Muscle Collagen Content Research Articles

Effects of ovariectomy on mechanical properties and collagen content in rabbit lower urinary tract smooth muscle.

Fourteen female rabbits underwent ovariectomy or were sham-operated six weeks before investigation. Detrusor and urethral strips (longitudinal and circular urethral muscle fibers were studied separately) were prepared and length-tension relations studied in organ baths experiments. In addition, the specimens were examined for collagen content. Maximal active tension in the detrusor, longitudinal and circular urethral preparations, determined as the response to K+ (124mM), was reached when the length of the strips was 178 +/- 8% (n = 7), 153 +/- 9% (n = 5), and 127 +/- 5% (n = 7) of the resting length, respectively. Ovariectomy did not alter the length for development of maximal active tension. In detrusor strips, ovariectomy caused a significant increase in maximal active tension from 39 +/- 7 mN (sham-operated rabbits) to 79 +/- 11 mN (p < 0.01), despite an unchanged relative amount of smooth muscle. The maximal active tension produced in the urethra was lower (15-25 mN) than in the detrusor, and not significantly affected by ovariectomy. Approximately 40% of the dry defatted tissue weight of the detrusor consisted of collagen, whereas corresponding value in the urethra was 50-60%. Ovariectomy had no effect on tissue collagen concentrations. In conclusion, ovariectomy for six weeks did not affect the passive mechanical properties or the collagen concentration in rabbit lower urinary tract smooth muscle, but increased the responsiveness of the detrusor muscle to K+ (124 mM).

Regenerative capacity of mdx mouse muscles after repeated applications of myo-necrotic bupivacaine.

We injected bupivacaine (BPVC), which produces muscle fiber necrosis, repeatedly into the soleus muscles of mdx mice, which represent a model of human Duchenne muscular dystrophy, over a 12-month period. Cytological and morphometric analysis revealed that the regenerative capacity of repeatedly BPVC-injected mdx muscles was almost equal to that of the saline-injected mdx muscles. At 9 months of age the endomysial collagen content of mdx muscles was 4.6 times that of control mice muscles, and was 7.2 times that of control mice muscle at 12 months. These results suggest that the regenerative capacity of the mdx muscle is quite large and that myo-necrosis induced by an extrinsic cause, such as BPVC, may not be an important factor in the disease progress. However, endomysial collagen, for which the mechanism of increase may be related to the defect of dystrophin, may play an important role in gradual decline of regeneration.

Interstitial space and collagen alterations of the developing rat diaphragm

The effect of growth on the relative interstitial space [%total cross-sectional area (CSA)] and collagen content of the rat diaphragm muscle was examined at postnatal ages of 0, 7, 14, and 21 days as well as in adult males. The proportion of interstitial space relative to total muscle CSA was determined by computerized image analysis of lectin-stained cross sections of diaphragm muscle. To assess collagen content and extent of collagen maturation (i.e., cross-linking), high-pressure liquid chromatography analysis was used to measure hydroxyproline concentration and the nonreducible collagen cross-link hydroxylysylpyridinoline (HP), respectively. At birth, interstitial space accounted for approximately 47% of total diaphragm muscle CSA. During postnatal growth, the relative contribution of interstitial space decreased such that by adulthood the interstitial space accounted for approximately 18% of total muscle CSA. The change in relative interstitial space occurred without a concomitant change in hydroxyproline concentration. However, the concentration of HP markedly increased with age such that the adult diaphragm contained approximately 17 times more HP than at birth. These results indicate that during development the relative CSA occupied by interstitial space decreases as muscle fiber size increases. However, the reduction in relative interstitial space is not associated with a change in collagen concentration. Thus collagen density in the interstitial space may increase with age. It is possible that the observed changes in relative interstitial space and collagen influence the passive length-force properties of the diaphragm.

