Gene/Protein Disease Symptom Drug Enzyme Compound
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 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Crosslinking of collagenous biomaterials currently employs the use of glutaraldehyde. The putative enhancement of glutaraldehyde crosslinking by lysine was investigated in three model systems: bovine pericardium, collagen membranes, and bovine serum albumin. Repetitive sequential treatment of bovine pericardium with glutaraldehyde and lysine and finally with formaldehyde produced a matrix which, by the two criteria used (shrinkage temperature and urea/SDS soluble collagen), was shown to be more highly crosslinked than pericardium fixed in glutaraldehyde alone. Essentially the same results were obtained when membranes prepared from pepsin-soluble pericardial collagen were subjected to sequential glutaraldehyde and lysine treatments, reaching shrinkage temperatures of more than 90 degrees C. Heart valves prepared from lysine-enhanced glutaraldehyde crosslinked bovine pericardium were tested in vitro in an accelerated fatigue tester and have been shown to behave satisfactorily after 300 million cycles. These additional crosslinks proved to be stable in saline at 37 degrees C. Studies on bovine serum albumin attempted to get an insight into the mechanisms of lysine enhancement of glutaraldehyde crosslinking by treating sequentially albumin with glutaraldehyde and lysine and analysis of the products by gel filtration and SDS-PAGE. These studies suggest that free amino groups exposed by proteins are initially reacted with glutaraldehyde and then bridged by the diamino compound (lysine) producing more extensive intermolecular crosslinking than glutaraldehyde alone.
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PMID:Lysine-enhanced glutaraldehyde crosslinking of collagenous biomaterials. 179 97

Isomyosin analyses by biochemical, immunochemical, and histochemical investigations have been carried out in five sheep following unilateral recurrent laryngeal nerve paralysis and direct functional electrostimulation of the denervated cricoarytenoid posterior muscle. Myosin light chains were identified by two-dimensional gel electrophoresis. Myosin heavy chains were analyzed by one-dimensional SDS-polyacrylamide gel electrophoresis. Slow myosin heavy chain was identified by orthogonal peptide mapping and immunochemistry. The stimulation effect at cellular level was determined using adenosine triphosphatase (ATPase) histochemistry. A dramatic increase of the type 1 fiber area (slow, fatigue-resistant fibers) could be seen after many weeks of an increasing regime of low-frequency direct electrical stimulation. Biochemically, the amount of slow myosin was always higher than in normal muscles. Some muscles were transformed almost completely to the slow type. At the time they were studied and with the methods employed, the expression of embryonic isomyosin was not observed. In conclusion, after numerous weeks of maintained functional activity, elicited by direct electrostimulation, the denervated muscle regionally showed areas of hypertrophy or at least lack of atrophy of slow myofibers without major signs of muscle damage.
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PMID:Isomyosin changes after functional electrostimulation of denervated sheep muscle. 297 27

1. The effects of variations in pH between 7.00 and 6.20 on Ca2+ -activated tension development and maximum velocity of shortening (Vmax) were examined in skinned single skeletal fibres from rat slow-twitch soleus and fast-twitch superficial (s.v.l.) and deep (d.v.l.) regions of the vastus lateralis muscle. 2. At pH 6.50, Vmax was depressed to a similar degree in each of the soleus, d.v.l., and s.v.l. fibres. Lowering pH to 6.20 resulted in a further decline in Vmax in all fibres; however, differences between the slow fibres, identified by SDS-polyacrylamide gel electrophoresis, and fast fibres were apparent, with soleus retaining a significantly greater proportion of its control Vmax (0.83 +/- 0.03 in soleus vs. 0.69 +/- 0.03 in s.v.l.; mean +/- S.E.M.). 3. Maximum force production decreased significantly as pH was reduced. Peak force at pH 6.50, relative to that at pH 7.00, was significantly greater in soleus (0.80 +/- 0.01) than in the s.v.l. (0.75 +/- 0.01) fibres. At pH 6.20 these differences between slow and fast fibres were still greater, in that soleus fibres generated significantly greater relative forces (0.73 +/- 0.01) than did d.v.l. (0.67 +/- 0.02) or s.v.l. (0.63 +/- 0.02) fibres. 4. As pH was lowered the tension-pCa relationship shifted to the right (i.e. to higher [Ca2+]), indicating a reduction in the Ca2+ sensitivity of tension development. The [Ca2+] necessary to achieve half-maximal tension in both the slow- and fast-twitch fibres increased approximately 5-fold when pH was lowered from 7.00 to 6.20. Furthermore, in the case of the soleus, the Ca2+ threshold for tension development was 45 times greater at pH 6.20 than at pH 7.00, while in the fast-twitch fibres, this increase was 4-fold. 5. Increased [H+] differentially affected the steepness of the tension-pCa relationship between slow and fast fibres. As pH was lowered, the steepness of the lower portion of the tension-pCa curve increased in the soleus and decreased in d.v.l. and s.v.l., suggesting that apparent positive co-operativity of tension development had increased in soleus and decreased in d.v.l. and s.v.l. fibres. 6. These results (1) demonstrate an increased resistance to H+ ion-mediated contractile dysfunction in slow- compared to fast-twitch single fibres, and (2) support the hypothesis that muscular fatigue resulting from short-term, intense muscular contraction may in part be related to elevated H+ ion concentration.
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PMID:Greater hydrogen ion-induced depression of tension and velocity in skinned single fibres of rat fast than slow muscles. 344 9

