THE f* MESON PRODUCED IN K$sup -$p INTERACTION 4.6 AND 5.0 Bev/c

Barnes, V. E.; Dornan, P. J.; Guidoni, P.

doi:10.2172/4519462

Cited by 8 publications

(12 citation statements)

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“…The absence or extremely low levels of association complexes or what others have termed triglyceride-rich lipoproteins (37) correlates with the reduced levels of plasma triacylglycerol and VLDL (39,50). The low amounts of association complexes strongly suggest that an insignificant amount, if any, of intact VLDL or other lipoproteins from the mother cross the placenta in agreement with other investigators (9,10,21,23,25,50). This conclusion is supported by evidence indicating that of the lipid moieties in maternal serum only free fatty acids (20) and unesterified cholesterol (lo, 28) are transferred across the placental membranes at term.…”

supporting

confidence: 91%

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Studies on the Apolipoproteins and Lipoproteins of Cord Serum

McConathy

Lake

1980

Pediatr Res

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SummaryStudies on the cord serum lipid transport system were initiated to determine whether there is a correlation between decreased cord serum lipid levels and the absence or diminished level of some or all of the human serum apolipoproteins. Immunologic studies indicated the presence of all the well-characterized apolipoproteins and provided evidence that these apolipoproteins occurred primarily as distinct lipoprotein species with a paucity of association complexes or what others have termed "triglyceride-rich" lipoproteins. Quantitation of the apolipoproteins present in cord serum by electroimmunoassay yielded the following mean levels: A-I = 730 mg/liter; A-11 = 410 &liter; apolipoprotein B = 280 mg/ liter; C-I = 59 mg/liter; C-I1 = 32 &liter; C-111 = 65 mg/liter; apolipoprotein D = 37 &liter; and apolipoprotein E = 85 mg/ liter. Levels of C-I, C-11, and apolipoprotein E approached adult levels (83 to 86% of the adult levels), whereas apolipoproteins B and D were most reduced when compared to the adult concentrations, 29 and 37%, respectively. The three other apolipoproteins were present at approximately one-half the levels found in adults. SpeculationThe immunochemical studies on the apolipoprotein levels and lipoprotein forms of cord serum provide part of the data necessary for studying the progressive changes in the human lipid transport system from its fetal form to that of the adult.Studies on the human adult serum lipid transport system have established that the major serum lipids (triacylglycerol, cholesterol, cholesteryl esters, and phospholipids) are bound to particular protein constituents (14, 32). designated apolipoproteins. Such lipid-protein complexes (lipoproteins) have been most commonly classified on the basis of two of their characteristic physical properties. i.e., hydrated density (26) and charge (30).Studies on the antigenic components of the major lipoprotein density classes and electrophoretic bands in the human adult have clearly demonstrated their protein heterogeneity (4, 37) and lead to a classification system based on apolipoproteins as the only distinct chemical markers of this system (1, 2). This concept has been developed into the lipoprotein family theory and has been described elsewhere (2). Recently, the levels of all well-recognized apolipoproteins have been reported (3).Application of these physicochemical techniques to cord sera has established that compared to normal adult levels, very low density lipoprotein (VLDL) is virtually absent (39) or present in low concentrations (13, 15), low-density lipoprotein (LDL) is markedly decreased (8,42), and the predominant lipoprotein density class is high-density lipoprotein (49). In addition, the lipid levels of cord sera are also lower than the corresponding levels in adult sera (42,49,50). However, it has not been established whether there is a correlation between the decreased cord serum lipid levels (42,49,50) and the absence or diminished level of some or all of the apolipoproteins. The studies described herein are the first...

