Late adverse effects of streptokinase.
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Humans↗
Biomedical subjects
C N Chesterman
Publications and source records attributed to C N Chesterman.
Platelet-derived growth factor and alternative splicing: a review.
The mitogenic and chemotactic potency of platelet-derived growth factor (PDGF) has linked this polypeptide to the pathogenesis of several disease states including atherosclerosis and neoplasia. We have reviewed the recent literature on aspects relating to the structure, distribution and biology of PDGF and its high-affinity cell-surface and intracellular receptors. In addition to platelets, several normal and tumor cells secrete the mitogen in one or more of three possible dimeric configurations. Alternative splicing of exon 6 in PDGF A-chain RNA results in the formation of two protein species with different carboxy-termini. Initially, it was thought that the longer A-chain variant was processed only by transformed cells. However, recent evidence indicates that alternative splicing occurs in several cells which express the A-chain, including early Xenopus embryos. The functional significance of the exon 6 product, a highly basic region spanned by 18 amino acid residues (A194-211), is not precisely clear. We have summarized recent findings which implicate roles for A194-211 in the processing, secretion, and mitogenesis of the A-chain homodimer, nuclear transport signalling, and heparin binding. Thus, alternative splicing could play an important role in the modulation of the functional properties of the PDGF A-chain variants per se and in the complex interactive network of polypeptide growth factors and cytokines.
Alternative Splicing↗
Establishment in culture and characterization of a strain with mast cell and monocytic properties from the bone marrow of a child with diffuse cutaneous mastocytosis.
Bone marrow was isolated from a child with congenital mastocytosis. Upon prolonged in vitro culture, initially in the presence of interleukin-3 (IL-3), a population of relatively large fusiform, strongly adherent cells grew out plus a subpopulation of smaller nonadherent cells. The morphology of the adherent cells was not typical of fibroblasts, epithelial cells, nor of standard hematopoietic cell types, whereas the morphology of the nonadherent cells resembled mast cells. Neither cell type required the presence of IL-3 nor a feeder layer of fibroblasts for continued growth. Attempts to isolate the two populations were unsuccessful. This cell strain comprised of both cell populations has been termed human bone marrow-derived mastocytosis cells (HBM-M). These cells were found to possess some of the cytochemical, ultrastructural, and surface phenotypic features of degranulated mast cells. They reacted with the mast cell marker, monoclonal antibody YB5.B8, but not with the basophil specific monoclonal antibody Bsp-1 and released the inflammatory mediators histamine, leukotriene C4, prostaglandin D2, and platelet-activating factor constitutively. This release was not potentiated by immunologic- or nonimmunologic-activating stimuli. In addition, they exhibited cytochemical and surface phenotypic features of monocytes. Our results indicate that a population of abnormal proliferative cells exist in the marrow of this patient; that these cells may be responsible for the patient's pronounced systemic proliferation of mast cells and the associated symptoms; and that the cell's mast cell, monocyte properties may be indicative of a common bone marrow-derived mast cell/monocyte precursor.
Antibodies, Monoclonal↗
A crossreactive antipeptide monoclonal antibody with specificity for lysyl-lysine.
Synthetic peptides meeting certain guidelines have been used as immunogens to generate antibodies with predefined specificity. We have raised and characterized using established methods a monoclonal antibody against a synthetic peptide corresponding to the 18-amino acid carboxyterminal sequence (A194-211) of the platelet-derived growth factor (PDGF) A chain expressed by the U343 human glioma cell line. This antibody was generated in order to carry out structure-function studies on this region of PDGF whose biological significance is not yet clear. Anti-PDGF-A194-211 was found to be a low titre, IgM kappa molecule, with a Kd of 2.8 x 10(-7) M. When antibody reactivity was tested with parent PDGF-AAL (A chain homodimer containing a carboxyterminal extension) significant binding was observed. Surprisingly, 125I-PDGF-AAS, consisting of truncated A chains but lacking the extension was also bound. Moreover, poly-L-lysine, beta-thromboglobulin, PDGF-A194-211, and myoglobin competed dose-dependently with 125I-PDGF-AAL for antibody. 125I-bovine serum albumin was also bound. Examination of the primary sequence of proteins and peptides bound by the antibody revealed only one shared structural motif: a lysyl-lysine moiety. Selected small synthetic peptides containing this and other sequences were used as potential competitors of 125I-PDGF-A194-211 in antibody binding. Lysyl-lysyl-glycyl-glutamic acid [corrected] and lysyl-lysine competed, whereas lysyl-leucine did not. These results suggest that as few as two amino acid residues constitute a functional antigenic determinant and contrast with most previous estimates of the minimum number of residues required. Furthermore, we show that guidelines governing the design of synthetic peptides for their use as antigens to produce monoclonal antibodies of predetermined specificity may be unreliable.
