scholarly journals Changes in Proteolytic Activity and Cysteine Proteinase Gene Expression during the Senescence of etr1-1 Transgenic Petunias

HortScience ◽  
2005 ◽  
Vol 40 (4) ◽  
pp. 1105B-1105
Author(s):  
Michelle Jones ◽  
Gunching Chaffin ◽  
David Clark
Keyword(s):  
Proteolytic Activity ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Transcript Abundance ◽  
Flower Senescence ◽  
Cysteine Proteinases ◽  
University Of Florida ◽  
Nitrogen Levels ◽  
Protein Levels ◽  
The University

Corolla senescence in petunias was accompanied by a decrease in total proteins and a corresponding increase in proteolytic activity. Transgenic petunias that contain the mutated ethylene receptor (35S:etr1-1) have reduced sensitivity to ethylene and delayed flower senescence. Declines in total protein levels and increases in proteolytic activity were also delayed in etr1-1 flowers and corresponded with corolla wilting. Experiments using class-specific proteinase inhibitors indicated that proteolytic activity in petunia corollas was largely due to cysteine proteinases. Total nitrogen levels within the corollas of both wild type and etr1-1 flowers also decreased during senescence. Nine cDNAs encoding putative cysteine proteinases (CPs) were identified from a petunia EST database developed at the University of Florida. Six of these cysteine proteinases showed increased transcript abundance during corolla senescence (senescence-associated CPs) while three decreased in abundance. Of the six senescence-associated cysteine proteinases, only five showed delayed up regulation in etr1-1 flowers that corresponded with corolla wilting. The role of ethylene in the regulation of protein degradation during flower senescence will be discussed.

scholarly journals Cystatins — Inhibitors of Cysteine Proteinases

1992 ◽  
Vol 3 (4) ◽  
pp. 307-332 ◽  
Author(s):  
Libuse A. Bobek ◽  
Michael J. Levine
Keyword(s):  
Common Ancestor ◽  
Molecular Level ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Diverse Group ◽  
Cysteine Proteinases ◽  
Future Directions ◽  
Cysteine Proteinase Inhibitors ◽  
Physicochemical And Functional Properties

The cystatin superfamily of proteins, derived from a common ancestor, is comprised of a diverse group of potent cysteine proteinase inhibitors and antibacterial/viral agents grouped into several families. This review concentrates on family 2 cystatins, namely, the human salivary cystatins and cystatin C. Emphasis is given to their physicochemical and functional properties at both the protein and the molecular level. The role of cystatins in disease processes, including those in the oral cavity, is also discussed. Finally, future directions for cystatin research in oral biology are presented.

Involvement of cysteine proteinases in excystment of Paragonimus ohirai metacercariae induced by sodium cholate and A23187

2003 ◽  
Vol 77 (1) ◽  
pp. 21-26 ◽  
Author(s):  
T. Ikeda
Keyword(s):  
Proteinase Inhibitor ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Serine Proteinase ◽  
Sodium Cholate ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases ◽  
Serine Proteinase Inhibitor ◽  
Similar Activity

AbstractThe involvement of intrinsic proteinases in the excystment of Paragonimus ohirai metacercariae was studied in in vitro excystment induced by sodium (Na) cholate, a bile salt and A23187, a Ca2+ ionophore. The effects of various proteinase inhibitors on the in vitro excystment were examined and similar inhibitory profiles were obtained. Benzyloxycarbonyl-L-leucyl-L-leucinal (Z-Leu-Leu-H), a cysteine proteinase inhibitor and 4-(2-aminoethyl)-benzenesulfonyl fluoride (Pefabloc SC), a serine proteinase inhibitor completely inhibited excystment, while L-3-carboxy-2,3-trans-epoxypropionyl-leucylamido (4-guanidino)-butane (E-64), a cysteine proteinase inhibitor and leupeptin, a cysteine/serine proteinase inhibitor permitted partial excystment at a lower rate, but inhibited it from proceeding from the partial excystment stage. In secretions released from metacercariae during excystment, proteinase activities detected towards various fluorogenic peptidyl substrates were almost completely inhibited by Z-Leu-Leu-H and E-64, but not by Pefabloc SC. Sodium cholate induced a higher secretion of cysteine proteinases and a higher rate of excystment than A23187. Profiles of cysteine proteinase activities towards five peptidyl substrates detected were markedly different among the two secretions and the lysate of newly excysted juveniles. Newly excysted juveniles released cysteine proteinases with similar activity profiles and levels to metacercariae induced by Na cholate-incubation, whereas the release of cysteine proteinases was reduced compared with metacercariae induced by A23187-incubation. These results provide valuable information about the involvement of intrinsic proteinases in metacercarial excystment.

scholarly journals Identification of three stage-specific proteinases of Plasmodium falciparum.