Ten patients aged 5-14 years and 1 adolescent were treated by CAPD during 12 patient years. Overall survival and rehabilitation were good despite relatively high serum concentrations of urea (19 mmol/l) and creatinine (735 mumol/l). Dietary restrictions were only occasionally necessary, 6 patients required phosphate binders. No radiological bone changes developed in 4 patients with initially normal x-rays, but lesions progressed in 3 with pre-existing osteodystrophy despite administration of 1.25 (OH) 2D3 and Al-hydroxide. Statural growth was unsatisfactory: Height decreased in the 7 patients observed over 1 year from -2.4 to -2.7 SDS. Peritoneal diffusion curves varied considerably between patients, yet remained unchanged at repeat examination. Parents fatigue developed in 6 families and was partly responsible for peritonitis. The incidence of peritonitis fell from 1 episode in 3.3 months to 1 in 8 months. Intensive family support by regular telephone contact and home visits appeared as the most important measure in prevention of parents fatigue and hence of peritonitis. We consider CAPD as a valuable alternative method to haemodialysis.
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PMID:[5 years of continuous ambulatory peritoneal dialysis in the child]. 395 93

Normal and dystrophic mouse muscles were separated into a predominantly white muscle fraction (gastrocnemius, extensor digitorum longus) and a predominantly red muscle fraction (diaphragm). Acetylcholinesterase (AChE) was extracted from each muscle fraction using a Triton X-100/NaCl buffer. Six forms of AChE were separated from each muscle homogenate by velocity sedimentation on linear sucrose gradients. Their apparent sedimentation coefficients in each case were 19.7S, 16.0S, 13.3S, 10.4S, 7.6S, and 3.9S. Gel electrophoresis of crude muscle homogenates under nondenaturing conditions (native gels) and of ech separate isozyme fraction gave one band of AChE activity with a consistent Rf (relative mobility) value. Reelectrophoresis of native gel bands on SDS/acrylamide slab gels revealed a similar monomeric subunit protein from either crude muscle homogenates or isozyme fractions with an apparent molecular weight of approximately 69,000 daltons. Our results indicate that the AChE distribution and activity are severely affected in dystrophic "white" muscles (anaerobic) but much less so in "red" muscles (aerobic). Dystrophic predominantly white muscles weigh less, contain less protein, and have a decreased total AChE activity in comparison with their normal counterparts. Furthermore, the relative proportions of AChE activity in each isozyme fraction is altered between normal white and dystrophic white muscle fractions: i.e., dystrophic white muscle contains a decreased proportion of a low molecular weight form (7.6S) and increased proportions of higher molecular weight forms (16.0S, 19.7S). In contrast, no significant differences occur in AChE activity or distribution between normal and dystrophic predominantly red muscle. The changes in white muscle AChE are toward a pattern common to red muscle. This suggests that the effect of muscular dystrophy and its related stress on mouse white muscle is at least in part a shift from a predominantly anaerobic, fatigable metabolism to an aerobic, fatigue-resistant metabolism.
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PMID:Altered acetylcholinesterase isozyme patterns in mice with hereditary muscular dystrophy. 724 Oct 63

