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A Rowlerson

Publications and source records attributed to A Rowlerson.

35 records · Page 2Linked to original sources
PubMed1987

Rat muscle during post-natal development: evidence in favour of no interconversion between fast- and slow-twitch fibres.

1. It was confirmed that in the fourth deep lumbrical muscle of the rat the number of muscle fibres at birth is about half that in the adult. 2. The average number of slow-myosin-containing (S) fibres (as determined by specific antibody binding) remains constant from birth to adulthood. Therefore it is likely that all the muscle fibres generated post-natally are type F (i.e. slow-myosin-free). 3. A comparison in the electron microscope between transverse mid-belly sections from new-born (day 0) and 4 day muscles showed many muscle fibres or myotubes to be intimately associated with other fibres and cells of other types in the new-born, but to be much less closely grouped at 4 days. 4. A full cell count was obtained from electron microscopy of a mid-belly section of a lumbrical muscle at birth. 5. Cross-sectional area measurements in the light microscope at 3-5 days and in the adult showed that at 3-5 days on average the S fibres have a greater cross-sectional area than the F fibres. This is reversed in the adult where the S fibres are the smaller. At 3-5 days the range of cross-sectional areas of F fibres is much wider than for S fibres. Some F fibres are among the largest fibres in the muscle. 6. It is argued from the data that the motor units of adult muscle, which are homogeneous with respect to muscle-fibre types, are produced by selective withdrawal of neonatal motor-unit contacts during developmental synapse elimination.

Animals↗
PubMed1987

Muscle fibre types in the external eye muscles of the pigeon, Columba livia.

Fibre typing with antisera raised against specific myosin types from muscles of known physiological properties were used to characterise the fibre types within the oculorotatory muscles of pigeons. Fibres reacting strongly to antiserum anti-ALD (specific for tonic fibre myosin) were found lying along the global margin of the muscle and also in a layer lying immediately beneath a discrete band of fibres running along the orbital margin. These fibres resembled those of the skeletal muscle ALD in their type properties. Using another antiserum, anti-I, specific for slow twitch and to a lesser extent, slow tonic myosins, it was possible to identify another slow fibre type which formed the orbital layer and also lay scattered randomly through the body of the muscle. No equivalent to this type was found in the skeletal muscles ALD or iliofibularis. The remaining fibres which did not react with either anti-ALD or anti-I formed 58% of the fibre population and reacted with an antiserum specific for fast myosin. However, their response to alkali preincubation suggests that the fast fibres of eye muscles also contain a myosin which is different from those in skeletal muscle.

Adenosine Triphosphatases↗
PubMed1985

Comparative study of myosins present in the lateral muscle of some fish: species variations in myosin isoforms and their distribution in red, pink and white muscle.

Myosin isoforms and their distribution in the various fibre types of the lateral muscle of eight teleost fish (representing a wide range of taxonomic groups and lifestyles) were investigated electrophoretically, histochemically and immunohistochemically. Polyclonal antisera were raised against slow (red muscle) and fast (white muscle) myosins of the mullet, and used to stain sections of lateral muscle. Antisera specific for fast and slow myosin heavy chains only (anti-FHC and anti-SHC respectively) and for whole fast and slow myosins (anti-F and anti-S respectively) were obtained, and their specificity was confirmed by immunoblotting against electrophoretically separated myofibrillar proteins. The ATPase activity of myosin isoforms was examined histochemically using methods to demonstrate their acid- and alkali-lability and their Ca-Mg dependent actomyosin ATPase. As expected, the predominant myosin (and fibre) type in the red muscle showed an alkali-labile ATPase activity, reacted with the anti-S and anti-SHC sera (but not anti-F or anti-FHC) and contained two 'slow' light chains, whereas the predominant myosin (and fibre) type in the white muscle showed an alkali-stable ATPase activity, reacted with anti-F and anti-FHC sera (but not anti-S or anti-SHC) and contained three 'fast' light chains. However, superimposed upon this basic pattern were a number of variations, many of them species-related. On analysis by two-dimensional gel electrophoresis fish myosin light chains LC1s, LC2s and LC2f migrated like the corresponding light chains of mammalian myosins, but fish LC1f consistently had a more acidic pI value than mammalian LC1f. Fish LC3f varied markedly in Mr in a species-related manner: in some fish (e.g. eel and mullet) the Mr value of LC3f was less than that for the other two light chains (as in mammalian myosin), whereas in others it was similar to that of LC2f (e.g. cat-fish) or even greater (e.g. goldfish). Species differences were also seen in the relative intensity of LC1f and LC3f spots given by the fish fast myosins. In most of the fish examined the red muscle layer showed some micro-heterogeneity, containing (in addition to the typical slow fibres) small numbers of fibres with a histo- and immunohistochemical profile typical of white muscle (fast) fibres. However, other immunohistochemically distinct minority fibres were found in the red muscle of the goldfish. Three types of pink muscle were distinguished: a mosaic of immunohistochemically typical red and white fibres (e.g. grey mullet).(ABSTRACT TRUNCATED AT 400 WORDS)

