Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.5 (thrombin)
 33,306 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Removal of calcium by either citrate, oxalate, or ethylenediaminetetraacetate inhibited coagulation of blood at an early stage and prevented the release of beta-lysin from platelets. In contrast, heparin caused platelet agglutination and stimulated beta-lysin release in vitro and in vivo. This release was calcium dependent and may have been due to a calcium-dependent reaction in the blood coagulation sequence. Thrombin which by-passed the early calcium-dependent stages of coagulation directly stimulated the release of beta-lysin from platelets. However, thrombin alone or in combination with other plasma factors was not as effective in releasing beta-lysin as the regular coagulation process. Thrombin's platelet degranulating activity correlated with its beta-lysin releasing activity. In contrast to thrombin, staphylococcal coagulase, which also by-passed the calcium-dependent stages of coagulation, coagulated citrated blood without releasing beta-lysin. The release of beta-lysin has been observed previously in the absence of blood coagulation, but this is the first observation of coagulation without beta-lysin release. It is clear that beta-lysin is released from platelets during coagulation by the direct action of thrombin and that it may be released in an earlier calcium-dependent reaction.
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PMID:Release of beta-lysin from platelets by thrombin and by a factor produced in heparinized blood. 420 88

Fertilization is a precisely controlled process involving many gamete molecules in sperm binding to and penetration through the extracellular matrix of the egg. After sperm bind to the extracellular matrix (vitelline coat), they undergo the acrosome reaction which exposes and partially releases a lytic agent called "lysin" to digest the vitelline coat for the sperm penetration. The vitelline coat sperm lysin is generally a protease in deuterostomes. The molecular mechanism of the actual degradation of the vitelline coat, however, remains poorly understood. In order to understand the lysin system, we have been studying the fertilization mechanism in ascidians (Urochordata) because we can obtain large quantities of gametes which are readily fertilized in the laboratory. Whereas ascidians are hermaphrodites, which release sperm and eggs simultaneously, many ascidians, including Halocynthia roretzi, are strictly self-sterile. Therefore, after sperm recognize the vitelline coat as nonself, the sperm lysin system is thought to be activated. We revealed that two sperm trypsin-like proteases, acrosin and spermosin, the latter of which is a novel sperm protease with thrombin-like substrate specificity, are essential for fertilization in H. roretzi. These molecules contain motifs involved in binding to the vitelline coat. We found that the proteasome rather than trypsin-like proteases has a direct lytic activity toward the vitelline coat. The target for the ascidian lysin was found to be a 70-kDa vitelline coat component called HrVC70, which is made up of 12 EGF-like repeats. In addition to the proteasome system, the ubiquitination system toward the HrVC70 was found to be necessary for ascidian fertilization. In this review, I describe recent progress on the structures and roles in fertilization of the two trypsin-like proteases, acrosin and spermosin, and also on the novel extracellular ubiquitin-proteasome system, which plays an essential role in the degradation of the ascidian vitelline coat.
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PMID:Ascidian sperm lysin system. 1201 76