Does increased lipase activity in serum imply damage to the pancreas?
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Humans↗
Biomedical subjects
F S Apple
Publications and source records attributed to F S Apple.
Time course of serum protein changes after strenuous exercise of the forearm flexors.
The time course of changes in serum proteins and other blood constituents after eccentric exercise of the forearm flexors by six nonweight-trained female subjects (age, 19.7 +/- 1.9 years) was investigated. Eccentric muscle actions are those in which the muscle lengthens as it exerts force, as when a person lowers a weight. Serum levels of creatine kinase, lactate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, gamma-glutamyl transpeptidase, myoglobin, as well as urea nitrogen, uric acid, creatinine, calcium, and phosphorus were examined before and for 6 days after exercise. Creatine kinase increased dramatically (peak value ranged from 6740 to 24,200 U/L) and aspartate aminotransferase, lactate dehydrogenase, alanine aminotransferase, and myoglobin followed the same time course as creatine kinase, but their peak values were lower. These proteins did not increase significantly until 48 hours after exercise and reached peak values 3 to 5 days after exercise. Alkaline phosphatase, gamma-glutamyl transpeptidase, uric acid, urea nitrogen, creatinine, calcium, and phosphorus showed no change. There is either a delay in muscle protein release by damaged muscle fibers, or the proteins are unable to leave the interstitial area for the 24 to 48 hour period after exercise. Because of the long delay, care should be taken when blood protein levels are interpreted in persons who have exercised strenuously (even if only for a short period of intense effort) several days before any diagnostic tests are performed.
Adolescent↗
Clinical chemistry.
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Chemistry, Clinical↗
Geographic distribution of xanthine oxidase, free radical scavengers, creatine kinase, and lactate dehydrogenase enzyme systems in rat heart and skeletal muscle.
The geographic distribution of the following enzyme systems is described in the rat heart (left and right ventricles) and in different skeletal muscles (soleus, plantaris, and red and white gastrocnemius): xanthine oxidase and dehydrogenase, creatine kinase isoenzymes, lactate dehydrogenase isoenzymes, and the free radical scavenger enzymes superoxide dismutase, glutathione reductase, and glutathione peroxidase. No substantial difference in enzyme activities was observed between the left and right ventricles. Skeletal muscles showed a clear distinction between enzyme activities depending on their composition of oxidative fibers and glycolytic fibers.
Animals↗
Iron status of active women and the effect of running a marathon on bowel function and gastrointestinal blood loss.
This study compared the bowel function, fecal hemoglobin (Hb) loss, iron status and diets of 36 women of varying activity levels. In addition, we examined the effect of a marathon race on bowel function and fecal Hb loss in 15 of these women. The subjects were divided into 4 groups based on estimated daily exercise energy expenditure: Group A) less than 400 kcal/d (less than 1674 kJ/d); Group B) 400-599 kcal/d (1674-2507 kJ/d); Group C) 600-800 kcal/d (2511-3348 kJ/d); and Group D) greater than 800 kcal/d (greater than 3348 kJ/d). There were no differences in hematological and iron indexes among the 4 groups. Mean daily stool wet weights and individual stool weights were greater for groups B and D as compared to group A. However, transit time and frequency of defecation were not different. Daily fecal Hb losses (mg/day) were greater in groups B, C, and D as compared to A, but there was no difference in fecal Hb concentrations (mg/g feces) among the groups. Dietary intakes of energy, protein, fat and fiber were similar for all groups. Ascorbic acid and iron intakes from food significantly increased with increased estimated daily energy expenditure. Total intakes of ascorbic acid and iron, including oral supplements, were not different among the groups. Marathon racing resulted in a 21% increase in mean transit time, a 27% decrease in daily stool weight and 21% lower frequency of defecation. Fecal Hb concentrations and daily Hb losses before and after the race were not significantly different, despite an increased daily Hb loss in 10 of the 15 runners after the race.(ABSTRACT TRUNCATED AT 250 WORDS)
Adult↗
Canine myocardial creatine kinase isoenzymes after chronic coronary artery occlusion.
