Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have cloned a novel murine cDNA encoding a multidomain serine protease, termed neurotrypsin, which exhibits an unprecedented domain composition. The deduced amino acid sequence defines a mosaic protein of 761 amino acids consisting of a kringle domain, followed by three scavenger receptor cysteine-rich repeats, and a serine protease domain. Based on comparisons of the primary structure, the protease domain belongs to the subfamily of trypsin-like serine proteases. In situ hybridization revealed that the expression of neurotrypsin in the adult murine nervous system is confined to distinct subsets of neurons. The most prominent expression was found in the cerebral cortex, the hippocampus, and the amygdala. Le., structures engaged in the processing and storage of learned behaviors and memories. Together with the recently obtained evidence that extracellular serine proteases play a role in neural plasticity, this expression pattern suggests that the extracellular proteolytic action of neurotrypsin subserves structural reorganizations associated with learning and memory operations.
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PMID:Neurotrypsin, a novel multidomain serine protease expressed in the nervous system. 924 3

We present the cloning and structural analysis of a novel member of the large family of trypsin-related serine proteases. Northern blot analysis shows that this protease, in adult tissues, is expressed almost exclusively in the human testis. In addition, a larger transcript was detected in relatively high abundance in several embryonic tissues, indicating different functions during embryonic and adult life. Sera raised against this protease was used to locate the expression in adult tissues to the testosterone producing cells of the testis, the interstitial Leydig cells. We therefore propose the name leydin for this novel protease. Leydin is clearly distinct from acrosin, the other testis-specific serine protease which is expressed by the spermatocytes. Leydin is probably a two-chain protease such as acrosin, prostasin, and coagulation factor XI. The heavy chain consists of 246 amino acids, corresponding to a molecular mass of 27384 Da and a net charge of +10.76. The size of the light chain is between 9 and 18 amino acids depending on the site of proteolytic cleavage, which remains to be determined. The amino-acid residues surrounding the active site indicate a trypsin-like cleavage specificity. The presence of two dibasic sequences Arg-Arg and Lys-Arg at the N-terminus of the heavy chain indicate that one or more subtilisin-like endopeptidases are responsible for the processing of leydin. However, leydin may also be activated by a trypsin-like enzyme, possibly by auto catalysis.
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PMID:Cloning and structural analysis of leydin, a novel human serine protease expressed by the Leydig cells of the testis. 1010 56

Several serine proteases including thrombin, tissue-type plasminogen activator and urokinase-type plasminogen activator have been well characterized in the brain. In this article, we review the brain-related trypsin and trypsin-like serine proteases. Accumulating evidence demonstrates that trypsin and trypsin-like serine proteases play very important roles in neural development, plasticity, neurodegeneration and neuroregeneration in the brain. Neuropsin is able to hydrolyze the extracellular matrix components by its active site serine, and regulates learning and memory in normal brain. The mutant neurotrypsin contributes to mental retardation in children. Neurosin seems to be involved in the pathogenesis of neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease or multiple sclerosis. Although mesotrypsin/trypsin IV is also implicated in neurodegeneration, its functional significance still remains largely unknown. Particularly, mesotrypsin/trypsin IV, P22 and neurosin exert their physiological and pathological functions through activation of certain protease-activated receptors (PARs). In the brain, the presence of serpins controls the activity of serine proteases. Therefore, understanding the interaction among brain trypsin, serpins and PARs will provide invaluable tools for regulating normal brain functions and for the clinical treatment of neural disorders.
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PMID:Trypsin and trypsin-like proteases in the brain: proteolysis and cellular functions. 1796 32