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confidence: 91%

“…Only the total cholesterol levels of males and females were significantly different (P < 0.05). The lower levels of cholesterol in males agree with studies on sex differences in cord sera at birth (9,10).…”

supporting

confidence: 87%

Studies on the Apolipoproteins and Lipoproteins of Cord Serum

McConathy

Lake

1980

Pediatr Res

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“…Platelet activating factor (PAF) is an ether linked phospholipid, produced by a variety of inflammatory cells which has several properties relevant to a mediator of allergic inflammation Barnes et al, 1988). PAF increases vascular permeability in a number of tissues including the airways (Evans et al, 1987), and is the most potent chemoattractant for eosinophils described to date (Wardlaw et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Effect of a PAF antagonist, BN52063, on PAF‐induced bronchoconstriction in normal subjects.

Roberts

McCusker

Chung

et al. 1988

Brit J Clinical Pharma

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1. The effects of an oral platelet activating factor (PAF) antagonist, BN52063, or matched placebo on inhaled PAF challenge were assessed in a double‐blind study in eight normal subjects. 2. PAF (24 micrograms) induced an immediate bronchoconstriction, with a maximum fall in flow at 30% of vital capacity from a partial flow volume manoeuvre (Vp30) of 47.1 +/‐ 7% (mean +/‐ s.e. mean) 5 min after inhalation following placebo treatment. Repeated PAF challenges at 15 min intervals resulted in tachyphylaxis of the bronchoconstrictor response. 3. Two hours after the ingestion of BN52063 (120 mg) the maximum bronchoconstriction induced by inhaled PAF was attenuated (35.9 +/‐ 9% fall at 5 min) with a significant reduction (P less than 0.05) in response after the first and second inhalations. 4. Inhaled PAF induced an immediate neutropenia (73.2 +/‐ 9% fall 5 min after inhalation) followed by a rebound neutrophilia, which were unaffected by pretreatment with BN52063. 5. Oral ingestion of a dose of BN52063 which is effective in reducing skin responses to PAF gave partial protection against the bronchoconstrictor effect of inhaled PAF in normal subjects.

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“…In particular, BK is known to be produced during nasal allergen exposure (21,22), where it binds to human nasal mucosa (23) and evokes severe bronchoconstriction during asthma (24). The bradykinin structure within the kininogen sequence .…”

mentioning

confidence: 99%

A Novel Mechanism for Bradykinin Production at Inflammatory Sites

Kozik¹,

Moore²,

Potempa³

et al. 1998

Journal of Biological Chemistry

103

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Coprocessing of kininogens by a mixture of human mast cell tryptase and neutrophil elastase was explored as a potential substitute for the kallikrein-dependent pathway for kinin generation during inflammation. Tryptase easily excised bradykinin from the synthetic heptadecapeptide, ISLMKRPPGFSPFRSSR, but was unable to produce significant amounts of kinin by proteolysis of kininogens. However, a mixture of tryptase and elastase released bradykinin from each protein with a yield comparable to that of human plasma kallikrein. Significantly, neither plasma nor tissue kallikrein was able to effectively process N-chlorosuccinimide-oxidized high molecular weight kininogen, an effect attributed to the oxidation of a methionine residue upstream from the N terminus of the kinin domain. In support of these results the model heptadecapetide, ISL(MO)KRP-PGFSPFRSSR, was also resistant to hydrolysis by either kallikrein. In contrast, the release of bradykinin from oxidized peptide or protein substrates by the tryptase/ elastase mixture was not altered. Because kininogen modification may occur at inflammatory sites, as a result of the oxidative burst of recruited neutrophils and macrophages, these results suggest an alternative pathway for kinin production and the necessity for the novel utilization of two specific proteinases known to be released from these cells during inflammatory episodes.

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THE f* MESON PRODUCED IN K$sup -$p INTERACTION 4.6 AND 5.0 Bev/c

Cited by 8 publications

References 0 publications

Studies on the Apolipoproteins and Lipoproteins of Cord Serum

Studies on the Apolipoproteins and Lipoproteins of Cord Serum

Effect of a PAF antagonist, BN52063, on PAF‐induced bronchoconstriction in normal subjects.

A Novel Mechanism for Bradykinin Production at Inflammatory Sites

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