BACKGROUND: Creatine kinase (CK) exists as three cytosolic isoenzymes, CK-MM, CK-MB, and CK-BB, and one mitochondrial isoenzyme. Animal and human observations suggest that the CK-MB content of myocardium is dynamic and may increase in response to ischemia, but the response of the myocardial CK system to chronic coronary artery occlusion is not well-defined. METHODS AND RESULTS: We measured serial changes in myocardial total CK, percent CK-MB, and percent CK-BB before and 3 weeks after coronary artery occlusion in 17 pentobarbital-anesthetized dogs. Tissue biopsies were obtained from the left anterior descending (LAD) coronary artery myocardium, the right coronary artery (RCA) myocardium, and the circumflex coronary artery myocardium at baseline and 3 weeks after LAD occlusion (n = 6), RCA occlusion (n = 5), and no coronary artery occlusion (n = 6). Tissue samples were assayed for total CK, percent CK-MB, and percent CK-BB. Samples were also examined by electron microscopy for evidence of ischemic myopathy. Total myocardial CK activity did not change over 3 weeks. Percent CK-MB increased significantly in the tissue supplied by the occluded artery (4.1-fold in dogs with LAD occlusion and 6.7-fold in dogs with RCA occlusion). Percent CK-BB did not change. Dogs with LAD occlusion had ultrastructural evidence of myopathic fibers interspersed with normal fibers in the LAD myocardium. Dogs with RCA occlusion had no ultrastructural evidence of myopathic fibers in the RCA myocardium. CONCLUSIONS: Chronic coronary artery occlusion causes a pronounced change in the canine myocardial CK system that is limited to the tissue supplied by the occluded coronary artery. These biochemical alterations do not correlate with any cellular ultrastructural changes. Myocardial CK-MB content is dynamic, varies geographically within the heart, and increases rapidly after coronary artery occlusion.
Animals↗
Biochemical mechanisms for oxygen free radical formation during exercise.
The biochemical mechanisms behind skeletal muscle soreness and damage with muscular overuse have remained unclear. Recently, however, a growing amount of evidence indicates that free radicals play an important role as mediators of skeletal muscle damage and inflammation. During exercise, two of the potentially harmful free radical generating sources are semiquinone in the mitochondria and xanthine oxidase in the capillary endothelial cells. During high intensity exercise the flow of oxygen through the skeletal muscle cells is greatly increased at the same time as the rate of ATP utilisation exceeds the rate of ATP generation. The metabolic stress in the cells causes several biochemical changes to occur, resulting in a markedly enhanced rate of production of oxygen free radicals from semiquinone and xanthine oxidase. During normal conditions free radicals are generated at a low rate and subsequently taken care of by the well developed scavenger and antioxidant systems. However, a greatly increased rate of free radical production may exceed the capacity of the cellular defence system. Consequently, a substantial attack of free radicals on the cell membranes may lead to a loss of cell viability and to cell necrosis and could initiate the skeletal muscle damage and inflammation caused by exhaustive exercise.
Adenosine Triphosphate↗
Financial impact of a rapid CK-MB-specific immunoassay on the diagnosis of myocardial infarction.
The purpose of this study was twofold. First, we evaluated the financial impact of a rapid, monoclonal antibody-based CK-MB mass assay (Stratus, Dade Division, Baxter Laboratories, Miami, Fla) for the direct measurement of CK-MB in serum samples from 65 patients admitted to the coronary care unit with the possible diagnosis of acute myocardial infarction. Second, we evaluated retrospectively the Stratus assay and an activity assay (electrophoresis) for CK-MB in the following patient categories: acute myocardial infarction treated with and without thrombolytic therapy, angina, congestive heart failure, skeletal muscle trauma, and the acutely ill without acute myocardial infarction. The advantageous features of the Stratus mass assay were as follows. First, the laboratory was able to perform the assay more frequently because of the short assay time per specimen (less than 10 minutes) without additional personnel. This had a substantial impact on the clinician's ability to diagnose acute myocardial infarction and to move patients out of an intensive care unit at substantial financial savings to the patient, the hospital, or the third-party payer. Second, the Stratus assay was able to detect low levels of CK-MB (1 to 2 micrograms/L) in the presence of low total creatine kinase activity (less than 100 U/L). Third, the Stratus assay showed no interference due to very-high-total creatine kinase activities (greater than 100,000 U/L), CK-BB, macro-creatine kinase, and mitochondrial creatine kinase.