Amino Acid Sequence↗
Characterization of the binding domains on platelet glycoproteins Ib-IX and IIb/IIIa complexes for the quinine/quinidine-dependent antibodies.
Sera of 12 patients with quinine/quinidine-induced thrombocytopenia showed drug-dependent antibody binding to glycoprotein (GP) Ib-IX complex. The reaction with GPIb-IX complex of 11 of these 12 sera was strongly inhibited by the complex-specific monoclonal antibodies (MoAbs) AK1 and SZ1. The exception was a quinine-induced serum designated BU. The reaction of the six quinidine-induced sera was also partially blocked by an anti-GPIX MoAb, FMC25. Only 3 of the 12 patient sera showed drug-dependent antibody binding to GPIIb/IIIa, which was strongly inhibited by the anti-GPIIIa MoAb 22C4, and the anti-GPIIb alpha MoAb SZ22. With detergent-solubilized Serratia metalloprotease-treated platelets, quinine/quinidine-induced sera, except BU, immunoprecipitated a membrane-bound proteolytic fragment of GPIb-IX complex. In contrast, BU immunoprecipitated glycocalicin and a 40-Kd peptide tail fragment of GPIb alpha from the cell supernatant. Using purified GPIb-IX complex or its components as the target antigen, all the quinine-induced sera, except BU, immunoprecipitated GPIb-IX complex but failed to immunoprecipitate GPIb, GPIX, or the complex reformed from GPIb and GPIX. The quinidine-induced sera strongly immunoprecipitated purified GPIb-IX complex, weakly immunoprecipitated purified GPIX and the recombined complex, but did not immunoprecipitate purified GPIb. The combined data suggest that one quinine-dependent antibody (BU) recognizes an epitope in the peptide tail region of GPIb alpha and the other five quinine-dependent antibodies react with a complex-specific epitope on the membrane-associated region of GPIb-IX complex, whereas each of the six quinidine-induced sera contain two drug-dependent antibodies, one reactive with the GPIb-IX complex-specific epitope and the other reactive with GPIX. The binding domain(s) on GPIIb/IIIa for the quinine/quinidine-dependent antibodies appear to be sterically close to the epitopes for 22C4 and SZ22.
Antibodies↗
GMP-140 binding to neutrophils is inhibited by sulfated glycans.
GMP-140 is a 140-kDa granule membrane glycoprotein localized to the alpha-granules of platelets and the Weibel-Palade bodies of endothelial cells. Expression of GMP-140 on the activated cell surface has been shown to mediate the adhesion of thrombin-activated platelets to neutrophils and monocytes and the transient adhesion of neutrophils to endothelium. In contrast, fluid-phase GMP-140 strongly inhibits the CD18-dependent adhesion of tumor necrosis factor alpha-activated neutrophils to endothelium suggesting that GMP-140 can also serve an anti-adhesive function. In the present report, it is demonstrated that fluid-phase GMP-140 which exists predominantly as a tetramer binds to a single class of high affinity receptor on neutrophils and HL60 cells. Binding of 125I-labeled GMP-140 to neutrophils and HL60 cells and the rosetting of neutrophils and HL60 cells by thrombin-activated platelets were inhibited by EDTA, excess unlabeled fluid-phase GMP-140, Fab fragments of an affinity-purified rabbit anti-GMP-140 antibody, and by the murine anti-GMP-140 monoclonal antibody, AK 4. Both neutrophil and HL60 GMP-140 binding and platelet rosetting were strongly inhibited by heparin, fucoidin, and dextran sulfate 500,000, were partially inhibited by dextran sulfate 5,000 and lambda- and kappa-carrageenan, but were not inhibited by chondroitins 4- and 6-sulfate. Since this sulfated glycan specificity is identical to that previously reported by us for GMP-140, the present results suggest that the sulfated glycan binding site and the neutrophil receptor binding site on GMP-140 are either identical or proximal.