We investigated the validity and reliability of QOL questionnaire for lung cancer patients in palliative therapy. The questionnaire covered twelve items: appetite, feelings, sleep, mental and physical fatigue, pain, anxiety, daily activity, abdominal and respiratory conditions, linear and face scales. The data were collected from 65 patients and analyzed with principal component analysis and correlation analysis. 1) The percentage of complete answers was 81.5%. 2) Appetite, feelings, sleep, mental fatigue, anxiety and mental scale, pain, respiratory condition, abdominal condition, physical fatigue and physical scale, and satisfied internal consistency. 3) The test-retest reliability was satisfied 4) The inquiry items were grouped into physical, mental and activity scales, and these scales belonged to different dimension. 5) There were correlations between a linear scale, face scale, total score and items. 6) In concurrent validity, there were correlations between performance status and the activity scale, SDS, STAI and the mental scale. 7) In sensitivity, the total score and face score were worst within one week after chemotherapy, and then recovered. This questionnaire was indeed valid and reliable for use as a QOL questionnaire for lung cancer patients in palliative therapy.
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PMID:[Development of quality of life (QOL) questionnaire for use of lung cancer patients in palliative therapy--study of validity and reliability. No.1]. 754 Aug 25

Neurogenic orthostatic hypotension is a severely disabling condition due to deficient peripheral vasoconstrictor tone in response to the upright position and is characterized by a decrease in blood pressure upon standing associated with symptoms of lightheadedness, dizziness, visual "white-out", weakness, lack of energy, near syncope or even syncope. Previous pharmacologic treatment of neurogenic orthostatic hypotension has been problematic. Midodrine, a new specific alpha-1-agonist has been shown to produce arteriolar constriction and decrease in venous pooling via a constriction of venous capacitance vessels. Therefore, a recent multicenter study evaluated the safety and efficacy of midodrine therapy in 97 patients with neurogenic orthostatic hypotension due to various etiologies: Shy Drager syndrome (No. 18); Bradbury Eggleston syndrome (idiopathic orthostatic hypotension) (No. 20); diabetic autonomic neuropathy (No. 27); Parkinson's disease (No. 22); and miscellaneous (No. 10). Following one week of placebo therapy, the patients were randomized into 4 groups for a 4 week period of time; placebo, 2.5 mg, 5 mg, or 10 mg three times daily. The BE/SDS subgroup demonstrated a 27 +/- 8% (22 mmHg) increase in standing systolic blood pressure for the 10 mg dose. Diabetics achieved a significant increase at 5 mg. Similar increases were observed for the entire group on the 10 mg dose (p < 0.001). Symptoms or fainting, blurred vision, improved energy level, standing time, and depressed feelings were also significantly improved even at lower doses (p < 0.05 or less). Side effects were mild. Therefore, midodrine is an effective and safe agent for the treatment of neurogenic orthostatic hypotension.
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PMID:Midodrine in neurogenic orthostatic hypotension. A new treatment. 769 Mar 83

We characterized urinary excretion of C3 fragments among patients with systemic lupus erythematosus (SLE) as a possible indicator of renal involvement. 28 patients, representing a broad range of disease activity were admitted to our study. Urinary proteins were separated on 4-20% gradient SDS-PAGE gels, under reducing conditions, and transblotted to nitrocellulose. Western blots were developed with a polyvalent goat-anti-human C3d antiserum, and an alkaline phosphatase-conjugated rabbit anti-goat IgG. Three patterns were obtained: 1) no bands detected; 2) bands suggesting the presence of intact C3; and 3) samples with additional low molecular (< 4 x 10(4)) bands. The 12 patients with no C3 bands had minimal disease activity (e.g. fatigue, arthralgia, arthritis, rash, oral ulcers). The seven patients with intact C3 patterns also had minimally active disease. Their primary clinical findings included fatigue, pleurisy, renal disease which had been treated, hemolytic anemia, and arthritis. Patients with low molecular weight C3 fragments in their urine formed two sub-sets, based upon their presenting features. The first group had severe disease and contained all patients with active lupus nephritis (n = 4), while the second consisted of non-renal patients with primary clinical findings of moderate disease activity (e.g. thrombocytopenia, pneumonitis, arthritis). Our results suggest urinary excretion of low molecular weight C3 fragments correlates with active renal disease, but is a variable finding among SLE patients with non-renal manifestations of disease activity.
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PMID:Complement C3 fragments in urine: detection in systemic lupus erythematosus patients by western blotting. 819 18