Blood Protein Electrophoresis↗
Canine myocardial creatine kinase isoenzyme response to coronary artery occlusion.
The response of the myocardial creatine kinase system to acute coronary artery occlusion is not well defined. In the present study, we measured serial changes in myocardial creatine kinase and creatine kinase-MB activities after acute occlusion of the left anterior descending (LAD) coronary artery in 20 open-chest pentobarbital-anesthetized dogs. Tissue samples were obtained from both ischemic and nonischemic left ventricular myocardium at base line and 1-, 3-, and 5-h intervals after LAD occlusion and assayed for total creatine kinase and the isoenzymes creatine kinase-MM, and creatine kinase-MB. Total creatine kinase activity declined significantly in both the ischemic and the nonischemic tissue because of a decline in creatine kinase-MM activity. Concomitantly, creatine kinase-MB activity increased significantly in both the ischemic and the nonischemic tissue. These changes were observed when the duration of the LAD occlusion was 3 h or longer, but not when the duration of the occlusion was 1 h. Thus acute myocardial ischemia causes pronounced changes in the canine myocardial creatine kinase system. These rapid biochemical alterations occur both locally in ischemic tissue and remotely in nonischemic tissue.
Animals↗
CK and LD isozymes in human single muscle fibers in trained athletes.
Individual human muscle fibers from the vastus lateralis were isolated from age-matched endurance-trained and strength-trained athletes and untrained controls. Slow- (ST) and fast-twitch (FT) fibers were assayed for total creatine kinase (CK), CK-MB, total lactate dehydrogenase (LD), the LD isozyme that predominates in the heart muscle of most vertebrates (LD1), and citrate synthase (CS). Regardless of training of the athletes, both CK-MB and CS were higher in ST than in FT fibers. Also, irrespective of fiber type, CK-MB and CS were greatest in the endurance-trained group. A positive correlation existed between CK-MB and CS, relating oxidative capacity of individual fibers with CK-MB. Total CK varied little among the fiber types, trained groups, or controls. Total LD in FT fibers was greater than in ST fibers in all groups, with only ST fibers from the endurance-trained group containing substantial amounts of LD1. These findings suggest that specific training, endurance exercise, causes a favorable metabolic adaptation of CK and LD isozymes at the individual fiber level, allowing for the muscle to cope with increased energy demands during prolonged exercise.
Adult↗
Factitiously high sodium activities on the Ektachem 400 owing to interferences by high gamma-globulin concentrations.
Sera from patients with above-normal gamma-globulin concentrations give sodium values as much as 10% higher when measured in the Kodak Ektachem 400 analyzer than results obtained with the Beckman Astra-8 analyzer. Results obtained with the Astra were in agreement with flame photometry. A similar relative bias was observed for potassium measurement in the Ektachem. This discrepancy was corrected when we used a new generation of reference fluid provided by Kodak, which is currently available for general use.
Adult↗
Diagnostic use of CK-MM and CK-MB isoforms for detecting myocardial infarction.
Following acute myocardial infarction, total CK and CK-MB levels begin to rise 5 to 6 hours after the onset of chest pain. The serial profile of the rise and fall of both activities is nearly always indicative of AMI. The recent increase in the use of thrombolytic agents in an attempt to attain reperfusion of occluded coronary arteries alters the enzyme profiles observed in blood after AMI. After successful reperfusion a washout phenomenon occurs in which early restoration of blood flow to damaged myocardium causes an early rise in total CK and MB levels above the normal range 2 to 4 hours after AMI, with earlier and higher peak enzyme values. Recently reports have appeared describing numerous serum and plasma CK-MM and CK-MB isoform patterns after AMI. Following release from injured myocardium CK-MM3 and CK-MB2 (designated the tissue isoforms) are converted in the circulation to post-translation products (MM2, MM1, MB1, respectively). Studies have now shown that CK-MM isoform patterns provide a unique means of assessing the time of onset of necrosis and a monitor of the duration of enzyme release from the site of injury. Following AMI, MM3, the MM3/MM1 ratio, or both rises and peaks earlier than either total CK or CK-MB levels. During successful reperfusion, the rate of rise of CK-MM3 is more rapid and the MM3/MM1 ratio peaks earlier than without reperfusion. However, any concomitant release of CK-MM3 from skeletal muscle would decrease the clinical utility of MM isoforms in detecting myocardial damage. Recent advances in technology have shown that CK-MB2 rise parallels the CK-MM increase and also rises earlier than total CK and total MB levels and provides increased specificity for the myocardium. The full potential of the diagnostic utility of MM and MB isoforms will not be realized until a reliable, sensitive, simple, and rapid quantitative assay becomes available.
