Disease relevance of proteinase

• A specific extracellular proteinase, degrading selectively the cecropin-based defence system of insects, is secreted into the larval body during parasitism of the greater wax moth by the Heterorhabditis bacteriophora/Photorhabdus luminescens complex and by phase 1 of P. luminescens [1].
• In this study, a 1713bp long cDNA encoding for a putative proteinase of O. volvulus has been isolated [2].
• Recombinant propeptides of HGCP-Iv, expressed in E. coli, presented high inhibitory activity in vitro towards its cognate enzyme and proteinase activity of Meloidogyne incognita females, suggesting its usefulness in inhibiting nematode CPs in biological systems [3].

High impact information on proteinase

• MMC contain and secrete a neutral proteinase, rat mast cell protease II (RMCP II); detection and assay of secreted RMCP II therefore provides a direct measurement of MMC activity [4].
• The amount of the Cu(2+)- Zn(2+) superoxide dismutase (CE23550) and an aspartyl proteinase (CE21681) was highest in the first larval stage (L1) and decreased during the ontogenesis from the first larval stage to the adult [5].
• Identification of stable plant cystatin/nematode proteinase complexes using mildly denaturing gelatin/polyacrylamide gel electrophoresis [6].
• Interestingly, the two plant cysteine proteinase inhibitors OCI and OCII showed different degrees of affinity for the major proteinase form, Mhp1 [6].
• A pepstatin A-agarose column was used in an attempt to purify a previously described antibody-degrading aspartyl proteinase from excretory-secretory material from the L4 and the adult stages of the bovine abomasal nematode Ostertagia ostertagi [7].

Biological context of proteinase

• As with these, the predicted amino-acid sequence comprises a head-to-tail array of similar polypeptides with regularly spaced consensus proteinase cleavage sites [8].
• We produced a recombinant protein from a cDNA library from muscle larvae of Trichinella spiralis which had proteinase inhibitory activity [9].
• Hence, partial acid hydrolysis and proteinase K digestion was performed followed by RP-HPLC [10].

Anatomical context of proteinase

• The type of medium used to isolate the mitochondria is crucial in such studies; an ionic medium with Nagarse proteinase was optimal for fish muscle mitochondria [11].

Associations of proteinase with chemical compounds

• The information gained from these studies indicates that serine proteinases are an important group of enzymes in H. glycines and further characterization will aid the development of a proteinase inhibitor-based approach for transgenic plant resistance to plant parasitic nematodes [12].
• Binding of the monoclonal antibodies to the third-stage larvae was abrogated by treatment of the worms with trypsin and proteinase K, but was unaffected by treatment with periodate or the detergents sodium deoxycholate and SDS [13].
• Egg disruption procedures tested included probe sonication, bath sonication, bead beating, boiling, microwaving, proteinase K/SDS digestion, freezing, and various combinations of the above with the incorporation of sodium dodecyl sulfate [14].
• The proteinase K digested peaks were subjected to Edman degradation (first peak, ser-pro-ser/gly-ser; second peak, tyr/arg-leu), mass spectrometry (no result) and MALDI analysis (no result) [10].
• Worms from lambs given molybdenum contained less proteinase enzyme activity and secreted less proteinases in culture irrespective of the sex of the host [15].

Other interactions of proteinase

• The proteinase showed a pH optimum at 8 and activity against azocoll and keratin [16].
• The purified proteinase, from cultures of L4, has a molecular weight of approximately 46 kDa, functions as an endopeptidase, and digests several native proteins of host origin including fibrinogen and fibronectin [17].
• Chemical degradation of one particular epitope recognized by monoclonal antibody PP1/117, and designated ep117, occurred after treatment with NaOH, periodate or Proteinase K, suggesting that an O-linked glycoprotein may be involved [18].

Analytical, diagnostic and therapeutic context of proteinase

• The relatively low concentrations of SMCP in blood and lymph reflect the presence of proteinase inhibitor(s) which interfered with the ELISA [19].
• The rational development of this strategy involves characterization of nematode proteinase genes and optimization of inhibitors by protein engineering [20].
• A variety of genes, besides (Bt) toxins that are now available for genetic engineering for pest resistance are genes for vegetative insecticidal proteins, proteinase inhibitors, alpha-amylase inhibitors, and plant lectins [21].
• Southern blot analysis suggests that the cathepsin S-like enzyme, HGCP-II, is encoded by a single-copy gene in contrast to the cathepsin L-like proteinase, HGCP-I which may have 2 homologues [22].
• Molecular cloning of a novel multidomain Kunitz-type proteinase inhibitor from the hookworm Ancylostoma caninum [23].

References