scholarly journals Expression Of Cytokeratin 18 In The Peripheral Nerves

2016 ◽  
Vol 60 (2) ◽  
pp. 5-10
Author(s):  
E. Marettová

Abstract The perineurium constitutes the basis for the regulation of endoneurial fluid homeostasis. In the work presented here, cytokeratin 18, as an immunohistochemical marker for epithelial cells, was used to identify the perineurium in the peripheral nerves of two species. Two organs, rich in peripheral nerves, were used; the tongue of the bull and the ductus deferens of the male goat. Special attention was paid to one of the the nerve sheath cells - the perineurial cells of myelinated nerves in the skeletal muscle of the tongue and in the smooth muscle in the wall of the ductus deferens. A positive reaction to cytokeratin 18 was found in the perineurial cells of the perineurial sheath in the nerves of various sizes. No difference in the reactivity was observed between the peripheral nerves of the tongue and that of the ductus deferens.

2018 ◽  
Vol 62 (1) ◽  
pp. 11-17
Author(s):  
E. Marettová ◽  
M. Maretta

Abstract Ductus deferens plays an important role in sperm transport and participates in the preservation of structure, maturation, and viability of sperm. In this study, we have immunohistochemically examined the ductus deferens in the goat. For immunohistochemical study the following monoclonal antibodies were used: cytokeratin 18, α-smooth muscle actin (α-SMA), vimentin and elastin. Morphologically, three distinct layers were identified in the goat ductus deferens — tunica mucosa, tunica muscularis and tunica adventitia. The epithelium of the mucosa was intensely stained with cytokeratin 18 (CK 18). The fibroblasts in the lamina propria and blood capillaries in the muscle layer showed positive reaction for vimentin. A positive reaction for α-SMA was observed in the smooth muscle cells of the tunica muscularis in the internal, middle and outer sublayers. An intense positive reaction for α-SMA was observed in the wall of the blood vessels. Elastic fibers in the form of a loose meshwork were present in all three layers. The high density of elastic fibers were found in the tunica adventitia.


2003 ◽  
Vol 51 (3) ◽  
pp. 339-348 ◽  
Author(s):  
Benoit J. Gentil ◽  
Christian Delphin ◽  
Christelle Benaud ◽  
Jacques Baudier

Here we report a detailed analysis of the expression and localization of the giant protein AHNAK in adult mouse tissues. We show that AHNAK is widely expressed in muscle cells, including cardiomyocytes, smooth muscle cells, skeletal muscle, myoepithelium, and myofibroblasts. AHNAK is also specifically expressed in epithelial cells of most lining epithelium, but is absent in epithelium with more specialized secretory or absorptive functions. In all adult tissues, the main localization of AHNAK is at the plasma membrane. A role for AHNAK in the specific organization and the structural support of the plasma membrane common to muscle and lining epithelium is discussed.


Peripheral nerves consist of afferent and efferent neurones with different functions. TENS can be used to excite somatic efferents to influence the activity of skeletal muscle, and autonomic efferents to influence the activity of smooth muscle, cardiac muscle, and glands. There are physiological rationale to support the use of TENS to manage various non-painful conditions. Clinical experience suggests TENS is often beneficial. The purpose of this chapter is to describe the mechanism of action, clinical use and clinical efficacy for TENS when used to manage non-painful conditions. The chapter covers the effects of TENS on the autonomic nervous system, circulatory system, tissue regeneration, and psychomotor conditions. It also considers the use of TENS for incontinence, constipation, ileus and gastrointestinal discomfort, post-surgical symptoms, and antiemesis.


Reproduction ◽  
2001 ◽  
pp. 317-325 ◽  
Author(s):  
K Whittington ◽  
SJ Assinder ◽  
T Parkinson ◽  
KR Lapwood ◽  
HD Nicholson