Chemistry Techniques, Analytical↗
Assessment of renal function by inulin clearance: comparison with creatinine clearance as determined by enzymatic methods.
We compared creatinine clearances determined by enzymatic (Kodak Ektachem 700 single-slide, Boehringer Mannheim creatinine PAP) and nonenzymatic (Jaffé, HPLC) methods with glomerular filtration rate measured by inulin clearance in patients with varying degrees of renal function. The Kodak enzymatic assay gave values for creatinine 2 to 3 mg/L higher than the other methods. This resulted in significantly lower creatinine clearances than inulin clearances and creatinine clearances determined by the other methods. However, correlations between all methods for serum and urinary creatinine values and clearances were good. To avoid between assay (enzymatic vs nonenzymatic) discrepancies, manufacturers should agree to an acceptable standard of calibration under the usual conditions used with patients.
Chromatography, High Pressure Liquid↗
Early peak of creatine kinase-MB in acute myocardial infarction with a nondiagnostic electrocardiogram.
This study compared the time from the onset of symptoms to the peak of the creatine kinase-myocardial band (CK-MB) in 34 consecutive patients with acute myocardial infarction. Patients were separated into two groups: group 1 (n = 21) had diagnostic (greater than or equal to 0.1 mV) ST segment elevation on the initial ECG, and group 2 (n = 13) did not have diagnostic ST segment elevation on the initial ECG. In group 1 the time to the peak CK-MB was 16.2 +/- 50 hours vs 10.0 +/- 2.0 hours for group 2 (p = 0.0001). Peak CK-MB was 331 +/- 276 IU/L in group 1 vs 81 +/- 54 IU/L in group 2 (p less than 0.005). In group 1 there were 16 patients who subsequently had a Q wave myocardial infarction as opposed to one patient in group 2 (p = 0.0001). Patients who do not have diagnostic ST segment elevation on the initial ECG have an early but low peak of CK-MB and typically have a non-Q wave infarction. These findings are consistent with early spontaneous restoration of blood flow during the infarction process in these patients. This early restoration of blood flow may provide the substrate for the high incidence of recurrent ischemic events noted in patients with non-Q wave myocardial infarction.
Aged↗
Liver and blood postmortem tricyclic antidepressant concentrations.
Tricyclic antidepressants (TCAs) are one of the major causes of death from drug ingestions. Because TCAs are highly tissue bound, it has been postulated that postmortem tissue release would give rise to elevated blood levels. This study examines the authors' experience with TCAs as a cause of death and the reliability of postmortem liver and blood levels. Postmortem liver and blood TCA levels (parent drug and active metabolite) were quantitated by high-pressure liquid chromatography (HPLC) and gas chromatography mass spectrometry (GC-MS). From 1977 through 1985 the number and percentage of deaths caused by TCA overdoses have remained constant in regard to the total number of deaths caused by poisonings and overdoses: range: 4-17; 5.6-20.2%, respectively. During a six-month period in 1986-1987, nine deaths were caused by six different TCAs. Substantial increases in blood TCA levels were observed as the postmortem interval increased. The mean liver and blood levels were as follows: 232 micrograms/g of tissue (SD, 168) and 6.2 mg/L (SD, 2.4). The liver to blood ratio for the nine cases was 37 (SD, 22):1. In comparison, in cases (n = 4) in which the causes of death were not TCA related but the patients were taking therapeutic doses of TCA, the mean liver and blood levels were 10.8 micrograms/g (SD, 6.0) and 0.26 mg/L (SD, 0.06), respectively. The liver to blood ratio of 39.2 (SD, 17.9): 1 was not different than in the overdose cases. This large tissue to blood gradient in both TCA overdose and therapeutic ingestion cases indicates that postmortem release of tissue-bound TCAs into the blood might falsely show elevated postmortem blood levels that could be indicative of a manner of death even in the nonoverdose, therapeutic ingestion. Thus, only liver TCA levels should be quantitated to specify the manner of death.