An anomaly in the effect of temperature on collagen fluorescence in beef

Although the collagen content of beef semimembranosus muscle was predictable ( r = 0·93) with a fibre-optic fluorimetry probe at 5°C, this was not possible at <0°C. Contrary to the normal inverse relationship between temperature and fluorescence, probe signals were weaker at the lower temperature: relative to samples at 5°C, those at <0°C had fewer (53%, p≤0·01) fluorescence peaks above a cut-off for noise and the peaks were less intense (64%, p≤0·01). To investigate the cause of this problem, the fluorescence of bovine tendon collagen was measured by fibre-optics and found to be inversely proportional to temperature ( r = −0·95, p≤0·001) over a wide range from −5 to 40°C, as expected. However, an anomaly was found over a narrow range from 0 to 5°C in samples with ascending temperatures. As samples were thawed and warmed, their fluorescence increased with temperature ( p≤0·001) from 470 to 510 nm. The anomaly may have been caused by changes in light scattering associated with the melting of ice crystals in the tissue. Thus, to use a fibre-optic probe to identify beef carcasses that are likely to produce tough meat because of a high collagen content, it will be necessary either to standardise or correct for the effects of temperature, and to avoid measurements on frozen meat that has just been thawed.

Toughness and Collagen Content of Abalone Muscles.

Toughness and collagen content were measured for various muscle parts of the Japanese abalone, kuro-awabi (Haliotis discus), in relation to muscle structures. The dorsal surface of the foot was toughest, followed by the hard and soft part of the foot, then the upper and middle part of the adductor muscle, irrespective of being reared or wild specimens. When compared with other abalone species, kuro-awabi showed the highest toughness for all the muscle parts, followed by madaka (H. sieboldii) and megai-awabi (H. gigas), while ezo-awabi (H. discus hannai) was softest. Collagen content was parallel with muscle toughness: the higher the collagen content, the tougher the muscle. Light micrographs of kuro-awabi showed that foot and the dorsal surface of foot were dominated by connective tissues, while adductor muscle was mainly composed of myofibrils. Transmission electron micrographs demonstrated that myofibrils in the foot were surrounded by thick layers of collagen fibrils of about 1 μm, confirming light microscopic observations.

DETERMINATION OF COLLAGEN CROSSLINKS IN ROCKFISH SKELETAL MUSCLE

The low collagen content in fish muscle makes the quantitative analysis of collagen crosslinks difficult. We have developed a method for the quantitative determination of reducible difunctional collagen crosslinks in samples containing as little as 0.5 picomoles of crosslink per microgram of hydroxyproline. The low collagen-containing tissue is first enriched by removing most of the non-collagenous protein with cold sodium hydroxide solution. The lyophilized alkali-insoluble extract is then reduced with NaB3H4 and acid-hydrolyzed. Initial fractionation of hydrolysates on a Bio-Gel P-2 gel filtration column provides partial separation of components with a sharp peak of radioactivity containing more than 90% of the difunctional crosslinks. This peak is ultimately analyzed by HPLC for the quantitative determination of specific difunctional crosslinks. This method has been used to show that the difunctional crosslink composition of muscle collagen from two species of Pacific rockfish differs quantitatively from each other and from that of rat tail tendon.

Muscle composition of steers treated with the β-agonist, cimaterol

The effect of the β-adrenergic agonist, cimaterol, on the nature and amount of collagen in three individual muscles ( Longissimus dorsi, Vastus lateralis and Semitendinosus) from young steers was investigated. β-Agonist-treated animals showed similar rates of liveweight gain to those of control animals but the weight and protein content of the Longissimus dorsi and Vastus lateralis muscles were significantly increased (muscle weights 1216 versus 1494 g, P < 0·05; 514 versus 642 g, P < 0·01, respectively, for control and cimaterol animals). The Semitendinosus muscle, however, showed no significant increase in weight or protein content ( P > 0·05). The total collagen content and the proportion of heat-soluble collagen varied considerably between muscles, but no significant muscle × treatment interactions were detected ( P > 0·05). Cimaterol treatment reduced total muscle collagen content (controls 15·2, cimaterol 12·5mg/g fresh tissue, P < 0·05) and also reduced the percentage of heat-soluble collagen (controls 18·9%, cimaterol 13·0%, P < 0·05).

