[59] Lima bean trypsin inhibitors

Birk, Yehudith

doi:10.1016/s0076-6879(76)45062-0

Cited by 15 publications

(8 citation statements)

References 7 publications

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“…The enzyme we have characterized is unusual in that it is inhibited by BBI (which inhibits trypsin and chymotrypsin) (30), chymostatin, and TPCK (chymotrypsin inhibitors) (31,32), but it is not inhibited by SBTI (a trypsin inhibitor) (33). Therefore, this protease is trypsin-like in that it cleaves a substrate with arginine at the pl site, but it is unlike trypsin in its sensitivity to chymostatin and TPCK.…”

Section: Resultsmentioning

confidence: 96%

A serine protease activity in C3H/10T1/2 cells that is inhibited by anticarcinogenic protease inhibitors.

Billings¹,

Carew²,

Keller-McGandy³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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Several different protease inhibitors have the ability to suppress transformation in vitro and carcinogenesis in vivo. The mechanism(s) by which protease inhibitors suppress carcinogenesis, however, is not fully understood. Presumably, these agents inhibit one (1, 2, 4).The mechanism by which protease inhibitors suppress malignant transformation is unknown. We believe they act by inhibiting one or more proteases that are critical for the induction and/or expression of the transformed phenotype. One approach to determining how protease inhibitors suppress carcinogenesis involves the identification of the particular cellular protease(s) with which the anticarcinogenic protease inhibitors interact. We have assayed C3H/1OTV2 cell homogenates for protease activity using many different fluorogenic substrates (with different amino acid sequences) and have observed that the cleavage of all but two of these substrates is unaffected by protease inhibitors that suppress malignant transformation. The present report involves a detailed study of a particular cellular proteolytic activity in C3H/10T½ cells that is strongly inhibited by the anticarcinogenic protease inhibitors. The anticarcinogenic protease inhibitors utilized here prevent malignant transformation induced by many different carcinogens in in vitro and in vivo carcinogenesis systems (1-6).

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Section: Resultsmentioning

confidence: 96%

A serine protease activity in C3H/10T1/2 cells that is inhibited by anticarcinogenic protease inhibitors.

Billings¹,

Carew²,

Keller-McGandy³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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“…Fig. 4A) and the fact that in solution, the trypsin inhibitor which is known to interact with trypsin through an arginyl residue (at position 63 [37]), also inhibits the kinase at low concentrations of its protein substrate (histone H2B).…”

Section: Theoretical and Practical Implications Of The Results And Thmentioning

confidence: 99%

Immobilized Soybean Trypsin Inhibitor in the Stabilization, Resolution and Purification of Adenosine‐3′: 5′‐monophosphate‐Dependent Protein Kinases

Alhanaty

Shaltiel

Bashan

et al. 1979

European Journal of Biochemistry

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The protein kinase dependent on adenosine 3': 5'-monophosphate (CAMP) in homogenates of rat intestinal mucosa was found to be remarkably unstable during its purification due (at least in part) to proteolysis. Since soybean trypsin inhibitor was found to protect the kinase from inactivation, an attempt was made to use this inhibitor, coupled to Sepharose, in order to extract and remove the proteolytic enzyme(s) responsible for the instability at an early stage of the purification. Indeed, this column excluded the undissociated form of CAMP-dependent protein kinase (R2C2) in a considerably more stable form, illustrating the use of immobilized proteolytic inhibitors for stabilizing proteins in crude extracts containing potent proteases. But unexpectedly the same column retarded a protein kinase which was not activated by CAMP. The latter enzyme was identified as the free catalytic subunit (C) of CAMP-dependent protein kinase since it was found to be inhibited by the Walsh-Krebs specific protein inhibitor. On the basis of these observations, a method was developed for the purification of C from rabbit muscle which is based on (a) passage of the crude extract on the column and (b) biospecific dissociation of R2C2 by CAMP and rechromatography of the extract on the same column. This procedure yields > 300-fold purification of C in the last step (with a recovery of 34 %) and a rapid resolution between R2C2 and C. The same column can also be used for the resolution of type I and type I1 CAMP-dependent protein kinases, and for a > 40-fold purification of the type I1 form of the enzyme, in one step. The theoretical and practical implications of these results with regard to the use and abuse of biorecognition in chromatography are discussed.Affinity chromatography was originally developed [ 1 -31 to replace the time-consuming, trial-and-error approach to the purification of proteins by a rational strategy based on retention of desired proteins through selective biorecognition by their physiological ligands. It was hoped that this new approach would provide rapid and effective (preferably one-step) purification of enzymes, for example, using carefully designed columns of immobilized ligands of these enzymes such as their substrates, inhibitors, cofactors, etc.