Antibodies, Monoclonal↗
Novel human PDGFA gene transcripts derived by alternative mRNA splicing.
The polymerase chain reaction (PCR) has been used to amplify sequences coding for the platelet-derived growth factor A chain (PDGFA) using mRNA populations derived from two transformed cell lines (a human osteosarcoma, U-2OS, and a human glioma, U-343) and from human umbilical vein cells. The primers used for PCR were designed to amplify both of the two transcripts previously reported for the PDGFA gene. These transcripts differ from each other by the presence or absence of sequences from a sixth exon located near the 3' end of the gene. The PCR procedure revealed not only these expected transcripts, but additional RNAs that were shown by cloning and sequencing to lack exon 2. These species were present at variable levels in the three cell types examined. We propose that this novel splicing pattern, generating mRNAs encoding truncated and non-functional polypeptides, signals an additional, post-transcriptional mechanism for modulation of PDGFA gene expression.
Base Sequence↗
Immunology and clinical importance of antiphospholipid antibodies.
Having reviewed the literature on the association of aPL antibodies with clinical manifestations, it is clear that this group of autoantibodies are of considerable importance. The presence of aPL antibodies in some but not all individuals confers a risk of a clinical syndrome characterized by recurrent arterial or venous thrombosis, thrombocytopenia, hemolytic anemia, or positive Coombs' test, and in females, recurrent idiopathic fetal loss. In SLE, the risk is approximately 40%, compared with a risk of 15% in the absence of aPL antibodies. However, only one half of persons possessing these antibodies have SLE, and overall the risk is around 30%. In some circumstances, such as in chlorpromazine or infection-associated aPL antibodies, there appears to be no increased risk. At the other end of the spectrum are seen patients whose only clinical manifestations comprise features of this clinical syndrome, and this entity has been designated the primary antiphospholipid syndrome (PAPS). aPL antibodies are also important because they are not uncommon. They have been found frequently in women with idiopathic recurrent fetal loss (30%), in non-autoimmune patients with ischemic heart disease (20%), or venous thrombosis (up to 30%), or stroke (4-47%), and in chronic immune thrombocytopenia (30%). These autoantibodies can be detected using sensitive solid-phase immunoassays employing the CL antigen, or in appropriate coagulation tests to detect LA activity. These assays are simple to perform but require care in selection of the best test and in interpretation of results. Current tests do not distinguish between those persons at risk of the clinical events and those not at risk. Detection of specific isotypes (especially IgG) and antibody level may aid in such a designation. Treatment of aPL antibody-associated syndromes remains a controversial subject. Since thromboses are associated with significant morbidity and potential mortality, there is a good argument for long-term preventive antithrombotic therapy, at least for as long as the antibodies are detectable, in those patients in whom clinical complications have previously occurred. It is not generally recommended that this treatment be offered to individuals in whom aPL antibodies are detected but who have not suffered previous thromboses, since the risk of such events does not appear to be equal within a group of aPL antibody-positive persons. This particularly applies to pregnant women, since live births and uncomplicated pregnancies are observed regularly in the presence of aPL antibodies without specific treatment. A previous history of at least one unexplained, late fetal loss is considered a prerequisite before intervention in subsequent pregnancies.(ABSTRACT TRUNCATED AT 400 WORDS)
Anemia, Hemolytic↗
Increased plasma beta-thromboglobulin in patients with coronary artery vein graft occlusion: response to low dose aspirin.