Content and partial characterization of collagen in crustacean muscle

1. 1. The collagen content in the abdominal muscle of seven species including shrimp, prawn, lobster and squilla varied among the species ranging from 1.1 to 6.2% of total tissue protein and the content in pereiopod and thoracic muscles of four species of crab varied ranging from 0.2 to 0.8%. 2. 2. These results indicate that the musculature in flexible part comprises a high proportion of collagen. 3. 3. The major collagen from the crustacean muscle was found to be similar to Type V collagen from the vertebrate muscle with respect to the solubility and amino acid composition.

Protein and collagen content of rat skeletal muscle following space flight.

Biochemical determinations of non-collagenous protein and hydroxyproline were made on rat skeletal muscles following 7 days of space flight aboard the NASA space shuttle mission SL-3. Relative to ground-based controls, the wet weight of each experimental muscle was significantly reduced. This was concomitant with a reduction in non-collagenous protein in the muscles. Protein concentration, however, was reduced only in slow-twitch muscles. The effect of space flight on the concentration and hydroxyproline content was different among the muscles. As a result, the loss of muscle mass in some muscles was the consequence of a reduction in both collagenous and non-collagenous proteins, while in others it was primarily the result of a non-collagenous protein loss.

Relation between muscular development and muscle collagen content in pigs

The relationship between muscle collagen content and muscular development was investigated in the pig using eight Large Whites, eight halothane-negative (HN) and eight halothane-positive (HP) Pietrain pigs. Three muscles varying in the degree of hypertrophy in Pietrain pigs as compared to Large White pigs were studied. Pietrain pigs had higher loin and ham percentages, as well as higher muscle to bone ratio in the ham than Large White pigs. A trend to lower collagen contents in Pietrain pigs as compared to Large White pigs was observed in biceps femoris and longissimus dorsi muscles, although the differences were not significant. On the whole, there does not seem to be any clear relationship between muscle collagen content and muscular development in the porcine species.

Collagen metabolism of mouse skeletal muscle during the repair of exercise injuries.

The activities of prolyl 4-hydroxylase and beta-glucuronidase, the concentration of hydroxyproline as well as reticulin and collagen type III, IV and V stainings were followed in skeletal muscle during a 20-day period after a 9-h treadmill running in untrained and trained male mice, aged 4-6 months. The prolonged 9-h running of untrained mice temporarily increased prolyl 4-hydroxylase activity 2, 5 and 10 days after exercise, more prominently in the red than in the white part of quadriceps femoris-muscle, and in analogical manner as beta-glucuronidase activity in tibialis anterior-muscle. Twenty days after exercise these enzymatic activities were back to the control level. The hydroxyproline content of red muscle was increased for 10 and that of white muscle for 20 days after the exertion. Training for 45 days did not affect hydroxyproline content and prolyl 4-hydroxylase activity was at the control level after the training. A 9-h exercise increased prolyl 4-hydroxylase activity much less in trained muscle than in the untrained muscle and did not affect muscle collagen content. Histological observations showed fiber necrosis 2 days and signs of fiber regeneration 5 days after the exertion in untrained mice. Twenty days afterwards the regeneration was nearly completed. Reticulin staining was increased in injured muscle areas 10-20 days after the exertion. In immunohistochemical staining, antibodies to all studied collagen types (type III, IV and V) showed increased staining 5-20 days after the exertion in the areas of muscle injuries and regeneration.(ABSTRACT TRUNCATED AT 250 WORDS)

Collagen content of muscles from boars of the Pietrain breed

Collagen content of muscles from boars of the Pietrain breed

The influence of age, sex and breed of cattle on their muscle characteristics

In order to gain more knowledge of the systematic changes occurring in meat tenderness and colour of different breeds and sexes of growing cattle, a number of characteristics were studied in five different muscles of Afrikaner and Friesland bulls and steers between birth and 24 months of age. Muscle collagen content of bulls was higher at birth than at all other ages and solubility of collagen decreased markedly between birth and 16 months of age. Shear force increased between 8 and 16 months, partially coinciding with the decrease in collagen solubility. Collagen content of muscles was higher in bulls than in steers and solubility decreased markedly between 12 and 16 months, only in the case of bulls. Afrikaner muscles were more tender than those of Frieslands and had a higher content and solubility of collagen. Pigment content was higher in Afrikaner than in Friesland muscles and increased steadily with age in all animals. The results show that the biological differences found to influence muscle characteristics were particularly those of age and breed of animal.

