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1.
Pediatr Allergy Immunol Pulmonol ; 30(1): 2-6, 2017 Mar 01.
Article in English | MEDLINE | ID: mdl-28465863

ABSTRACT

ß-adrenergically stimulated sweat secretion depends on the function of the cystic fibrosis transmembrane conductance regulator (CFTR) and discriminates between cystic fibrosis (CF) patients and healthy controls. Therefore, we sought to determine the feasibility, safety, and efficacy of assaying ß-adrenergic sweating in children identified by CF newborn screening to help determine prognoses for individuals with CFTR-related metabolic syndrome (CRMS). Preschool age children with a positive newborn screening test for CF participated in this cross-sectional study. Sweat rates were measured by evaporimetery (cyberDERM, inc.) as transepidermal water losses (g H2O/m2/h) before and after selectively stimulating sweat glands either cholinergically or ß-adrenergically. Net peak sweat responses assayed as evaporation rates were compared between CF and CRMS cohorts. After a pilot test in adults, children between 4 and 6 years of age were evaluated (CF, n = 16; CRMS, n = 10). The test protocol was well tolerated; electrocardiograms and vital signs were within normal range for all subjects. The mean evaporative sweat rates in both groups in response to cholinergic stimulation were similar (CF, 60.3 ± 23.8; CRMS, 57.7 ± 13.9; p = 0.72) as well as to ß-adrenergic stimulation (CF, 1.1 ± 1.7; CRMS, 2.0 ± 2.0; p = 0.14). The ß-adrenergic sweat test is safe and well tolerated by young children. However, the ß-adrenergic sweat secretion rates as measured by evaporimetery did not discriminate between CF and CRMS cohorts.

2.
J Histochem Cytochem ; 59(9): 849-63, 2011 Sep.
Article in English | MEDLINE | ID: mdl-21705646

ABSTRACT

Cat masticatory muscle during regeneration expresses masticatory-specific myofibrillar proteins upon innervation by a fast muscle nerve but acquires the jaw-slow phenotype when innervated by a slow muscle nerve. Here, we test the hypothesis that chronic low-frequency stimulation simulating impulses from the slow nerve can result in masticatory-to-slow fiber-type transformation. In six cats, the temporalis muscle was continuously stimulated directly at 10 Hz for up to 12 weeks using a stimulator affixed to the skull. Stimulated muscles were analyzed by immunohistochemistry using, among others, monoclonal antibodies against masticatory-specific myosin heavy chain (MyHC), myosin binding protein-C, and tropomyosins. Under the electrodes, stimulation induced muscle regeneration, which generated slow fibers. Deep to the electrodes, at two to three weeks, two distinct populations of masticatory fibers began to express slow MyHC: 1) evenly distributed fibers that completely suppressed masticatory-specific proteins but transiently co-expressed fetal MyHCs, and 2) incompletely transformed fibers that express slow and masticatory but not fetal MyHCs. SDS-PAGE confirmed de novo expression of slow MyHC and ß-tropomyosin in the stimulated muscles. We conclude that chronic low-frequency stimulation induces masticatory-to-slow fiber-type conversion. The two populations of transforming masticatory fibers may differ in their mode of activation or lineage of their myogenic cells.


Subject(s)
Masticatory Muscles/cytology , Muscle Contraction , Muscle Fibers, Skeletal/cytology , Animals , Cats , Electric Stimulation , Electrodes , Immunohistochemistry , Masticatory Muscles/physiology , Muscle Fibers, Skeletal/physiology , Muscle Proteins/metabolism
3.
J Histochem Cytochem ; 58(11): 989-1004, 2010 Nov.
Article in English | MEDLINE | ID: mdl-20679518

ABSTRACT

Cat jaw-closing muscles are a distinct muscle allotype characterized by the expression of masticatory-specific myofibrillar proteins. Transplantation studies showed that expression of masticatory myosin heavy chain (m-MyHC) is promoted by fast motor nerves, but suppressed by slow motor nerves. We investigated whether masticatory myosin-binding protein-C (m-MBP-C) and masticatory tropomyosin (m-Tm) are similarly regulated. Temporalis muscle strips were transplanted into limb muscle beds to allow innervation by fast or slow muscle nerve during regeneration. Regenerated muscles were examined postoperatively up to 168 days by peroxidase IHC using monoclonal antibodies to m-MyHC, m-MBP-C, and m-Tm. Regenerates in both muscle beds expressed fetal and slow MyHCs, m-MyHC, m-MBP-C, and m-Tm during the first 4 weeks. Longer-term regenerates innervated by fast nerve suppressed fetal and slow MyHCs, retaining m-MyHC, m-MBP-C, and m-Tm, whereas fibers innervated by slow nerve suppressed fetal MyHCs and the three masticatory-specific proteins, induced slow MyHC, and showed immunohistochemical characteristics of jaw-slow fibers. We concluded that expression of m-MBP-C and m-Tm is coregulated by m-MyHC and that neural impulses to limb slow muscle are capable of suppressing masticatory-specific proteins and to channel gene expression along the jaw-slow phenotype unique to jaw-closing muscle.