Anguilla↗
PubMed1984

The fibre type composition of the striated muscle of the oesophagus in ruminants and carnivores.

The fibre type composition of the striated muscle layer of the oesophagus of the cow, sheep, donkey, dog and cat was examined with standard histochemical methods and immunohistochemical staining using type-specific antimyosin sera. The heavy chain and light chain composition of oesophageal myosin was also examined using electrophoretic peptide mapping and 2-dimensional gel electrophoresis respectively. In the ruminants and donkey the oesophagus was composed of fibre types I, IIA and IIC with immunohistochemical characteristics identical to those of the same fibre types found in control skeletal muscle. In the ruminants there was a gradient in the proportion of type I fibres from 1% (at the cervical end) to about 30% (at the caudal end). In the carnivores the oesophageal muscle was composed of a very small percentage of type I and IIC fibres, but the predominant type was very different histochemically and immunohistochemically from all the fibre types (I, IIA, IIB, IIC) present in the control muscles. This oesophageal fibre type ( IIoes ) had an acid- and alkaline-stable m-ATPase activity, a moderate histochemical Ca-Mg actomyosin ATPase activity, and reacted weakly with anti-IIA and anti-IIB myosin sera. Although the light chains of the IIoes myosin were the same as the light chains of a mixture of IIA and IIB myosins, their respective heavy chains gave different peptide maps. Greater differences were obtained between the heavy chains of IIoes and other striated muscle myosins. These observations lead us to conclude that this predominant fibre type of the carnivore oesophageal striated muscle is of the 'fast' type, and contains a distinct isoform of myosin similar but not identical to the other fast type myosins.

Adenosine Triphosphatases↗
PubMed1983

Type-specific proteins of single IIM fibres from cat muscle.

The fibre type IIM, present in the jaw-closer muscles of the cat, has a characteristic form of myosin. To analyse other proteins present in IIM fibres and the usual types I, IIA and IIB, 14C-labelled typed single fibres were analysed by 2-dimensional gel electrophoresis. Whereas types I, IIA and IIB contained both alpha- and beta-forms of tropomyosin, IIM fibres contained only a single form, shown by 1-dimensional peptide mapping to be different from the tropomyosins present in the other fibre types. This single form of tropomyosin, and two soluble proteins seen only in IIM fibres, were also found in IIM fibre-containing muscles from other species, demonstrating that IIM fibres are a distinct type.

Animals↗
PubMed1983

The fibre-type composition of the first branchial arch muscles in Carnivora and Primates.