Congestive heart failure is often associated with skeletal muscle abnormalities that contribute to early fatigue and acidosis. Up to the present time, however, the mechanisms responsible for these changes are unclear. Myocardial infarctions were produced by coronary ligation in adult Sprague-Dawley rats. At 20 weeks, 10 control rats, and 15 animals with heart failure [defined by elevated LVEDP (26.1 +/- 3.1 v 2.5 +/- 0.5 mmHg) and RV hypertrophy (300 +/- 21 g v 158 +/- 9 mg)] underwent in vivo measurements of total body, and soleus total protein and myosin heavy chain (MHC) synthesis by [3H]leucine constant infusion. Soleus muscle was also analysed for protein content, and MHC isoenzyme content by SDS-PAGE. Northern blotting also was used to determine levels of the mRNA's encoding type I, IIa, IIb, and IIx MHC, alpha-skeletal actin, COX III, SDH and GAPDH. Soleus muscles in heart failure rats were smaller than controls (112 +/- 6 v 126 +/- 5 mg) and the degree of atrophy was significant when corrected for body mass (0.38 +/- 0.02 v 0.46 +/- 0.02 mg/g. P = 0.007). Although there was no significant difference in plasma leucine flux (an index of whole-body protein synthesis), soleus muscle total and MHC synthesis was reduced in heart failure animals. Whereas the Type I MHC isoenzyme (beta MHC) was the only MHC detected in the soleus of control animals, type II MHC isoenzyme comprised 11.8 +/- 3.1% of the MHC in the heart failure group. Furthermore, steady-state mRNA levels encoding beta MHC were significantly depressed in the heart failure rats, where those encoding Types IIb and IIx MHC were increased. Steady-state mRNA levels of alpha-skeletal actin, cytochrome C oxidase (COX III) and succinate dehydrogenase (SDH) were also significantly depressed. This animal model of chronic heart failure is associated with quantitative and qualitative alterations in skeletal muscle gene expression that are similar to those reported in skeletal muscle of patients with chronic heart failure. The altered phenotype and impaired metabolic capacity may contribute to exercise intolerance in CHF.
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PMID:Alterations in skeletal muscle gene expression in the rat with chronic congestive heart failure. 887 78

The extensor carpi radialis muscle of the horse is deceptive at first appearance. It has a fusiform shape similar to other forearm extensor muscles. The fiber arrangement also appears long and relatively parallel. However, it may contain two or more compartments that correlate with differing functional roles. Histochemical and immunocytochemical analysis of proximal and distal regions of the muscle (n = 9) demonstrate that the proximal portion of the muscle is composed of a mean of 13% type I, presumed slow twitch, and 61% type IIb, presumed fast twitch fibers. In contrast, the distal compartment is composed of a mean of about 43% type I and only 22% type IIB fibers. The type I and IIa fibers are all highly aerobic based on nicotinamide dinucleotide tetrazolium reductase reactions. Correlative data regarding the myosin isoforms has been obtained with 4% SDS-PAGE analysis of myosin heavy chain isoforms which demonstrate isoforms migrating at rates similar to rat type I, IIa, and IIx. The latter has been referred to as type IIB/X in a study of the horse's gluteus medius muscle. We propose that the in-series 'compartmentalization' of the muscle, while not conforming strictly to the definitions of neuromuscular compartments, relates to the insertion of the lacertus fibrosus, a distal slip of the biceps brachii, upon the extensor carpi radialis. Earlier studies demonstrated a high proportion of type I fibers in the equine lateral biceps brachii which were thought to stabilize the shoulder during long periods of quiet standing. Because of action imposed on the distal compartment by the biceps brachii, slow and fatigue-resistant functions are part of the limb's passive stay apparatus to effect long-term standing by the horse. Thus, the fatigue-resistant compartments of biceps brachii and extensor carpi radialis may constitute an in-series arrangement of the two muscles. The proximal compartment is suited to provide powerful, more fatigable contractions during locomotion and likely affects stress or strain within the distal postural compartment.
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PMID:Architecture and the division of labor in the extensor carpi radialis muscle of horses. 957 63


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