The therapeutic effect of aspirin on vein graft patency was studied in patients undergoing coronary artery bypass graft surgery. The study design enabled the prospective evaluation of the relation of platelet activation, as measured by plasma beta-thromboglobulin concentration, to subsequent coronary vein graft occlusion. Serial beta-thromboglobulin levels were measured in 105 patients randomized to receive aspirin (324 mg/day) or placebo beginning within 1 h after surgery. Graft patency was assessed angiographically at 1 week and 1 year after surgery. Of 49 patients receiving placebo, 17 (34.7%) had one or more graft occlusions, 6 early, 10 late and 1 with both early and late occlusion. Of 56 patients receiving aspirin, 7 (12.5%) had one or more occlusions, 3 early and 4 late (p less than 0.01). Preoperatively, the beta-thromboglobulin level in surgical patients (29 +/- 13.5 ng/ml) was significantly higher than that of 51 control subjects (22.6 +/- 11.1 ng/ml) (p less than 0.004). Plasma beta-thromboglobulin levels remained comparatively constant at 3 and 12 months after surgery in the 43 patients who had both samples available (p less than 0.001, r = 0.65). The reduction in beta-thromboglobulin concentration from the preoperative level to 12 months postoperatively was greater in the aspirin-treated group (p less than 0.001). Multivariate logistic regression analysis demonstrated a significant association between preoperative beta-thromboglobulin concentration and graft occlusion (p less than 0.02), and aspirin treatment was effective in preventing occlusion when adjusted for the preoperative beta-thromboglobulin level (p less than 0.005). Plasma beta-thromboglobulin concentrations are elevated in patients with coronary artery disease, suggesting ongoing platelet activation.(ABSTRACT TRUNCATED AT 250 WORDS)
Adult↗
Anti-phospholipid antibodies are directed against a complex antigen that includes a lipid-binding inhibitor of coagulation: beta 2-glycoprotein I (apolipoprotein H).
Anti-phospholipid (aPL) antibodies that exhibit binding in cardiolipin (CL) ELISA can be purified to greater than 95% purity by sequential phospholipid affinity and ion-exchange chromatography. However, these highly purified aPL antibodies do not bind to the CL antigen when assayed by a modified CL ELISA in which the blocking agent does not contain bovine serum, nor do they bind to phospholipid affinity columns. Binding to the phospholipid antigen will only occur if normal human plasma, human serum, or bovine serum is present, suggesting that the binding of aPL antibodies to CL requires the presence of a plasma/serum cofactor. Using sequential phospholipid affinity, gel-filtration, and ion-exchange chromatography, we have purified this cofactor to homogeneity and shown that the binding of aPL antibodies to CL requires the presence of this cofactor in a dose-dependent manner. N-terminal region sequence analysis of the molecule has identified the cofactor as beta 2-glycoprotein I (beta 2GPI) (apolipoprotein H), a plasma protein known to bind to anionic phospholipids. These findings indicate that the presence of beta 2GPI is an absolute requirement for antibody-phospholipid interaction, suggesting that bound beta 2GPI forms the antigen to which aPL antibodies are directed. Recent evidence indicates that beta 2GPI exerts multiple inhibitory effects on the coagulation pathway and platelet aggregation. Interference with the function of beta 2GPI by aPL antibodies could explain the thrombotic diathesis seen in association with these antibodies.
Amino Acid Sequence↗
Prevalence of lupus anticoagulant and anticardiolipin antibodies in a healthy population.
This study was designed to explore the incidence of lupus anticoagulant (LA) and anticardiolipin antibodies (ACA) and their relationship to each other in a healthy population of 499 blood donors. Plasma samples were tested for LA activity and IgG, IgM and polyvalent ACA. Prolongation of the kaolin clotting time of a mixture of 80% normal plasma and 20% test plasma compared to the normal (dKCT) was used to detect LA activity. A normal distribution of dKCT was found with the mean 3.5 seconds +/- SD 10.6 seconds. Forty subjects (8%) were greater than 10% of the normal control; among these, 18 (3.6%) were outside the 95% confidence limits. The median age (29.3) and sex (M = 12, F = 28) of the 40 subjects with prolonged KCT were significantly different (p less than 0.001) from the group as a whole, younger females predominating. The frequency distribution of IgG, IgM and polyvalent ACA was skewed and the majority did not have detectable levels. ACA concentration falling within 95% of the population group were regarded as normal. Applying this definition, abnormal IgG ACA was greater than 4.33 U/ml, IgM ACA greater than 3.55 U/ml and polyvalent ACA greater than 4.55 U/ml with a prevalence of 4.6%, 4.6% and 5.6% respectively. Of the subjects with positive ACA of any class there was no significant association with either age or sex or the presence of LA. Only three plasma samples had both activities. Neither ACA nor LA were associated with antinuclear antibodies (ANA) or rheumatoid factor (Rh factor). Thus, in a healthy population LA is found predominantly in younger females and neither LA or ACA appear to identify subjects with other autoimmune parameters such as ANA or Rh factor or, for that matter, each other.
Adult↗
The effect of heparin and other glycosaminoglycans on levels of tissue plasminogen activator and plasminogen activator inhibitor in cultured human umbilical vein endothelial cells.
