The distribution of heavy-chain isoforms of myosin in airways smooth muscle from adult and neonate humans

Mohammad, Mukhallad A.; Sparrow, Malcolm

doi:10.1042/bj2600421

Cited by 31 publications

(14 citation statements)

References 22 publications

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“…In the rodent ventricle, the slow migrating MHC isoform is predominant in fetal life, whereas the faster migrating MHC is more prevalent during adult life (21). In the pig tracheal smooth muscle, there is a decrease in the ratio of MHCl to MHC2 during maturation (24), whereas similar work on human tracheal smooth muscle failed to show any change in MHC isoform with maturation (25).…”

Section: Newborn Fundusmentioning

confidence: 86%

Characterization of Actin and Myosin in the Developing Stomach

1995

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During growth and development, dietary intake changes from being predominantly liquid in the newborn period to mixed solid liquid meals. These alterations in diet vary the functional demands placed on the stomach. It has been shown that, during development, smooth muscle of the stomach undergoes changes in the mechanism responsible for the contractile process. In this study, we have investigated the possibility that there are structural changes in two of the major proteins that are responsible for generation of force during smooth muscle contraction: actin and myosin. Actin and myosin were identified in newborn kittens (1 wk old) and adult gastric smooth muscle using one-dimensional SDS-PAGE. Although both the antrum and fundus of the kitten have significantly smaller total amounts of actin and myosin per mg protein than the adult, the ratio of actin to myosin is not significantly different between the age groups. Two different The changes in diet ary constitu ents during growth and development from predominantl y liquid to mixed solid liquid meals places an increasing burd en on the stomach that is required to triturate these solids and empty them from the stoma ch. The fundus or proxim al portion of the stomach is respon sibl e for the storage and empty ing of gastric food stuffs, whereas the antrum redu ces the size of ing ested solids and faci litates emptying (1). Th ere is a growing bod y of experiment al ev ide nce suggesting that functional characteristics of smoo th muscle in the sto mac h und ergo changes that parallel these alte rations in dietary mili eu. Th e frequ enc y and amplitude of contractions in the ca nine stoma ch increase during the newborn period (2). Th e in vitro force-generating capacit y of smoo th mu scle from the stomach of newborn rabbit s is less than that of adult gastri c muscl e, and this reduction in forcegeneratin g capacity did not appear to be accounted for by changes in receptor function (3,4). In addition to these quantitative differences in ability to ge nerate force, we have recentl y repo rted that isolated muscle ce lls from the antrum of the adult cat use intr acellular Ca 2 + stores that are not available for kitten antral cells (5). We observed an increase in the amount of MHC2 in the adult, which resulted in a decreased ratio of MHC1 to MHC2 in the adult. We postulate that the decreased quantity of actin and myosin in the kitten stomach and the observed changes in the ratio of the MHC isoforms are related to changes in the gastric motor that occur during growth and development. (Pediatr Res 37: 202-206, 1995) Abbreviations PMSF , phenylmethyl sulfanyl fluoride f3ME, f3-mercaptoethanol MHC , myosin heavy chain Actin and myo sin are two of the major structural proteins involved in the contractil e machinery of the cell. Th e generation of tension during muscle contraction is the result of the interaction between myos in heads and adjacent actin filaments (6). Previous studies have suggested that changes in the absolute amount and relative abundance of isoforms ...

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Section: Newborn Fundusmentioning

confidence: 86%

Characterization of Actin and Myosin in the Developing Stomach

1995

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“…At the end of an experiment, the bronchial tree was placed in Cryo-M-Bed and frozen in isopentane precooled in liquid nitrogen. Transverse sections of airways, 10 µm thick, were cut on a cryostat and stained concurrently for both smooth muscle myosin, using a polyclonal antibody to smooth muscle myosin [14], followed by a rhodamine red conjugated secondary antibody, and for nerve fibres using a monoclonal antibody to the 68 kDa component of neurofilament (Amersham, UK) followed by a fluorescein isothiocyanate (FITC) conjugated secondary antibody. For H&E staining, the bronchial tree was fixed in formal saline (4% formaldehyde) in situ at the end of an experiment.…”

