeloproliferative syndrome (MS) in order to investigate the possible existence of heterogeneity in the “in vivo” proteolytic cleavage of the protein, previously observed in this entity. Six patients lacked large vWF multimers, five of them having normal bleeding times (BT) and clinically documented episodes of thrombotic origin, whereas one patient had long BT and bleeding symptoms. Seven patients showed a relative increase in the 176 kDa subunit fragment while the 189 kDa polypeptide was increased in only one. In addition, another patient (and prior to any therapy) showed the presence of a new fragment of approximately 95 kDa which disappeared after Busulfan therapy. The collection of blood from these patients with proteinase inhibitors did not correct the abnormalities.The infusion of DDAVP to two patients with abnormal vWF was accompanied by: the appearance of larger vWF multimers which disappeared rapidly from plasma; an increase in the relative proportion of the satellite bands of each multimer and a further increase of the 176 kDa fragment. These data point to some heterogeneity in the vWF abnormality present in MS which may be related in part to a variable degree of proteolysis of vWF occurring “in vivo” rather than “in vitro”, and which may be associated to either a thrombotic or a bleeding diathesis. They also suggest that despite the presence of abnormal, already proteolyzed vWF, DDAVP-enhanced proteolysis occurs in MS to a similar extent to what is described in normal individuals.


1984 ◽  
Vol 52 (03) ◽  
pp. 243-249 ◽  
Author(s):  
S Izaki ◽  
T Hibino ◽  
Y Isozaki ◽  
P S Hsu ◽  
M Izaki ◽  
...  

SummaryPlasminogen activator that is associated with the development of hypersensitivity granulomas (gPA) was partially purified from a saline soluble fraction of murine lepromas elicited in “resistant” mice, C57BL/6N. The gPA was shown to consist of two subspecies (23,000 and 48,000 in molecular weight) with essentially identical enzymologic properties. The gPA was found to be a relatively heat stable weakly alkaline serine proteinase with trypsin-like characteristics in the specificity for synthetic substrates and proteinase inhibitors. It showed a high affinity for H- D-Ile-Pro-Arg-pNA (Km = 1.4 × 10-4 M) H-D-Val-Leu-Lys- pNA (Km = 5.2 × 10-4 M), and L-pyroGlu-Gly-Arg-pNA (Km = 9.3 × 10-4 M). The gPA did not demonstrate antigenic cross reaction with urokinase-type or tissue-type plasminogen activator.Two distinct enzymatic regulators of the gPA were also demonstrated in the saline soluble fraction of the hypersensitivity granulomas. The gPA and its regulation are assumed to be correlated with macrophage activation in the hypersensitivity granulomas


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