Human umbilical vein endothelial cells (HUVEC) were cultured in the presence of various glycosaminoglycans and the intracellular levels of tissue plasminogen activator (tPA) and plasminogen activator inhibitor-1 (PAI-1) measured by ELISA. 10 IU/ml heparin (90 micrograms/ml) brought about a significant (20-fold) increase in intracellular tPA levels over the 6-day culture period; intracellular PAI-1 levels were significantly decreased (by 60-70%) and culture growth rate promoted. The final cell density of heparin-containing cultures was 1.7 to 2.3 times greater than that of control cultures. Low molecular weight heparin (First International Standard) had similar effects but was less potent than unfractionated heparin. Chondroitin sulphate and heparan sulphate had no effect on tPA and PAI-1 levels but dermatan sulphate reduced PAI-1 significantly. The changes observed following exposure of HUVEC to heparin are consonant with the view that glycosaminoglycans may affect endothelial production of fibrinolytic components.
Cell Division↗
Characterization of human platelet GMP-140 as a heparin-binding protein.
Human platelet GMP-140 has been identified as a heparin-binding protein. Purified platelet GMP-140 bound to Heparin-Sepharose CL-6B and was eluted by approximately 0.5 M sodium chloride. Radioiodinated GMP-140 bound specifically and saturably to heparin immobilized on Matrex-Pel 102 beads. Binding of radioiodinated GMP-140 to heparin-Matrex-Pel 102 beads was divalent cation-independent and was strongly inhibited by excess fluid phase GMP-140 and heparin and by other sulfated glycans such as fucoidin and dextran-sulfate. Binding was not inhibited by chondroitins 4- and 6-sulfate or mannose 6-phosphate.
Antibodies, Monoclonal↗
Heparin-induced thrombocytopenia: studies with a new low molecular weight heparinoid, Org 10172.
Studies were performed to determine the cross-reaction rate of the heparin-dependent antibody with Org 10172, a new low molecular weight heparinoid, and to investigate the effect of Org 10172 on platelet activation induced by the antibody. The plasmas of 17 patients with thrombocytopenia induced by standard heparin were shown, by platelet aggregation studies, to contain the heparin-dependent antibody. Of these 17 patient plasmas, only three cross-reacted with the heparinoid, producing a cross-reaction rate of 18%. When Org 10172 was added to a reaction mixture containing normal platelet-rich plasma, patient plasma, and standard heparin with non-cross-reacting plasmas, it inhibited platelet aggregation and thromboxane B2 production induced by the antibody, provided that the ratio of Org 10172 concentration (anti-Xa U/mL) to standard heparin concentration (IU/mL) exceeded 2.5 to 5.0. This inhibitory effect was observed only with platelet activation mediated by the antibody, but not by collagen (2 micrograms/mL) or ADP (5.0 mumol/L). Additionally, three of 17 patients with serious thrombosis, whose plasma showed no cross-reaction with the heparinoid, received Org 10172 treatment with a good response in each case. These findings suggest that Org 10172 may be a useful drug for the treatment of heparin-induced thrombocytopenia.
Antigen-Antibody Reactions↗
Hyperinducible gene expression from a metallothionein promoter containing additional metal-responsive elements.
We describe the development of metallothionein-based vectors with low basal levels of expression that are hyperinducible upon treatment with heavy metals. Vectors were constructed by substituting a region in the hMTIIA promoter (bp -70 to -129) containing an element (BLE) involved in basal level expression with multiple metal responsive elements (MREs). In expression studies utilizing cat as a reporter gene, heavy metal inducibility was examined in both transiently transfected and permanently transformed Chinese hamster ovary (CHO) cells. Our results demonstrate that, within the same promoter structure, inducibility can be increased by altering the ratio of MREs to BLEs. Optimal induction of expression in permanently transformed CHO cells was achieved by exposure to heavy metals for 48 h prior to cell harvest, with an additional boost 12 h before harvest. These vectors have the potential to be used for production of proteins in cultured mammalian cells and in gene expression in transgenic animals.
Animals↗
Heparin-induced thrombocytopenia: mechanism of interaction of the heparin-dependent antibody with platelets.
