PubMed Health⌕ Search

Biomedical subjects

J Malmquist

Publications and source records attributed to J Malmquist.

At least 55 records · Page 3Linked to original sources
PubMed1979

Turnover of human lactoferrin in the rabbit.

Lactoferrin turnover was studied in the rabbit with 125I- and 131I-labelled human lactoferrin. Plasma lactoferrin activity showed a rapid decrease during the first 24 h, followed by a 'final slope' with a T1/2 of about 25 h. Turnover studies after transfer of plasma from one rabbit (A) 3 h after injection to another rabbit (B), showed a recovery of 100% compared to 30% in A rabbits but otherwise a similar disappearance curve. The rapid turnover was confirmed in whole body studies. Concomitantly with the initial dissapearance from the plasma, there was a marked accumulation of proteinbound activity only in the liver in both A and B rabbits. From these results, the rate of synthesis in normal man can be estimated at around 25 mg per d. The disappearance pattern and hepatic uptake are discussed in relation to knowledge about lactoferrin receptors in macrophages, asialo elimination, and fucose group recognition. Concerning the significance of lactoferrin turnover for iron metabolism it is concluded that the plasma turnover results are insufficient to explain the disturbance in iron kinetics seen in the anaemia of chronic disorders; however, it is likely that lactoferrin plays a role in iron metabolism within the extravascular space.

Animals↗
PubMed1978

Adenylate cyclase activity in human liver membranes and its inhibition by adenosine and adenine nucleotides.

The production of adenosine 3',5'-monophosphate (cyclic AMP) in a membrane preparation from human liver homogenate has been studied. Cyclic AMP production was enhanced by glucagon, guanylyl 5'-imidodiphosphate (GMP-PNP), or fluoride, or combinations of these. Adenosine, adenosine monophosphate (AMP) and adenosine diphosphate (ADP) at a concentration of 10(-3) mol/l antagonized the effects of all stimulants. These data suggest that inhibitory effects are exercised at the catalytic moiety of the adenylate cyclase system, or at the transducer function between hormone receptor and catalytic unit. In contrast, adenosine at a concentration of 10(-5) mol/l antagonized glucagon- but not fluoride-stimulated adenylate cyclase activity.

Adenosine↗
PubMed1977

Lactoferrin and lysozyme in arthritic exudates.

Lactoferrin (LF) has been assayed by radioimmunoassay in plasma and arthritic exudates and compared with lysozyme (LZ) levels and leukocyte counts. The mean LF concentration in 38 rheumatoid arthritis (RA) exudates was 9.1 mg/l (range 0.02-39.2). In 30 non-RA exudates LF was 3.3 mg/l (range 0.01-14.6). The corresponding LZ levels were 7.4 mg/l (range 2.5-18.5) in RA and 4.7 (range 1.0-12.5) in non-RA fluids. Exudate/plasma ratios were much higher for LF than for LZ and higher in RA than in non-RA exudates, whereas leukocyte counts did not differ. The LF/leukocyte count ratio was significantly higher in RA than in the non-RA group. The data suggest a more prominent release of neutrophilic granulocyte components in RA than in non-RA arthritis.

Animals↗
PubMed1976

Neutrophilic granulocytes in acute bacterial infection. Sequential studies on lysozyme, myeloperoxidase and lactoferrin.

The changes in intraneutrophilic and plasma concentrations of the three antibacterial proteins lysozyme, lactoferrin, and myeloperoxidase were studied sequentially during acute bacterial infection in nine patients. Intraneutrophilic concentrations of the three proteins were decreased by more than 50% during the 1st week of infection, followed by a slow increase over the following 2 weeks. Nadir values coincided with maximal toxic granulation of the neutrophils. The data suggest that neutrophilic granulocytes are deficient during early bacterial infection, possibly because of deficient synthesis of antibacterial proteins in the bone marrow, and that neutrophil toxic granulation is the visual counterpart of this defect. The plasma concentrations of the three proteins showed considerable differences: whereas plasma lysozyme did not show any sequential changes, plasma myeloperoxidase was high at the start of infection and quickly decreased towards normal values, and plasma lactoferrin, high in the first samples, showed a secondary peak 1 week after onset of disease, before normalization was seen. These differences may result from differences in the signals are specific for the individual antibacterial protein and not for the different types of neutrophil granules.

Adult↗
PubMed1975

Plasma myeloperoxidase and lactoferrin measured by radioimmunoassay: relations to neutrophil kinetics.

In 31 patients, covering a wide range of blood neutrophil counts and turnover rates, the plasma concentrations of myeloperoxidase and lactoferrin have been measured with radioimmunoassays and compared to neutrophil kinetic parameters, measured with DF32P-labeled neutrophils. It was found that the plasma concentrations of both proteins correlated significantly with the total number of neutrophils in the blood (TBGP=total blood granulocyte pool) as well as with the neutrophil turnover rate (GTR=granulocyte turnover rate), which is evidence that neutrophilic granulocytes are the main suppliers of myeloperoxidase and lactoferrin to the plasma. In contrast to the previously demonstrated better relationship between the GTR and plasma lysozyme, a protein also originating in neutrophil granules, both myeloperoxidase and lactoferrin correlated better with the TBGP. These differences may reflect differences in the mode of release of intragranular proteins from neutrophils to the plasma. The correlation of the plasma lactoferrin concentration with the TBGP was so good as to suggest its use in the clinical assessment of the TBGP.

Arthritis, Rheumatoid↗