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“…These observations suggest that the effects on proteinase activity and class‐specificity of PIs are likely to play a role in the choice of diet a caterpillar will make. LBTI is a Bowman‐Birk PI with trypsin‐ and chymotrypsin‐specific PI‐domains (Birk, ), and TPCK is a chymotrypsin‐specific inhibitor. SKTI and TLCK, on the other hand, are strong inhibitors of trypsins, the predominant class of digestive proteinases in these insects (Bown, Wilkinson, & Gatehouse, ; Johnston, Lee, Gatehouse, & Anstee, ).…”

Section: Discussionmentioning

confidence: 99%

“…LBTI is a Bowman-Birk PI with trypsin-and chymotrypsin-specific PI-domains (Birk, 1976), and TPCK is a chymotrypsin-specific inhibitor. SKTI and TLCK, on the other hand, are strong inhibitors of trypsins, the predominant class of digestive proteinases in these insects (Bown, Wilkinson, & Gatehouse, 1997;Johnston, Lee, Gatehouse, & Anstee, 1991).…”

Section: Discussionmentioning

confidence: 99%

Effects of class‐specific, synthetic, and natural proteinase inhibitors on life‐history traits of the cotton bollworm Helicoverpa armigera

Kuwar

Pauchet

Heckel

2019

Arch Insect Biochem Physiol

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Herbivorous insects have more difficulty obtaining proteins from their food than do predators and parasites. The scarcity of proteins in their diet requires herbivores to feed voraciously, thus heavily damaging their host plants. Plants respond to herbivory by producing defense compounds, which reduce insect growth, retard development, and increase mortality. Herbivores use both pre‐ and postdigestive response mechanisms to detect and avoid plant defense compounds. Proteinase inhibitors (PIs) are one example of plant compounds produced as a direct defense against herbivory. Many insects can adapt to PIs when these are incorporated into artificial diets. However, little is known about the effect of PIs on diet choice and feeding behavior. We monitored the diet choice, life‐history traits, and gut proteinase activity of Helicoverpa armigera larvae using diets supplemented with synthetic and natural PIs. In choice experiments, both neonates and fourth‐instar larvae preferred the control diet over PI‐supplemented diets, to varying degrees. Larvae that fed on PI‐supplemented diets weighed less than those that fed on the control diet and produced smaller pupae. Trypsin‐specific PIs had a stronger effect on mean larval weight than did other PIs. A reduction of trypsin activity but not of chymotrypsin activity was observed in larvae fed on PI‐supplemented diets. Therefore, behavioral avoidance of feeding on plant parts high in PIs could be an adaptation to minimize the impact of this plant's defensive strategy.

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[59] Lima bean trypsin inhibitors

Cited by 15 publications

References 7 publications

A serine protease activity in C3H/10T1/2 cells that is inhibited by anticarcinogenic protease inhibitors.

A serine protease activity in C3H/10T1/2 cells that is inhibited by anticarcinogenic protease inhibitors.

Immobilized Soybean Trypsin Inhibitor in the Stabilization, Resolution and Purification of Adenosine‐3′: 5′‐monophosphate‐Dependent Protein Kinases

Effects of class‐specific, synthetic, and natural proteinase inhibitors on life‐history traits of the cotton bollworm Helicoverpa armigera

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