The interaction of the heparin-dependent antibody with heparin and platelets has been studied using the sera and purified IgG of four patients with heparin-induced thrombocytopenia. Both normal platelets and Bernard-Soulier syndrome (BSS) platelets which lack glycoprotein (GP) Ib. GPV and GPIX, aggregated in response to patient serum or IgG, but only in the presence of heparin. A monoclonal antibody (Mab) against platelet Fc II receptor (IV.3) strongly inhibited the heparin-dependent aggregation of both normal and BSS platelets induced by patient sera/IgG. Inhibition by the anti-GPIb Mab (AK2) was variable and occurred only with normal platelets. Anti-GPIX Mab (FMC 25) was not inhibitory with either normal or BSS platelets. Similar results were obtained using 14C-serotonin release instead of platelet aggregation as a measure of platelet activation. These findings suggest that (1) the reaction of the heparin-dependent antibody with platelets and heparin is mediated by a Fc-dependent mechanism, (2) GPIb, GPV and GPIX are not involved in this reaction, and (3) the inhibitory effect of anti-GPIb Mab on normal platelets is due to steric interference consistent with the platelet Fc receptor being in close proximity to GPIb.
Antibodies, Monoclonal↗
Anticardiolipin antibodies and lupus anticoagulants comprise separate antibody subgroups with different phospholipid binding characteristics.
Autoantibodies to phospholipid antigens can be characterized using solid phase immunoassays to detect anticardiolipin antibodies (ACA) or in phospholipid-dependent clotting tests where lupus anticoagulant (LA) activity can be demonstrated. It has not been established whether each activity is due to the same or separate antibody subgroups. Plasma from two patients with high levels of both activities were used for purification of ACA and LA using sequential ion-exchange, gel-filtration, and anti-Ig affinity chromatography. Plasma could be separated into fractions containing each activity in the absence of the other. In these fractions, antibodies responsible for LA activity do not bind to isolated phospholipids in solid phase immunoassays, and conversely antibodies binding in these assays (ACA) do not possess LA activity, suggesting LA are directed against a more complex lipid epitope. In addition, in one patient ACA was of IgG isotype only, whilst LA was due to IgG and IgM isotypes. In this patient, the IgG-ACA was heterogeneous with three peaks clearly separated on ion-exchange chromatography. Affinity purified antiphospholipid antibodies have been previously prepared from a number of patients using a phosphatidyl-serine column and antibodies purified in this manner possess ACA but not LA activity. Taken together, these data indicate that tests for ACA and LA define separable subgroups of phospholipid binding antibodies, thus explaining the discordance often seen between the two activities.
Adult↗
Effects of fish oil supplementation on glucose and lipid metabolism in NIDDM.
Fish oils, containing omega-3 fatty acids (omega 3FAs), favorably influence plasma lipoproteins in nondiabetic humans and prevent the development of insulin resistance induced by fat feeding in rats. We studied the effects of fish oils in 10 subjects (aged 42-65 yr) with mild non-insulin-dependent diabetes mellitus (NIDDM). Subjects were fed a standard diabetic diet plus 1) no supplementation (baseline), 2) 10 g fish oil concentrate (30% omega 3FAs) daily, and 3) 10 g safflower oil daily over separate 3-wk periods, the latter two supplements being given in radom order by use of a double-blind crossover design. At the end of each diet period, fasting blood glucose (FBG), insulin, and lipids were measured, and insulin sensitivity was assessed with a hyperinsulinemic-euglycemic clamp performed with [3-3H]glucose. FBG increased 14% during fish oil and 11% during safflower oil supplementation compared with baseline (P less than .05), whereas body weight, fasting serum insulin levels, and insulin sensitivity were unchanged. The absolute increase in FBG during each supplementation period correlated with the baseline FBG (fish oil, r = .83, P less than .005); safflower oil, r = .75, P = .012). Fasting plasma triglyceride levels decreased during fish oil supplementation in the 4 subjects with baseline hypertriglyceridemia (greater than 2 mM) but were not significantly reduced overall. There was no significant change in fasting plasma total, high-density lipoprotein, and low-density lipoprotein cholesterol levels. In summary, dietary fish oil supplementation adversely affected glycemic control in NIDDM subjects without producing significant beneficial effects on plasma lipids. The effect of safflower oil supplementation was not significantly different from fish oil, suggesting that the negative effects on glucose metabolism may be related to the extra energy or fat intake.(ABSTRACT TRUNCATED AT 250 WORDS)
Blood Glucose↗