Oxytocin is present in the male reproductive tract and has been shown to increase contractility in the epididymis and to modulate steroidogenesis. This study investigated the effects of oxytocin in the testis in vivo, and the presence and cellular localization of oxytocin receptors in the reproductive tract of rams. During the breeding season, mature rams underwent efferent duct ligation before injection of either oxytocin (20 microg) or oxytocin plus an oxytocin antagonist (20 microg) into the testicular artery; the contralateral testicular artery received saline. Injection of oxytocin caused a significant increase (P < 0.05) in the concentration of spermatozoa collected from the rete testis. This effect was not observed after treatment with the oxytocin antagonist plus oxytocin. Western blot analysis performed using a specific oxytocin receptor antibody (020) identified a single immunoreactive band of 66 kDa in testicular and epididymal tissue. This band was present in uterine tissue but not in liver or muscle. Immunocytochemistry identified oxytocin receptors on Leydig and Sertoli cells of the testis, on epithelial cells throughout the epididymis, on peritubular smooth muscle cells in the cauda epididymidis, and on the epithelial cells and circular smooth muscle layer of the ductus deferens. These findings indicate that oxytocin can modulate sperm transport in the ram testis. A role for oxytocin in promoting sperm transit is supported by the localization of oxytocin receptors in the cauda epididymis and ductus deferens, and the presence of receptors on Leydig, Sertoli and epididymal epithelial cells provides further evidence that oxytocin may be involved in the local regulation of steroidogenesis.


Author(s):  
A. V. Somlyo ◽  
H. Shuman ◽  
A. P. Somlyo

Electron probe analysis of frozen dried cryosections of frog skeletal muscle, rabbit vascular smooth muscle and of isolated, hyperpermeab1 e rabbit cardiac myocytes has been used to determine the composition of the cytoplasm and organelles in the resting state as well as during contraction. The concentration of elements within the organelles reflects the permeabilities of the organelle membranes to the cytoplasmic ions as well as binding sites. The measurements of [Ca] in the sarcoplasmic reticulum (SR) and mitochondria at rest and during contraction, have direct bearing on their role as release and/or storage sites for Ca in situ.


1999 ◽  
Vol 96 (3) ◽  
pp. 174-181
Author(s):  
Kerstin Wunderlich ◽  
Marcus Knorr ◽  
H. Northoff ◽  
Hans-J. Thiel

2000 ◽  
Vol 279 (5) ◽  
pp. C1656-C1664 ◽  
Author(s):  
B. Paul Herring ◽  
Shelley Dixon ◽  
Patricia J. Gallagher

The purpose of this study was to characterize myosin light chain kinase (MLCK) expression in cardiac and skeletal muscle. The only classic MLCK detected in cardiac tissue, purified cardiac myocytes, and in a cardiac myocyte cell line (AT1) was identical to the 130-kDa smooth muscle MLCK (smMLCK). A complex pattern of MLCK expression was observed during differentiation of skeletal muscle in which the 220-kDa-long or “nonmuscle” form of MLCK is expressed in undifferentiated myoblasts. Subsequently, during myoblast differentiation, expression of the 220-kDa MLCK declines and expression of this form is replaced by the 130-kDa smMLCK and a skeletal muscle-specific isoform, skMLCK in adult skeletal muscle. These results demonstrate that the skMLCK is the only tissue-specific MLCK, being expressed in adult skeletal muscle but not in cardiac, smooth, or nonmuscle tissues. In contrast, the 130-kDa smMLCK is ubiquitous in all adult tissues, including skeletal and cardiac muscle, demonstrating that, although the 130-kDa smMLCK is expressed at highest levels in smooth muscle tissues, it is not a smooth muscle-specific protein.


1975 ◽  
Vol 67 (1) ◽  
pp. 93-104 ◽  
Author(s):  
T D Pollard

Electron micrographs of negatively stained synthetic myosin filaments reveal that surface projections, believed to be the heads of the constituent myosin molecules, can exist in two configurations. Some filaments have the projections disposed close to the filament backbone. Other filaments have all of their projections widely spread, tethered to the backbone by slender threads. Filaments formed from the myosins of skeletal muscle, smooth muscle, and platelets each have distinctive features, particularly their lengths. Soluble mixtures of skeletal muscle myosin with either smooth muscle myosin or platelet myosin were dialyzed against 0.1 M KC1 at pH 7 to determine whether the simultaneous presence of two types of myosin would influence the properties of the filaments formed. In every case, a single population of filaments formed from the mixtures. The resulting filaments are thought to be copolymers of the two types of myosin, for several reasons: (a) their length-frequency distribution is unimodal and differs from that predicted for a simple mixture of two types of myosin filaments; (b) their mean length is intermediate between the mean lengths of the filaments formed separately from the two myosins in the mixture; (c) each of the filaments has structural features characteristic of both of the myosins in the mixture; and (d) their size and shape are determined by the proportion of the two myosins in the mixture.


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