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)

Carboxypeptidase M, a widely distributed membrane-bound carboxypeptidase that can regulate peptide hormone activity, was purified to homogeneity from human placenta (Skidgel, R. A., Davis, R. M., and Tan, F. (1989) J. Biol. Chem. 264, 2236-2241). The NH2-terminal 31 amino acids were sequenced, and two complementary oligonucleotide probes were synthesized and used to isolate a carboxypeptidase M clone from a human placental cDNA library. Sequencing of the cDNA insert (2009 base pairs) revealed an open reading frame of 1317 base pairs coding for a protein of 439 residues. The NH2-terminal protein sequence matched the deduced amino acid sequence starting with residue 14. Hydropathic analysis revealed hydrophobic regions at the NH2 and COOH termini. The NH2-terminal 13 amino acids probably represent part of the signal peptide, and the COOH-terminal hydrophobic region may act either as a transmembrane anchor or as a signal for attachment to a phosphatidylinositol glycan moiety. The carboxypeptidase M sequence contains six potential Asn-linked glycosylation sites, consistent with its glycoprotein nature. The sequence of carboxypeptidase M was 41% identical with that of the active subunit of human plasma carboxypeptidase N, 41% identical with bovine carboxypeptidase H (carboxypeptidase E, enkephalin convertase), and 15% with either bovine pancreatic carboxypeptidase A or B. Many of the active site residues identified in carboxypeptidases A and B, including all of the zinc-binding residues (2 histidines and a glutamic acid), are conserved in carboxypeptidase M. These data indicate that all of the metallocarboxypeptidases are related, but the nondigestive carboxypeptidases with more specialized functions, present in cell membranes, blood plasma, or secretory granules (i.e., carboxypeptidase M, carboxypeptidase N and carboxypeptidase H), are more closely related to each other (41-49% identity) than they are to carboxypeptidase A or B (15-20% identity).
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PMID:Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. 275 7

Effect of oxatomide on contraction of canine bronchial smooth muscle caused by administration of histamine and by challenge of ascaris-antigen were investigated and compared against the effects of histamine H1-receptor antagonist (CPM) and inhibitor of histamine release from mast cells (DSCG). Oxatomide in concentrations of 0.05 microgram/ml to 2.0 microgram/ml inhibited, dose-responsively, contraction of bronchial smooth muscle strip by administration of histamine (10 micrograms/ml). When this concentration was less than 0.3 microgram/ml, CPM inhibited the contraction significantly stronger than oxatomide. However, in concentration over 0.5 microgram/ml, no difference in inhibitory effect could be demonstrated. On the other hand, DSCG could not inhibit the contraction. Oxatomide in concentrations of 0.05 microgram/ml to 1.0 micrograms/ml inhibited, dose-responsively, contraction of the muscle strip sensitized spontaneously by ascaris antigen challenges. There was no difference in inhibitory effect between oxatomide and DSCG at the same level of concentration. Oxatomide (0.5 microgram/ml) and CPM (0.5 microgram/ml) both inhibited completely the constriction response of bronchus caused by histamine stimulation (10 micrograms/ml). Although constriction response by ascaris antigen challenge was inhibited completely by oxatomide (0.5 microgram/ml), it could not be inhibited completely by CPM (0.5 microgram/ml). Oxatomide inhibited even the residual constriction response which could not accomplished by CPM. These results suggest that oxatomide might have not only an effect as a histamine H1-receptor antagonist and anti-histamine releasing agent from mast cell, but also anti-SRS-A.
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PMID:[Effect of 1-[3-[4-(diphenylmethyl)-1-priperazinyl]-propyl]-1,3-dihydro-2H-benzimidazol-2- one (oxatomide) on contraction of canine bronchial muscle]. 614 14