A combination of standard histochemical techniques and immunohistochemical staining using myosin type-specific antisera was used to determine the fibre-type composition of the muscles of first branchial arch origin (that is, masseter, temporalis, pterygoideus medialis and lateralis, tensor veli palatini, tensor tympani, anterior digastricus and mylohyoideus) in a wide range of the Carnivora and the Primates. The rare IIM fibre type was found in the first branchial arch muscles of most of the species examined, but never in the limb muscles used as controls for this study. The jaw-closer muscles (masseter, temporalis and pterygoideus medialis) were found to contain IIM fibres in all the Carnivora except the lesser panda and in all the Primates except man. When present, the IIM fibres were usually the predominant fibre type, and the only other fibre types present were types I, II or IIC. The presence of IIM fibres in the jaw-closer muscles of most of the Carnivora and the Primates seems to be associated with an aggressive bite which is required for predation by the former and defence by the latter. In both groups of species there was the member which does not have an aggressive bite, the lesser panda and man, respectively, and these (like all other orders of mammals such as Lagomorpha, Rodentia, etc.) were found to have no IIM fibres in the jaw-closer muscles. The two muscles of the first branchial arch group which are derived from the ventral constrictor muscles of the (phylogenetically) original mandibular arch never contained IIM fibres, and were composed of type I and II fibres similar to those found in the control muscles of the limb. Tensor veli palatini and tensor tympani showed species-dependent variations in fibre-type composition and did not always reflect the composition of the jaw-closer muscles. Thus their common origin with the jaw-closers cannot be responsible for the occurrence of IIM fibres in tensor veli palatini and tensor tympani in some species. Furthermore, in tensor tympani but not in tensor veli palatini, the presence of IIM fibres was always accompanied by immunohistochemically slow-tonic fibres. Finally, the regard to the association of oxidative activity with the fibre type as defined by the myofibrillar ATPase method and by the isoform of myosin present, we suggest that in the first branchial arch muscles this is probably not directly comparable to the situation in the typical limb muscle.

Animals↗
PubMed1983

An immunohistochemical study of the middle ear muscles of some carnivores and primates, with special reference to the IIM and slow-tonic fibre types.

The middle ear muscles of several species of carnivores (cat, dog, fox, ferret and stone-marten) and some New World monkeys (Callithrix, Saimiri) and Old World monkeys (Cercopithecus, Macaca) were examined. The fibre type compositions of these muscles were determined by a combination of the standard histochemical myofibrillar ATPase method, and immunohistochemical techniques using myosintype-specific antisera. Immunohistochemically slow-tonic fibres were found in the stapedius muscles of only two carnivores, the ferret and stone-marten. In all the carnivores and the New World monkeys, tensor tympani muscle contained IIM, slow-tonic and slow-twitch fibres, but in the Old World monkeys it resembled stapedius muscle, and contained only Type I (slow-twitch) and IIA fibres. Thus, because all the species examined had IIM fibres in the jaw-closer muscles, this means that the common embryological origin of tensor tympani muscle and the jaw-closers does not necessarily result in tensor tympani muscle containing this fibre type even though IIM fibres occur only in first branchial arch muscles. This fact, together with other species differences in the fibre type composition of these muscles, shows that there is no typical composition of middle ear muscles in general, and suggests that the differences are related to very different functional requirements.

Animals↗
PubMed1982

No classical type IIB fibres in dog skeletal muscle.

To analyse the fibre type composition of adult dog skeletal muscle, enzyme histochemistry, immunohistochemistry for type I, IIA and IIB myosins, and peptide mapping of myosin heavy chains isolated from typed single according to the activity of the m-ATPase after acidic and alkaline preincubation proved to be rather difficult and was only consistently achieved after a very careful adjustment of the systems used. One of these sub-classes of type II fibres stained more strongly for m-ATPase activity after acidic and alkaline preincubation, was oxidative-glycolytic and showed a strong reaction with an anti-type IIA myosin. The other one, however, although showed a faint reaction with an anti-type IIB myosin. Peptide mapping of the myosin heavy chains of typed single fibres revealed two populations of heavy chains among the type II fibre group. Thus, in dog muscle, we are confronted with the presence of two main classes of type II fibres, both oxidative-glycolytic, but differing in the structure of their myosin heavy chains. In contrast to some reports in the literature, no classical type IIB fibres could be detected.

Adenosine Triphosphatases↗
PubMed1982

The tensor tympani muscle of cat and dog contains IIM and slow-tonic fibres: an unusual combination of fibre types.

Using recently developed highly specific antisera to the full range of known adult mammalian skeletal muscle myosins, an immunohistochemical and histochemical examination was made of the middle ear muscle tensor tympani in the dog and cat. Approximately half the fibres were of the IIM type and there was a substantial population of apparently slow-tonic fibres, both these types being rare in mammals. In addition, some type I but no IIA nor IIB fibres were detected. Moreover, as no multiple end-plate innervation, thought to be typical of slow-tonic fibres, could be demonstrated in this muscle by acetylcholinesterase staining or by Ruffini gold impregnation, it is suggested that in tensor tympani the slow-tonic fibres are focally innervated. The very short length of the fibres, only 1-2 mm, is probably sufficient to permit adequate depolarization of a whole fibre by a single centrally situated end-plate. The functional implications of this combination of very rare fibre types in tensor tympani are unclear at present.

