Regional Myosin heavy chain distribution in selected paraspinal muscles.
نویسندگان
چکیده
STUDY DESIGN Cross-sectional study with repeated measures design. OBJECTIVE To compare the myosin heavy-chain isoform distribution within and between paraspinal muscles and to test the theory that fiber-type gradients exist as a function of paraspinal muscle depth. SUMMARY OF BACKGROUND DATA There is still uncertainty regarding the fiber-type distributions within different paraspinal muscles. It has been previously proposed that deep fibers of the multifidus muscle may contain a higher ratio of type I to type II fibers, because, unlike superficial fibers, they primarily stabilize the spine, and may therefore have relatively higher endurance. Using a minimally invasive surgical approach, using tubular retractors that are placed within anatomic intermuscular planes, it was feasible to obtain biopsies from the multifidus, longissimus, iliocostalis, and psoas muscles at specific predefined depths. METHODS Under an institutional review board-approved protocol, muscle biopsies were obtained from 15 patients who underwent minimally invasive spinal surgery, using the posterior paramedian (Wiltse) approach or the minimally invasive lateral approach. Myosin heavy chain (MyHC) isoform distribution was analyzed using SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) electrophoresis. Because multiple biopsies were obtained from each patient, MyHC distribution was compared using both within- and between-muscle repeated measures analyses. RESULTS The fiber-type distribution was similar among the posterior paraspinal muscles and was composed of relatively high percentage of type I (63%), compared to type IIA (19%) and type IIX (18%) fibers. In contrast, the psoas muscle was found to contain a lower percentage of type I fibers (42%) and a higher percentage of type IIA (33%) and IIX fibers (26%; P<0.05). No significant difference was found for fiber-type distribution among 3 different depths of themultifidus and psoas muscles. CONCLUSION Fiber-type distribution between the posterior paraspinal muscles is consistent and is composed of relatively high percentage of type I fibers, consistent with a postural function. The psoas muscle, on the other hand, is composed of a higher percentage of type II fibers such as in the appendicular muscles. Our data do not support the idea of a fiber-type gradient as a function of depth for any muscle studied.
منابع مشابه
MyoD and Myf-5 differentially regulate the development of limb versus trunk skeletal muscle.
The myogenic progenitors of epaxial (paraspinal and intercostal) and hypaxial (limb and abdominal wall) musculature are believed to originate in dorsal-medial and ventral-lateral domains, respectively, of the developing somite. To investigate the hypothesis that Myf-5 and MyoD have different roles in the development of epaxial and hypaxial musculature, we further characterized myogenesis in Myf...
متن کاملThe distribution of heavy-chain isoforms of myosin in airways smooth muscle from adult and neonate humans.
Changes in the expression of heavy chains of myosin during development determine the functional characteristics of striated muscles. The distribution of heavy-chain isoforms of smooth-muscle myosin was determined in the airways of adult and infant humans to see whether it might underlie the hyperreactivity of human airways. The protein bands corresponding to myosin were separated using SDS/poly...
متن کاملPaylean alters myosin heavy chain isoform content in pig muscle.
Feeding beta-adrenergic agonists promotes muscle growth. Early histological techniques failed to show precisely how feeding ractopamine-HCl (Paylean) alters muscle growth in pigs. To understand these effects, an indirect enzyme-linked immunosorbent assay (ELISA) was used to determine the abundance of each adult skeletal muscle myosin heavy chain isoform, one means of assigning muscle fiber type...
متن کاملAre hybrid fibers a common motif of canine laryngeal muscles? Single-fiber analyses of myosin heavy-chain isoform composition.
BACKGROUND The canine lateral cricoarytenoid muscle contains a large proportion of muscle fibers that coexpress various combinations of myosin heavy-chain isoforms (ie, so-called hybrid fibers). OBJECTIVE To test the hypothesis that hybrid fibers are a common motif throughout laryngeal muscles. DESIGN The posterior cricoarytenoid, canine cricothyroid, and thyroarytenoid muscles were removed...
متن کاملSarcoplasmic reticulum fast CA(2+)-pump and myosin heavy chain expression in extraocular muscles.
PURPOSE To investigate the distribution of the sarcoplasmic reticulum fast-twitch Ca(2+)-pump (Ca(2+)-adenosine triphosphatase [Ca(2+)-ATPase]) in extraocular muscle fiber populations of the rat and rabbit, using fast Ca(2+)-adenosine triphosphatase-specific monoclonal antibodies. METHODS Adult female rats and rabbits were killed with overdose of sodium pentobarbital, and the extraocular musc...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Spine
دوره 35 13 شماره
صفحات -
تاریخ انتشار 2010