Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The role of serine endopeptidase in cucumber leaf senescence was studied by using the inhibitor of serine endopeptidase and plant growth regulators (6-BA and ABA) on darkness-induced cucumber leaves. The results showed that the senescence of cucumber leaves were delayed by AEBSF [4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride], an inhibitor of serine-type endopeptidase, or 6-BA treatment. The chlorophyll contents increased by AEBSF (Fig.3) and the protein degradation of leaves under AEBSF treatment declined more slowly than in the control or under ABA 50 micromol/L treatment (Fig.4), partly because the activities of serine endopeptidases became lower during senescence. However, the activities of endopeptidase in cucumber leaf were increased by ABA 50 micromol/L (Fig.2A), furthermore, the MDA content were also influenced by AEBSF and plant growth regulators (Fig.5). Native gradient PAGE showed that six bands of isoenzymes were detected in cucumber leaves and four bands of which were the type of serine-endopeptidase (Fig.1), and proved that the activities of serine-endopeptidase were inhibited by AEBSF, but enhanced by ABA (Fig.2B) in the leaves. It implies that serine endopeptidases might play an important role in cucumber leaf senescence.
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PMID:[The role of serine endopeptidase in cucumber leaf senescence]. 1707 85

Streptococcus (S.) phocae subsp. phocae causes bronchopneumonia and septicemia in a variety of marine mammals. Especially in harbor seals infected with phocine distemper virus it plays an important role as an opportunistic pathogen. This study was initiated by the detection of IgG cleavage products in Western blot analysis after incubation of bacterial supernatant with harbor seal serum. Hence, the objectives of this study were the identification and characterization of a secreted IgG cleaving protease in S. phocae subsp. phocae isolated from marine mammals. To further identify the responsible factor of IgG cleavage a protease inhibitor profile was generated. Inhibition of the IgG cleaving activity by iodoacetamide and Z-LVG-CHN2 indicated that a cysteine protease is involved. Moreover, an anti-IdeS antibody directed against the IgG endopeptidase IdeS of S. pyogenes showed cross reactivity with the putative IgG protease of S. phocae subsp. phocae. The IgG cleaving factor of S. phocae subsp. phocae was identified through an inverse PCR approach and designated IdeP (Immunoglobulin G degrading enzyme of S. phocae subsp. phocae) in analogy to the cysteine protease IdeS. Notably, recombinant (r) IdeP is a host and substrate specific protease as it cleaves IgG from grey and harbor seals but not IgG from harbor porpoises or non-marine mammals. The identification of IdeP represents the first description of a protein in S. phocae subsp. phocae involved in immune evasion. Furthermore, the fact that IdeP cleaves solely IgG of certain marine mammals reflects functional adaption of S. phocae subsp. phocae to grey and harbor seals as its main hosts.
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PMID:Identification of a novel host-specific IgG protease in Streptococcus phocae subsp. phocae. 2828 21