Section: Immunocytochemistry and Histologymentioning

confidence: 99%

Foetal airway motor tone in prenatal lung development of the pig

Sparrow¹,

Warwick²,

Mitchell³

1994

Eur Respir J

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F Fo oe et ta al l aai ir rw wa ay y m mo ot to or r t to on ne e i in n p pr re en na at ta al l l lu un ng g d de ev ve el lo op pm me en nt t o of f t th he e p pi ig g We speculate that the bronchomotor tone and associated spontaneous activity, which move the lung fluid along the airways, serve to maintain an even positive pressure in localized areas of the bronchial tree which is essential to provide the stimulus for continued growth of the lung.

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“…In hu mans, the expression of MHC isoforms during develop ment has been investigated only in nonvascular (tracheal) SMC [ 18], where it was found to be unchanged during the first 8 months of the postnatal period. In a previous study, using developing and adult thoracic aorta, we had charac terized the SMC phenotypes by following the patterns of expression of a number of cytoskeletal and cytocontractile proteins, such as vinculin, caldesmon, actin and myosin [8], However, in that work, we did not study the specific composition of each MHC [8].…”

Section: Introductionmentioning

confidence: 99%

Myosin Heavy-Chain Isoform Composition and Distribution in Developing and Adult Human Aortic Smooth Muscle

et al. 1993

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The myosin heavy-chain (MHC) composition of developing and adult human aortic smooth muscle (SM) was studied by SDS-polyacrylamide gel electrophoresis, Western blotting and indirect immunofluorescence using a panel of anti-MHC antibodies. On 5% SDS gels, three bands of 204, 200 and 196 kDa apparent molecular mass were identified in fetal, infant and adult stages of development. In the extracts from thoracic aorta (upper level), the 204, and 200-kDa bands (designated as SM-1 and SM-2, respectively) were recognized by SM-G4 and SMMS-1 antibodies, raised against a SM antigen, whereas the 196-kDa band was reactive with nonmuscle (NM)-F6 and NM-G2 antiplatelet MHC antibodies. Western blotting and immunofluorescence tests performed on bovine brain and other human NM tissues using NM-F6 and NM-G2 indicated that antigenic targets of the two antibodies resembled that of so-called IIB and IIA NM myosin found in the bovine system, respectively. In the aortic media, SM-1 was expressed throughout development, while SM-2 was upregulated during late fetal and postnatal development. Similarly, the 196-kDa band showed two distinct patterns of immunoreactivity with the anti-NM-MHC antibodies: with NM-G2, antigenicity was equal at all the developmental stages examined, whereas with NM-F6, it diminished during postnatal development. In the upper level, the cellular distribution of NM-G2 and NM-F6 immunoreactivities was similar in the early fetus but quite distinct at later stages of development. In infant and adult subjects, SM cells (SMC) reactive with NM-F6 accumulated predominantly within the intimal layer as well as in some areas of the underlying media as cell foci, whereas NM-G2 homogeneously stained the two layers. In the aorta near the diaphragm (lower level), both antibodies stained the thickened intima but not the underlying media. These data are consistent with the existence of developmental, stage-specific molecular and cellular transitions during vascular SMC maturation in human aortic media. In addition, these data suggest that IIB-like myosin may be expressed in SMC involved specifically in intimal thickening.

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The distribution of heavy-chain isoforms of myosin in airways smooth muscle from adult and neonate humans

Cited by 31 publications

References 22 publications

Characterization of Actin and Myosin in the Developing Stomach

Characterization of Actin and Myosin in the Developing Stomach

Foetal airway motor tone in prenatal lung development of the pig

Myosin Heavy-Chain Isoform Composition and Distribution in Developing and Adult Human Aortic Smooth Muscle

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