Posterior surgery causes muscular alterations; however, no correlation with pain or other clinical symptoms could be established. Therefore, in the case of unsatisfactory results after surgery of the lumbar spine, reasons other than muscle damage caused by use of the posterior approach must be considered.
A knowledge of the alteration in the fibre type profile of paraspinal muscle associated with low back pain is essential for the design of successful rehabilitation programmes. In attempting to compare the muscles of patients with low back pain with those of controls, few previous studies have considered factors such as gender, age, and size of the subjects, each of which can potentially confound interpretation of the results. We obtained samples of lumbar paraspinal muscle during spinal surgery from 21 patients with low back pain and, using the percutaneous biopsy technique, from 21 control volunteers matched for gender, age, and body mass. The samples were subject to routine histochemical analysis to determine characteristics of muscle fibre type. Compared with controls, the muscle of the patients had a significantly higher proportion of type-IIB (fast-twitch glycolytic) fibres than type-I (slow oxidative) fibres. The mean size of a given fibre type did not differ between the patients and the controls. Consequently, the relative area of the muscle occupied by type-IIB fibres was higher and that by type-I fibres was lower in the patients. The patients had a greater number of muscle samples with more than 1% type-IIC fibres, and abnormalities that could be described as pathological were more marked in the patients than in the controls. In conclusion, the paraspinal muscles of patients who have low back pain display a more glycolytic (faster) profile; this can be expected to render them less resistant to fatigue.
Biopsies of ventral neck muscles (sternocleidomastoid, omohyoid, and longus colli) and dorsal neck muscles (rectus capitis posterior major, obliquus capitis inferior, splenius capitis, and trapezius) were taken from 64 patients who underwent spondylodesis for cervical dysfunction of different etiologies. The muscle fibers were classified histochemically as type I, IIA, IIB, or IIC (transitional or intermediate fibers) according to the pH lability of their myofibrillar ATPase. Signs of muscle fiber transformations were observed in all muscles investigated, as evidenced by an increased relative amount of type-IIC fibers. The transformations occurred independently of (a) the type of muscle (i.e., more "postural" or more "phasic"), (b) the sex and age of the patient, (c) the type of condition, and (d) the presence of additional neurological deficits. Thus, the same pattern of muscular reaction was found in patients with rheumatoid arthritis as in patients with soft-tissue injuries of the neck (e.g., "whiplash injury"). In the ventral muscles and the obliquus capitis inferior, the occurrence of transformations correlated strongly with the duration of symptoms; in the ventral muscles the vast majority of transformations were encountered in patients with a shorter history of symptoms, whereas in the obliquus capitis inferior the reverse occurred. In the other dorsal muscles, no correlation with the duration of symptoms was found. Muscles in which transformations had ceased displayed, on average, a significantly higher percentage of fast type-IIB fibers than were found in muscles with ongoing transformations. This strongly indicates that the transformations proceeded in the direction from "slow oxidative" to "fast glycolytic."
α and β parvalbumins are Ca2+‐binding proteins of the EF‐hand type. We determined the protein sequence of human brain α parvalbumin by mass spectrometry and cloned human β parvalbumin (or oncomodulin) from genomic DNA and preterm placental cDNA. β parvalbumin differs in 54 positions from α parvalbumin and lacks the C‐terminal amino acid 109. From MS analyses of α and β parvalbumins we conclude that parvalbumins generally lack posttranslational modifications. α and β parvalbumins were differently expressed in human tissues when analyzed by immunoblotting and polymerase‐chain‐reaction techniques. Whereas α parvalbumin was found in a number of adult human tissues, β parvalbumin was restricted to preterm placenta. The pattern of α parvalbumin expression also differs in man compared to other vertebrates. For example, in rat, α parvalbumin was found in extrafusal and intrafusal skeletal‐muscle fibres whereas, in man, α parvalbumin was restricted to the muscle spindles. Different functions for α and β parvalbumins are discussed.
Biopsies of the sternocleidomastoid and omohyoid muscle were taken from 24 patients who underwent arthrodesis for cervical dysfunction of different etiologies. The two muscles, which are involved differently in movements of the head and cervical spine, were investigated histochemically. Muscle fibers were classified as type I, IIA, IIB, or IIC (transitional fibers) according to the pH lability of myofibrillar ATPase and calculated relative distribution. In both muscles, fiber transformations (as evidenced by an increase in the relative amount of type-IIC fibers) were regularly observed within the first 2 years after the onset of the symptoms. The occurrence of the transformation processes was independent of the patient's age and sex and was the same for the different etiologies. Since the overall fiber composition of the muscles remained essentially unchanged, the fiber transformations must occur alternatingly in both directions (from "slow" to "fast" and the reverse). Muscles of patients with a long case history showed no greater signs of fiber transformation. Therefore, fiber transformations in response to cervical dysfunction occur in the initial stage of the disease and involve different types of muscles. The muscles then return to a "stable" condition, independent of the continuation of the dysfunction and the chronic neck pain.
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