Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.2.2.7 (heparinase)
 1,270 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mast cell proteases in the tongue and jejunum of Mongolian gerbils (Meriones unguiculatus) were examined by enzyme-histochemical methods. Both trypsin-like (tryptase) and chymotrypsin-like (chymase) protease activities were demonstrated in mast cells in the tongue of fresh cryosections. When frozen sections of the tongue were post-fixed in various fixatives, those fixed in Carnoy's fluid showed strongest enzyme activities. Tryptase and chymase activities in paraffin sections of both tissues were well preserved when tissues were fixed in Carnoy's fluid at 4 degrees C for 15 min. However, enzyme activities in both tissues, especially in the tongue, were drastically reduced by longer fixation time and higher temperature. When Carnoy-fixed (4 degrees C for 15 min) paraffin sections were treated with heparinase I or chondroitinase ABC before enzyme-histochemical stainings for proteases, tryptase activities were lost entirely in the tongue and mostly in the jejunum by heparinase I digestion, and slightly in both organs by chondroitinase ABC digestion. In contrast, chymase activities at both sites were not influenced by these pretreatments. These results show that although mast cells in the tongue as well as in the jejunum of Mongolian gerbils contain both tryptase and chymase activities, their stability to fixations is variable among organs so that tissue fixation conditions are crucial for the preservation. At least some part of the stability of mast cell proteases is dependent on the proteoglycans present in mast cell granules.
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PMID:Reappraisal of the expression of mast cell proteases of Mongolian gerbils (Meriones unguiculatus). 974 May 13

Snake envenomation employs three well integrated strategies: prey immobilization via hypotension, prey immobilization via paralysis, and prey digestion. Purines (adenosine, guanosine and inosine) evidently play a central role in the envenomation strategies of most advanced snakes. Purines constitute the perfect multifunctional toxins, participating simultaneously in all three envenomation strategies. Because they are endogenous regulatory compounds in all vertebrates, it is impossible for any prey organism to develop resistance to them. Purine generation from endogenous precursors in the prey explains the presence of many hitherto unexplained enzyme activities in snake venoms: 5'-nucleotidase, endonucleases (including ribonuclease), phosphodiesterase, ATPase, ADPase, phosphomonoesterase, and NADase. Phospholipases A(2), cytotoxins, myotoxins, and heparinase also participate in purine liberation, in addition to their better known functions. Adenosine contributes to prey immobilization by activation of neuronal adenosine A(1) receptors, suppressing acetylcholine release from motor neurons and excitatory neurotransmitters from central sites. It also exacerbates venom-induced hypotension by activating A(2) receptors in the vasculature. Adenosine and inosine both activate mast cell A(3) receptors, liberating vasoactive substances and increasing vascular permeability. Guanosine probably contributes to hypotension, by augmenting vascular endothelial cGMP levels via an unknown mechanism. Novel functions are suggested for toxins that act upon blood coagulation factors, including nitric oxide production, using the prey's carboxypeptidases. Leucine aminopeptidase may link venom hemorrhagic metalloproteases and endogenous chymotrypsin-like proteases with venom L-amino acid oxidase (LAO), accelerating the latter. The primary function of LAO is probably to promote prey hypotension by activating soluble guanylate cyclase in the presence of superoxide dismutase. LAO's apoptotic activity, too slow to be relevant to prey capture, is undoubtedly secondary and probably serves principally a digestive function. It is concluded that the principal function of L-type Ca(2+) channel antagonists and muscarinic toxins, in Dendroaspis venoms, and acetylcholinesterase in other elapid venoms, is to promote hypotension. Venom dipeptidyl peptidase IV-like enzymes probably also contribute to hypotension by destroying vasoconstrictive peptides such as Peptide YY, neuropeptide Y and substance P. Purines apparently bind to other toxins which then serve as molecular chaperones to deposit the bound purines at specific subsets of purine receptors. The assignment of pharmacological activities such as transient neurotransmitter suppression, histamine release and antinociception, to a variety of proteinaceous toxins, is probably erroneous. Such effects are probably due instead to purines bound to these toxins, and/or to free venom purines.
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PMID:Ophidian envenomation strategies and the role of purines. 1173 31