Animals↗
PubMed1982

Isometric contractions of motor units and immunohistochemistry of mouse soleus muscle.

1. Isometric contractions of motor units, isolated functionally by ventral root splitting in vivo, were recorded from mouse soleus muscle. 2. Motor unit tensions varied over a narrow symmetrical range and averaged 4.7% of whole muscle tension, corresponding to twenty-one motor units per muscle. 3. There was considerable variation between muscles in isometric twitch times-to-peak and even greater variation for the motor units. The distribution of motor unit times-to-peak was apparently unimodal and could be fitted by a single normal population. A slightly better fit was, however, obtained with two normal populations, as suggested by the histochemistry. 4. Twitch time-to-peak decreased in proportion to axonal conduction velocity in individual animals. The whole population of motor units could be fitted by a linear relation between time-to-peak and the reciprocal of conduction time in the motor axon. Motor unit tension was also linearly related to the reciprocal of conduction time. 5. Histochemistry showed clear division between Type I and Type IIa fibres. Type I fibres reacted strongly with antibody against slow myosin of cat soleus muscle; Type IIa gave a reaction no stronger than the background. The division was as clear as in the cat or rat.

Animals↗
PubMed1982

Motor units and immunohistochemistry of cat soleus muscle after long periods of cross-reinnervation.

1. Cat soleus (slow twitch) was cross-reinnervated with nerve to flexor hallucis or digitorum longus muscle (fast twitch). More than 3 years later motor unit isometric contractions and muscle immunohistochemistry and histochemistry were investigated. All muscles differed from normal fast or slow muscle.2. The motor units could be divided into two groups: one with fast twitches and low tetanic tension, the other with slow twitches and high tension. This is the reverse of the relation between motor unit twitch time and tetanic tension in normal muscle (fast or slow).3. Motor unit twitch time to peak decreased with axonal conduction velocity, as in normal muscle, but so did tetanic tension, which is abnormal.4. Twitch-tetanus ratio increased with twitch time to peak in the group of slow units but not in the fast group (although the range of ratios was as great).5. A tetanus depressed the twitch tension of slow motor units and potentiated fast ones as in normal muscle but the potentiation was often accompanied by an abnormal prolongation of the twitch.6. The mean conduction velocity of axons was slightly higher than at 6 months' reinnervation but below the normal value for fast muscle.7. Antibody to slow myosin was bound strongly to Type I fibres but not to Type II fibres, confirming the histochemical division of fibres into Types I and II.8. More than 95% of the fibres were oxidative, with Type I predominating over Type II a in the ratio of about 2:1.9. The higher tension of the slow motor units was the result of three factors: the number of fibres per motor unit was at least three times that in the fast; Type I fibres had cross-sectional areas little less than Type II (a and b together) and were estimated to develop more tension per unit area. All three findings were different from those in normal fast muscle.10. One flexor hallucis longus muscle was self-reinnervated and examined histochemically. This muscle was abnormal in that a large majority of the fibres were Type I.

Adenosine Triphosphatases↗
PubMedDate not supplied

Preparation of type-specific antimyosin antibodies and determination of their specificity by biochemical and immunohistochemical methods.

This paper reports the preparation of specific anti-slow myosin antibodies (anti-I) and anti-fast myosin antibodies (anti-IIA) raised against myosins from sheep and guinea pig masseter muscles. The specificity of the antibodies has been studied by immunodiffusion in agar and by the GEDELISA test using slow-twitch (type I), fast-twitch red (type IIA) and fast-twitch white (type IIB) myofibrils isolated from guinea pig muscles. The principal specificity of the anti-I and anti-IIA antibodies was for the heavy chains of type I and IIA myosins, respectively. A smaller reaction with the corresponding light chains was also detected. Immunohistochemical staining of muscle sections using these antibodies confirmed their fibre type specificity.

Animals↗