Antidepressive Agents, Tricyclic↗
Enzymatic estimation of skeletal muscle damage by analysis of changes in serum creatine kinase.
Skeletal muscle damage size (SMDS) was assessed in 35 women and 34 men runners after a 42.2-km race using a method developed for estimation of myocardial infarct size. SMDS was computed according to the following equation: SMDS = (BW) (K) (CKr), where BW is body weight, K is a constant, and CKr is the cumulative amount of creatine kinase (CK) released over time. The method takes into account CK distribution space, fractional disappearance rate of CK, proportion of CK degraded in skeletal muscle, and proportion of CK released into the circulation. Assumptions are made regarding the relative amount of CK lost from skeletal muscle into the circulation. The SMDS in men, 808 +/- 1,229 (SD) CK g-eq was significantly (P less than 0.05) greater than in women, 160 +/- 147 (SD) CK g-eq. The ranges of SMDS (CK g-eq) were 23-5,397 in men and 7-624 in women. A significant difference (P less than 0.05) also remained after correction for body surface area; men 432 +/- 583 (SD), women 100 +/- 63 (SD) CK g-eq/m2. In men and women, no significant correlation existed between SMDS and age or marathon finish time. Although relatively theoretical, results indicate that greater skeletal muscle damage occurred in men vs. women runners after a marathon. Whether the release of CK from skeletal muscle is the result of irreversible and/or reversible injury has not yet been determined.
Adult↗
Kinetic characterization of human heart and skeletal muscle CK isoenzymes.
The purpose of this study was to investigate the kinetic properties of human creatine kinase (CK) isoenzymes partially purified from heart and skeletal muscle. Utilizing the backward CK-catalyzed reaction of creatine phosphate + ADP in equilibrium creatine + ATP, Km values for heart and skeletal muscle CK MM (3.7 mmol/l) were significantly (p less than 0.05) greater than CK MB (2.1 mmol/l) which were significantly (p less than 0.05) greater than mitochondrial CK (1.8 mmol/l) at variable creatine phosphate and fixed ADP concentrations. However, Km values for similar isoenzymes from the two different tissues, i.e., CK MB from heart vs. skeletal muscle, were not different. These results show that kinetic analysis of CK isoenzymes cannot differentiate the tissue source of elevated blood CK isoenzymes after the acute stress of long distance running or after acute myocardial infarction.
Creatine Kinase↗
Early detection of skeletal muscle injury by assay of creatine kinase MM isoforms in serum after acute exercise.
We could detect skeletal muscle injury early after an acute exercise bout by measuring creatine kinase (CK, EC 2.7.3.2) MM isoforms in serum. Eleven men performed 120 alternating-arm, eccentric (muscle lengthening) biceps contractions with the intensity of each contraction being 110% of maximal concentric strength--a form of exercise previously shown to cause significant increases of CK in serum at 24 h and muscle soreness 48 h after exercise. Total CK and CK-MM isoform activities in serum were determined before and at 0.5, 0.75, 1, 1.5, 2, and 6 h after exercise. Using thin-film agarose gels and a rapid isoelectric focusing technique, we separated the MM isoforms into MM3 (skeletal muscle form), MM2, and MM1 (in vivo conversion forms). The isoforms reflected the MM form released into the serum from tissue as well as the conversion of one form to another. There were no significant increases in total CK from before to 6 h after exercise: 75 (SD 36) vs 91 (SD 33) U/L. However, CK MM3 in serum increased significantly (P less than 0.01) within 2 h after exercise from 22 (SD 6)% to 28 (SD 6)%. The MM3 to MM1 ratio also increased significantly (P less than 0.05) during this time, from 0.6 (SD 0.3) to 0.9 (SD 0.4). Thus, quantification of CK MM isoforms permitted very early detection of skeletal muscle enzyme release.
Creatine Kinase↗