Turnover of muscle protein in the fowl Collagen content and turnover in cardiac and skeletal muscles of the adult fowl and the changes during stretch-induced growth

Turnover of muscle protein in the fowl Collagen content and turnover in cardiac and skeletal muscles of the adult fowl and the changes during stretch-induced growth

Turnover of muscle protein in the fowl. Collagen content and turnover in cardiac and skeletal muscles of the adult fowl and the changes during stretch-induced growth.

The collagen content and the rate of collagen synthesis were measured in the anterior and posterior latissimus dorsi muscles and in heart from fully grown fowl. This was done by measuring the proline/hydroxyproline ratios in the muscle and by a constant infusion of [(14)C]proline. These measurements were also made during the hypertrophy of the anterior muscle in response to the attachment of a weight to one wing of the fowl. In the non-growing muscles the collagen content was higher in the anterior muscle (22.8% of total protein) than in the posterior muscle (9.5% of total protein) and lowest in the heart (3.8% of total protein). In the two skeletal muscles a little over half of the collagen was accounted for by internal collagen (i.e. perimysium and endomysium). Collagen synthesis in these non-growing muscles occurred at 0.59%/day in each of the two skeletal muscles and at 0.88%/day in the cardiac muscle. During hypertrophy the collagen content of the anterior muscle increased, but not as fast as intracellular protein, so that after 58 days the concentration had fallen from 22.8 to 14.4% of total protein. This may have resulted from an incomplete production of the epimysial sheath, since the concentration of internal collagen did not fall and as a result accounted for over 80% of the total in the enlarged muscle. Collagen synthesis increased 8-fold during the first week of the hypertrophy, but never amounted to more than 4% of the total muscle protein synthesis. When the net accumulation of collagen is compared with the increased rate of synthesis it is concluded that between 30 and 70% of the newly synthesized collagen may have been degraded.

Carcass and meat quality of Friesian steers fed on either pasture or barley

Friesian steers were slaughtered as individual animals reached a fasted liveweight of c. 457 kg, after being on either a predominantly cereal diet (12 animals) or a predominantly pasture diet (13 animals) for at least 160 days. Those on the cereal diet grew 31% faster than the animals on pasture so that the latter group was an average of 69 days older. The carcasses of the cereal group were significantly fatter especially with regard to omental fat (+ 54%), intramuscular fat (+ 34% for M. semitendinosus) and dissectable fat from the 9–10–11 rib cut (+ 27%). These differences in composition may have been caused by either differences in growth rate or specific dietary effects. Measurements of tenderness all favoured the cereal group, the largest effect being on cold-shortened M. semitendinosus where the mean shear value was 50% greater for the pasture group. The greater age, lower percentage of intramuscular fat and greater susceptibility to cold-shortening may all be involved in these differences. The groups did not differ in ultimate muscle pH, muscle collagen content or adrenal cortical activity. A laboratory taste panel consisting of 15 members indicated that the flavour of topside roasts from the animals fed on the cereal was more acceptable.