1987 ◽  
Vol 166 (3) ◽  
pp. 816-821 ◽  
Author(s):  
P J Rosenthal ◽  
K Kim ◽  
J H McKerrow ◽  
J H Leech
Keyword(s):  
Plasmodium Falciparum ◽  
Life Cycle ◽  
Specific Activity ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Serine Proteinase ◽  
Cysteine Proteinases ◽  
Malaria Parasites ◽  
Neutral Ph ◽  
Cysteine Proteinase Inhibitors

We have identified and characterized three stage-specific proteinases of Plasmodium falciparum that are active at neutral pH. We analyzed ring-, trophozoite-, schizont-, and merozoite-stage parasites by gelatin substrate PAGE and characterized the identified proteinases with class-specific proteinase inhibitors. No proteinase activity was detected with rings. Trophozoites had a 28 kD proteinase that was inhibited by inhibitors of cysteine proteinases. Mature schizonts had a 35-40 kD proteinase that also was inhibited by cysteine proteinase inhibitors. Merozoite fractions had a 75 kD proteinase that was inhibited by serine proteinase inhibitors. The stage-specific activity of these proteinases and the correlation between the effects of proteinase inhibitors on the isolated enzymes with the effects of the inhibitors on whole parasites suggest potential critical functions for these proteinases in the life cycle of malaria parasites.

scholarly journals Cystatin-like cysteine proteinase inhibitors from human liver

1984 ◽  
Vol 218 (3) ◽  
pp. 939-946 ◽  
Author(s):  
G D J Green ◽  
A A Kembhavi ◽  
M E Davies ◽  
A J Barrett
Keyword(s):  
Human Liver ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Tight Binding ◽  
Cell Types ◽  
Dipeptidyl Peptidase ◽  
Tissue Homogenate ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases ◽  
Acetone Fractionation

Cysteine proteinase inhibitor (CPI) forms from human liver were purified from the tissue homogenate by alkaline denaturation of cysteine proteinases with which they are complexed, acetone fractionation, affinity chromatography on S-carboxymethyl-papain-Sepharose and chromatofocusing. The multiple forms of CPI were shown immunologically to be forms of two proteins, referred to as CPI-A (comprising the forms of relatively acidic pI) and CPI-B (comprising the more basic forms). CPI-A and CPI-B are similar in their Mr of about 12400, considerable stability to pH2, pH11 and 80 degrees C, and tight-binding inhibition of papain, several related cysteine proteinases and dipeptidyl peptidase I. Ki values were determined for papain, human cathepsins B, H and L, and dipeptidyl peptidase I. The affinity of CPI-A for cathepsin B was about 10-fold greater than that of CPI-B, whereas CBI-B showed about 100-fold stronger inhibition of dipeptidyl peptidase I. For all the cysteine proteinases the liver inhibitors were somewhat less tight binding than cystatin. The resemblance of both CPI-A and CPI-B in several respects to egg-white cystatin is discussed. CPI-A seems to correspond to the epithelial inhibitor described previously, and CPI-B to the inhibitor from other cell types [Järvinen & Rinne (1982) Biochim. Biophys. Acta 708, 210-217].

Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages

2004 ◽  
Vol 385 (6) ◽  
pp. 511-516 ◽  
Author(s):  
F. Lecaille ◽  
D. Muno ◽  
E. Kominami ◽  
K. Ishidoh
Keyword(s):  
Cathepsin B ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Vacuolar Atpase ◽  
Cysteine Proteinases ◽  
Bafilomycin A1 ◽  
Atpase Inhibitor ◽  
Peptide Bonds ◽  
Mature Form

Abstract The mammalian legumain is a recently identified lysosomal cysteine proteinase belonging to the clan CD and homologous to plant legumain. This enzyme has the characteristic of specifically hydrolyzing peptide bonds after asparagine residues. As in the case of papain-type cysteine proteinases, legumain is synthesized as an inactive zymogen, and processed into a mature form localized in lysosomes. However, the mechanism of its activation remains unclear. In this study, we analyze which types of proteinases may participate in the processing of legumain in rat primary cultured macrophages using various proteinase inhibitors after 24 h treatment with Bafilomycin A1, a vacuolar ATPase inhibitor. The processing of legumain in macrophages was accomplished by papain-type cysteine proteinases other than cathepsin B.

Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro

2002 ◽  
Vol 383 (5) ◽  
pp. 839-842 ◽  
Author(s):  
Natasa Sever ◽  
Metka Filipic ◽  
Joze Brzin ◽  
Tamara T. Lah
Keyword(s):  
Cell Invasion ◽  
Cathepsin B ◽  
Proteinase Inhibitor ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Cathepsin L ◽  
Cysteine Proteinase Inhibitor ◽  
Cysteine Proteinases ◽  
Cysteine Proteinase Inhibitors

Abstract Various types of proteinases are implicated in the malignant progression of human and animal tumors. Proteinase inhibitors may therefore be useful as therapeutic agents in antiinvasive and antimetastatic treatment. The aims of this study were (1) to estimate the relative importance of proteinases in B16 cell invasion in vitro using synthetic, classspecific proteinase inhibitors and (2) to assess the inhibitory effect of some naturally occurring cysteine proteinase inhibitors. Serine proteinase inhibitor reduced invasiveness by up to 24%, whereas inhibition of aspartic proteinases reduced invasion by 11%. Synthetic inhibitors of cysteine proteinases markedly impaired invasion: cathepsin B inhibitors, particularly Ca 074Me, inhibited invasion from 20 40%, whereas cathepsin L inhibitor Clik 148 reduced invasion by 11%. The potato cysteine proteinase inhibitor PCPI 8.7 inhibited invasion by 21%, whereas another potato inhibitor, PCPI 6.6, and the mushroom cysteine proteinase inhibitor clitocypin had no effects. As the inhibitors that inhibited cathepsin B were in general more efficient at impairing the invasiveness, we conclude that of the two cysteine proteinases, cathepsin B plays a more important role than cathepsin L in murine melanoma cell invasion.

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