Subject(s)
Carrier Proteins/metabolism , Extremities/innervation , Jaw/metabolism , Movement , Regeneration , Temporal Muscle/physiology , Tropomyosin/metabolism , Animals , Cats , Gene Expression Regulation , Organ Specificity , Phenotype , Protein Isoforms/metabolism , Temporal Muscle/innervation , Temporal Muscle/metabolism , Time Factors
4.
J Histochem Cytochem ; 58(7): 623-34, 2010 Jul.
Article in English | MEDLINE | ID: mdl-20354144

ABSTRACT

We test the hypothesis that cat jaw satellite cells belong to a distinct lineage preprogrammed to express masticatory-specific isoforms of myosin heavy-chain (m-MyHC), myosin-binding protein-C (m-MBP-C), and tropomyosin (m-Tm) during myogenesis in vitro. A monoclonal antibody (MAb) against m-MyHC and MAbs raised here against cat m-MBP-C and m-Tm were used to stain cryostat sections of cat masseter muscle and cultured myotubes derived from satellite cells of cat temporalis and limb muscles, using peroxidase immunohistochemistry. MAbs against m-MBP-C bound purified m-MBP-C in Western blots. MAbs against m-Tm failed to react with m-Tm in Western blots, but reacted with native m-Tm in gel electrophoresis-derived ELISA. In cat masseter sections, MAbs against m-MyHC, m-MBP-C, and m-Tm stained all masticatory fibers, but not the jaw-slow fibers. Cat jaw and limb muscle cultures mature significantly more slowly relative to rodent cultures. However, at 3 weeks, all three MAbs extensively stained temporalis myotubes, whereas they apparently stained isolated myotubes weakly in cat limb and rat jaw cultures. We conclude that satellite cells of masticatory fibers are preprogrammed to express these isoforms during myogenesis in vitro. These results consolidate the notion that masticatory and limb muscle allotypes are distinct.


Subject(s)
Carrier Proteins/metabolism , Masticatory Muscles/metabolism , Muscle Fibers, Skeletal/metabolism , Myosin Heavy Chains/metabolism , Satellite Cells, Skeletal Muscle/metabolism , Tropomyosin/metabolism , Animals , Antibodies, Monoclonal/metabolism , Carrier Proteins/immunology , Cats , Cells, Cultured , Immunoenzyme Techniques , Masticatory Muscles/cytology , Mice , Muscle Development , Myosin Heavy Chains/immunology , Rats , Tropomyosin/immunology
5.
J Comp Physiol B ; 176(7): 685-95, 2006 Sep.
Article in English | MEDLINE | ID: mdl-16773370

ABSTRACT

Myosin heavy chains (MyHCs) and fibre types in the masseter muscle of seven species of Australian marsupials (brushtail and ringtail possums, bettong, bandicoot, dunnart, two species of antechinuses) spanning three orders were studied by native myosin electrophoresis, SDS-PAGE, immunoblotting and immunohistochemistry. We found only two fibre types in the masseter muscles of these animals: (1) masticatory fibres expressing masticatory MyHC, and (2) hybrid alpha/beta fibres that co-express alpha-cardiac and beta-cardiac MyHCs. Masticatory fibres predominate in most species, being appropriate for predation or for chewing tough vegetable matter. The relative abundance of alpha/beta fibres decreased from 60% to 0 in the order: ringtail possum > brushtail possum > bettong > bandicoot > dunnart/antechinus. These variations in masseter fibre type are correlated with decreasing amounts of vegetable matter in the diets of these animals. The results are in contrast to earlier work on masseter fibres of macropodids that expressed alpha-cardiac MyHC almost homogeneously. The fact that the bettong (Family: Potoroidae), which belong to the same marsupial superfamily (Macropodoidea) as kangaroos and wallabies (Family: Macropodidae), has not specialized in the exclusive expression of alpha-cardiac MyHC as members of the latter family suggests that this specialization was of recent phylogenetic origin (30 million years before present).


Subject(s)
Marsupialia/physiology , Myosin Heavy Chains/isolation & purification , Protein Isoforms/isolation & purification , Adaptation, Physiological , Animals , Biological Evolution , Blotting, Western , Electrophoresis , Electrophoresis, Polyacrylamide Gel , Immunohistochemistry , Masseter Muscle/chemistry , Opossums , Ventricular Myosins/genetics
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