Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011570 (depression)
 172,036 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fifteen examples of red cells are described which showed discrepant reactivity on routine grouping with two monoclonal anti-D typing reagents, HAM-A being negative and MAD-2 strongly positive. The reaction profile of these cells with a number of monoclonal anti-D characterised the samples into two new variant groups, DHMi and DHMii. DHMi was characterised by a negative reaction with BRAD-8 and DHMii by a negative reaction with BRAD-5. DHMi cells were found to have a papain-sensitive site, identified by Mab 21 G6, which was not detectable in DHMii. The presence of allo-anti-D in one case of DHMi suggests a partial D in these individuals. The positive reaction of HAM-A with sialidase- and endo-F-treated DHMii cells suggests that sialic acid and/or N-glycans could possibly be involved in blocking the reaction with untreated cells. All samples typed as C-E+. One was e negative while the rest had variable depression of the e and f antigens. Marginal depression of E was seen with those DHMi cells tested, but not with DHMii cells. Data from family studies suggest that the variant D in both DHMi and DHMii is inherited as a cDE gene complex and is controlled by the RH locus.
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PMID:Identification of two new D variants, DHMi and DHMii using monoclonal anti-D. 857 37

1. Following intravenous administration of testes hyaluronidase in rabbits and dogs, there is a decrease in the level of the non-specific inhibitor of hyaluronidase in serum. 2. If a large amount of hyaluronidase is injected, the inhibitor level is reduced to zero and hyaluronidase may be present in serum for some time after the injection. The hyaluronidase activity of such samples of serum increases when the serum is incubated with papain. 3. Hyaluronidase activity is found in the livers of the injected animals in large amounts and this activity is increased considerably when the homogenate of this tissue is incubated with papain. 4. Intravenous administration of several proteases or venom produces a decrease in the serum inhibitor level. Intravenous administration of streptokinase produces such a decrease in rabbits but not in dogs. 5. There is a correlation between the depletion of the inhibitor from the serum and the occurrence of a slow, persistent depression of blood pressure upon administration of proteolytic enzymes.
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PMID:The interactions of the non-specific inhibitor of hyaluronidase with hyaluronidase and proteolytic enzymes in vivo. 1327 19

In the senescing endosperm of germinating castor bean (Ricinus communis) a special organelle (the ricinosome) releases a papain-type cysteine endopeptidase (CysEP) during the final stages of cellular disintegration. Protein cleavage sites for the Ricinus CysEP were determined with fluorogenic peptides (Abz-Xaa-Arg-/-Gln-Gln-Tyr(NO2)-Asp). The highest kcat/Km values were obtained with neutral amino acid residues with large aliphatic and non-polar (Leu, Val, Ile, Met) or aromatic (Phe, Tyr, Trp) side-chains. A second series (Abz-Leu-Xaa-/Gln-Pro-Tyr(NO2)-Asp) was evaluated. Based on these results, the covalent binding inhibitor H-D-Val-Leu-Lys-chloromethylketone (CMK) was chosen as substrate analogue for replacement in the catalytic site. Unusually, CysEP cleaved beta-casein N and C-terminal to the amino acid proline. CysEP was crystallized, its structure was solved by molecular replacement at 2.0 A resolution and refined to a R-factor of 18.1% (Rfree=22.6%). The polypeptide chain folds as in papain into two domains divided by the active site cleft, an elongated surface depression harboring the active site. The non-primed specificity subsites of the proteinase are clearly defined by the H-D-Val-Leu-Lys-CMK-inhibitor covalently bound to the active site. The absence of the occluding loop, which blocks the active site of exopeptidases at the C-terminal side of the scissile bond, identifies CysEP as an endopeptidase. The more open pocket of the Ricinus CysEP correlates with the extended variety of substrate amino acid residues accommodated by this enzyme, including even proline at the P1 and P1' positions. This may allow the enzyme to attack a greater variety of proteins during programmed cell death.
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PMID:The 2.0 A crystal structure and substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm. 1503 72

Blood samples from a 10-month-old male infant requiring transfusion were found to contain an allomtibody reacting at 37 degrees C in saline, by indirect antiglobulin test (IAT), and with a manual polybrene technique. Preliminary results suggested anti-D and another weaker reacting antibody, but the patient had been previously transfused with only D- blood. His serum reacted more weakly by IAT against red cells treated with 0.2M dithiothreitol (DTT), and one D+, LW(a-) sample was nonreactive. The patient's red blood cells (RBCs) typed as B, D-, LW(a-), K-, Fy(a-). Due to the age and clinical status of the child, 51Cr survival studies were not performed. One pediatric unit of D-, K-, Fy(a-) blood was transfused uneventfully; the expected increment of hemoglobin was achieved. Repeat testing 3 months later showed a weakly positive DAT, the patient's RBCs typed as LW(a+), and anti-LWa was detected only by a two-stage papain technique. These results suggest that the patient had a transient depression of LWa with a concurrent anti-LWa.
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PMID:An example of anti-LWa in a 10-month-old infant. 1594 14

The sera genes of the malaria-causing parasite Plasmodium encode a family of unique proteins that are maximally expressed at the time of egress of parasites from infected red blood cells. These multi-domain proteins are unique, containing a central papain-like cysteine-protease fragment enclosed between the disulfide-linked N- and C-terminal domains. However, the central fragment of several members of this family, including serine repeat antigen 5 (SERA5), contains a serine (S596) in place of the active-site cysteine. Here we report the crystal structure of the central protease-like domain of Plasmodium falciparum SERA5, revealing a number of anomalies in addition to the putative nucleophilic serine: (1) the structure of the putative active site is not conducive to binding substrate in the canonical cysteine-protease manner; (2) the side chain of D594 restricts access of substrate to the putative active site; and (3) the S(2) specificity pocket is occupied by the side chain of Y735, reducing this site to a small depression on the protein surface. Attempts to determine the structure in complex with known inhibitors were not successful. Thus, despite having revealed its structure, the function of the catalytic domain of SERA5 remains an enigma.
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PMID:Structural insights into the protease-like antigen Plasmodium falciparum SERA5 and its noncanonical active-site serine. 1959 43


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