LITERATURE ABSTRACTS

1. General Principles: Maturation of Meat, Post Mortem Development of Tenderness and Biochemical Changes in Myofibrillar Proteins’, by C. Valin and A. Pinkas1. General Principles: Flow Behavior, Surface Tension and Density of Pectin‐Sucrose Solutions’, by S. I. Jankov, K. M. Kolarov, and G. I. Popov1. General Principles: ‘Investigation of the Rheological Properties of Gluten. III. Role of Hydrophobic Bonds in the Rheological Properties of Gluten’, by R. Lasztity1. General Principles: ‘Viscoelastic Behavior of Rough Rice’, by A. Husain, K. K. Agrawal, T. P. Ojha, and N. G. Bhole1. General Principles: ‘Wheat Proteins (A Review)’, by D. G. Redman1. General Principles: ‘Proposed Techniques for Axial Compression Tests on Intact Agricultural Products of Convex Shape’, by P. C. Arnold and N. N. Mohsenin1. General Principles: ‘Response of Papaya Fruit to Dynamic Loading’, by L. Kumar and J. K. Wang1. General Principles: ‘To What Extent is the Quality Grading for Gouda, Jarlsberg and Small Swiss Cheese Dependent on Texture and Consistency Properties?’, by K. Steinsholt1. General Principles: ‘Rheological Characteristics of Mayonnaise’, by N. I. Kozin and B. Kh. Darchiev1. General Principles: ‘Capillary Viscometry of Macaroni Dough’, by N. I. Nazarov, B. M. Azarov, and M. A. Chaplin1. General Principles: ‘Comparison of Static Creep and Relaxation, Rate Sensitive, and Frequency Sensitive Loading for Axial Compression’, by J. R. Hammerle, M. V. N. Rao and D. D. Hamann2. Instrumentation and Methodology: ‘Determination of Rheological Properties of Liquid Foods, I. Thickening Agents’, by A. Escardino, P. Fito and A. Molina2. Instrumentation and Methodology: ‘New Results of Rheological Test Methods on Dough’, by C. W. Brabender and W. Schafer2. Instrumentation and Methodology: ‘Measurement of Curd Syneresis’, by E. Kiss2. Instrumentation and Methodology: ‘The Reliability and Suitability of Consistency Measurements for Judging the Quality of Cooked Sausages’, by J. J. Laine and A. M. Ullstedt2. Instrumentation and Methodology: ‘Instrument for Determining Rheological Properties of Butter at Tropical Temperatures’, by S. S. Chari and B. R. Awasthy2. Instrumentation and Methodology: ‘Texture Measurement of Canned Red Pimentos. Development of a New Device for Use With the Kramer Shear Press’, by L. Duran, C. Calvo and A. M. Bermell2. Instrumentation and Methodology: ‘Viscosity of Chocolate ‐ Determination of Casson Yield Value and Casson Plastic Viscosity’, by Office International du Cacao et du Chocolat2. Instrumentation and Methodology: ‘A Study of the Murbimeter’, by J. de Becker2. Instrumentation and Methodology: ‘Rotating Dull Knife Tenderometer’, by P. C. Anderson, J. L. C. Rapp and D. F. Costello3. Objective Measurements: ‘Application of the Brookfield Viscometer for Measuring the Apparent Viscosity of Acidulated Flour‐Water Suspensions’, by J. S. Kitterman and G. L. Rubenthaler3. Objective Measurements: ‘Objective Assessment of Curd Firmness’, by U. Behnke and E. Schalinatus3. Objective Measurements: ‘Reologie von Roggenteigen. I. Über die Möglichkeiten der Viskositätsmessungen an Roggenteigen’, by D. Weipert4. Factors Affecting Texture: ‘Effect of D‐Tubocurarine Chloride and Compound 48/80 on Muscle Tenderness’, by P. E. McClain and A. M. Mullin4. Factors Affecting Texture: ‘Effects of Age and Sex on Quality, Tenderness and Collagen Content of Bovine Longissimus Muscle’, by R. E. Hunsley, R. L. Vetter, E. A. Kline and W. Burroughs4. Factors Affecting Texture: ‘Effect of Break Temperature and Holding Time on Pectin and Pectic Enzymes in Tomato Pulp’, by B. S. Luh and H. N. Daoud4. Factors Affecting Texture: ‘Influence of Hydrothermal Treatment on Mechanical Properties of Buckwheat’, by T. V. Lokteva and E. M. Mel’nikov4. Factors Affecting Texture: ‘The Influence of Canning and Precanning Treatments on Firmness of Canned Sweet Potatoes’, Thesis by F. K. Abdulle4. Factors Affecting Texture: ‘Studies on Uptake of Calcium Salts During Pretreatment of Peaches for Freezing’, by A. Polesello and E. Maltini4. Factors Affecting Texture: ‘Histological and Histochemical Studies of Sweet Corn (Zea mays L.) Pericarp as Influenced by Maturity and Processing’, by T. Khalil and A. Kramer4. Factors Affecting Texture: ‘Fresh Peas. Relationships Between Percentage of Principal Chemical Components, Tenderness and Water Content’, by R. Cousin, G. Lefevre, J. Arnoux, G. Hiroux, and V. Boulaine4. Factors Affecting Texture: Special Causes of Improved Ice Cream Consistency’, by P. Geiger4. Factors Affecting Texture: ‘Study on Ultrasonic Vibrations in Their Action of Tenderizing Meat’, by J. F. Zayas, V. I. Solov’ev, T. M. Mittel’stein, T. N. Orlova, and B. V. Garian4. Factors Affecting Texture: ‘Production of Tender Beef (A Review)’, by R. L. Joseph4. Factors Affecting Texture: ‘Pattern of Firmness Within a Bread Loaf’, by A. L. Short and E. A. Roberts4. Factors Affecting Texture: ‘Properties of Glutens from Doughs Containing Components of Cheddar‐Cheese Whey’, by Mary V. Zaehringer

