Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The relationship between inter-alpha inhibitor (I alpha I) and urinary proteinase inhibitor (UPI) was examined by comparing purified UPI with a proteolytic fragment of I alpha I (I'), and by demonstrating that inflammatory cells produce similar fragments under physiologic conditions. Purified I', derived by chymotrypsin digestion of I alpha I, was similar to UPI in apparent molecular weight (68,000-69,000), amino acid composition, immunoreactivity, and inhibitory activity against trypsin, chymotrypsin, and neutrophil elastase. The production of similar inhibitory fragments by murine peritoneal macrophages, human neutrophils, and a murine mast cell line was quantified. Neutrophils were most efficient at proteolyzing I alpha I. Comparison of the pattern of I alpha I degradation by neutrophil preparations with that by pure enzymes, suggested that both elastase and cathepsin G mediate neutrophil proteolysis of I alpha I. These proteinases may thus be responsible for inflammation-related increases in UPI-like inhibitor levels in vivo.
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PMID:Inflammatory cells degrade inter-alpha inhibitor to liberate urinary proteinase inhibitors. 246 21

Complementary DNAs (cDNAs) encoding alpha 1-microglobulin (alpha 1mG)/bikunin, also known as inter-alpha-inhibitor (I alpha I) light chain, were cloned from liver extracts of the Mongolian gerbil, Meriones unguiculatus, and the Syrian golden hamster, Mesocricetus auratus, by reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends methods. From the deduced amino-acid sequences of alpha 1mG/bikunin of gerbil and hamster, the basic molecular structure of the proteins seemed to be well-conserved. However, near the proposed sequence of proteinase inhibitory sites of two Kunitz domains in the bikunin part, variable regions composed of three amino acids each were observed between species, including rodents. Since the second half of bikunin is genetically identical with the mast cell proteinase inhibitor, trypstatin, the bikunin of each animal may have distinct inhibitory activity against mast cell proteinases.
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PMID:Sequencing of cDNAs encoding alpha 1-microglobulin/bikunin of Mongolian gerbil and Syrian golden hamster in comparison with man and other species. 752 51