Effects of Age and Sex on Quality, Tenderness and Collagen Content of Bovine Longissimus Muscle

Effects of Age and Sex on Quality, Tenderness and Collagen Content of Bovine Longissimus Muscle

Differentiation of red and white fibers in muscle from fetal, neonatal and infant rhesus monkeys.

The hydroxyproline (collagen) content of muscle in terms of wet weight was lowest at 90 days gestational age (rhesus monkey) and increased until birth. Histologic techniques also demonstrated a progressive increase in staining density for connective tissue with increasing fetal age. However, when expressed in terms of nitrogen content of muscle, the hydroxyproline concentrations were similar from the 90-day fetal through the 2-6-week infant series, and were consistently higher in rapidly growing as compared to adult muscle. The succinic dehydrogenase activity (soleus), on the basis of wet weight or of nitrogen, was lowest in the 90-day fetal series and reached a plateau by 120 days. The histochemical data indicated an increase in staining density for succinic dehydrogenase in muscle as the fetus matured. By 90 days gestational age, the hydroxyproline concentration of red muscle was lower as compared to that of white muscle, and this difference was also apparent histologically. The succinic dehydrogenase activity was higher in red as compared to white muscle at all ages, and histochemical differentiation was apparent at 120 days fetal age.

Effect of Estrogen and Progesterone on Collagen Content of Rat Uterus, Heart and Skeletal Muscle

ArticleEffect of Estrogen and Progesterone on Collagen Content of Rat Uterus, Heart and Skeletal MuscleLucille S. Hurley, and Heinz HerrmannLucille S. HurleyFrom the Division of Chemical Embryology, Department of Pediatrics, University of Colorado Medical School, Denver, Colorado, and Heinz HerrmannFrom the Division of Chemical Embryology, Department of Pediatrics, University of Colorado Medical School, Denver, ColoradoPublished Online:30 Sep 1955https://doi.org/10.1152/ajplegacy.1955.183.1.67MoreSectionsPDF (727 KB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformationCited ByDer Einflu� von Sexualsteroiden auf die isometrische Kontraktion des isolierten RattenzwerchfellsArchiv f�r Gyn�kologie, Vol. 225, No. 2Über das Verhalten klinisch-chemischer Serumbestandteile bei Traberstuten während der Hochträchtigkeit und in der frühen Laktation.Reproduction in Domestic Animals, Vol. 10, No. 2Accumulation of collagen in the uterus of the immature rat administered estradiol-17βBiochemical Pharmacology, Vol. 22, No. 1Wirkungen der Gestagene auf den StoffwechselSonstige Wirkungen von GestagenenThe Physiology of the Connective Tissues of the Reroductive TractBIOLOGICAL FUNCTIONS OF COLLAGENBiological Reviews, Vol. 36, No. 4Wound HealingNew England Journal of Medicine, Vol. 259, No. 6 More from this issue > Volume 183Issue 1September 1955Pages 67-70 Copyright & PermissionsCopyright © 1955 by American Physiological Societyhttps://doi.org/10.1152/ajplegacy.1955.183.1.67PubMed13268637History Received 12 July 1955 Published online 30 September 1955 Published in print 30 September 1955 Metrics