Macrophages in Pacinian corpuscles

The presence of macrophages in the outer bulb region of mouse, monkey and human Pacinian corpuscles was demonstrated by light and electron microscopy. In the normal, nontreated, Pacinian corpuscles, a few particular cells were located in the spaces between lamellae of the outer bulb. These cells contained numerous vesicles and vacuoles, and various cytoplasmic processes. When horseradish peroxidase (HRP) was injected locally or systemically, many HRP-positive cells, which were considered to be similar to the particular cells described above, were found in the outer bulb region of the corpuscles. Electron microscopy revealed that these cells contained HRP in vesicles and vacuoles, suggesting that they were macrophages vigorously taking up exogenous HRP. Macrophages in the Pacinian corpuscles are considered to work as scavengers to keep the inner environment of the corpuscles clear and constant with regard to its macromolecular content.     

Water-soluble proteins of Pacinian corpuscles

The composition of water soluble proteins has been investigated in different parts of Pacinian corpuscles. The Pacinian corpuscles fluid proteins have been compared with the receptor homogenate proteins and blood serum of a cat. It is supposed that proteins of the Pacinian corpuscle fluid are produced from the blood system on the whole. The composition of the Pacinian corpuscle fluid as well as a great variety of glycoproteins in it allows to suppose that the Pacinian corpuscles fluid perform a transport function.     

Micropipette aspiration of the Pacinian corpuscle

The Pacinian corpuscle (PC) is a cutaneous mechanoreceptor sensitive to high-frequency vibrations (20–1000 Hz). The PC is of importance due to its integral role in somatosensation and the critical need to understand PC function for haptic feedback system development. Previous theoretical and computational studies have modeled the physiological response of the PC to sustained or vibrating mechanical stimuli, but they have used estimates of the receptor’s mechanical properties, which remain largely unmeasured. In this study, we used micropipette aspiration (MPA) to determine an apparent Young’s modulus for PCs isolated from a cadaveric human hand. MPA was applied in increments of 5 mm H₂O (49 Pa), and the change in protrusion length of the PC into the pipette was recorded. The protrusion length vs. suction pressure data were used to calculate the apparent Young’s modulus. Using 10 PCs with long-axis lengths of 2.99 ± 0.41 mm and short-axis lengths of 1.45 ± 0.22 mm, we calculated a Young’s modulus of 1.40 ± 0.86 kPa. Our measurement is on the same order of magnitude as those approximated in previous models, which estimated the PC to be on the same order of magnitude as skin or isolated cells, so we recommend that a modulus in the kPa range be used in future studies.     

A mathematical model of the Pacinian corpuscle

This article describes a mathematical model of the Pacinian corpuscle based on the analysis of the available experimental data and on previous theoretical research. The model includes the main anatomofunctional constituents of the corpuscle: the capsula and the mechano-to-neural transduction; its structure accounts for the formation of the receptor potential and of the spikes on the nerve terminal. Comparison of the theoretical predictions with the experimental results, in response to different types of stimuli provides a substantial validation of the model and an explanation for the basic aspects of the transduction, in particular for: a) the receptor potential time course for isolated stimuli; b) the frequency response, in terms of receptor potential ;c) the frequency threshold curve for the spikes; d) the firing rate, I.S.I. and P.S.T. histograms and the synchronization coefficient, in response to sustained sinusoidal inputs. Possible lines for future experimental research are suggested from the model predictions.     

Immunocytochemical identification of proteins within the Pacinian corpuscle

Light- and electron-microscopic immunocytochemistry (ICC) was performed on Pacinian corpuscles (PCs) obtained from cat mesentery to determine the presence and location of various proteins within the accessory capsule and the neurite. Antibodies to tubulin, neurofilament 200, actin, collagen II and V, glial fibrillary acidic protein (GFAP) and S-100 were used. Type II collagen was localized only in the outer core of the accessory capsule, which is composed of an inner core, an intermediate layer or growth zone, an outer core and an external capsule. Type V collagen was found only in the intermediate growth zone. Intermediate filaments labeled with anti-GFAP were only found in the inner core. The calcium-binding protein that was labeled by anti-S-100 was found only in the inner core. Diffuse and variable staining for actin is present throughout the accessory capsule. The differences in distribution of these various proteins within the capsule suggest different structural/functional properties of the various capsule regions. The neurite was found to contain microtubules (i.e., tubulin) and neurofilaments throughout, but these cellular inclusions were not found within the cytoplasmic extensions (filopodia) that project from the neurite into the hemilamellar clefts formed by the inner-core hemilamellae. The extensions, however, were found to contain actin in a much greater density than that seen in the neurite proper. The presence of actin, but apparent lack of other cytostructural elements within the extensions, is highly reminiscent of the composition of stereocilia found on vestibular and auditory hair cells. Since stereocilia have been shown to play a role in hair-cell mechanotransduction, it is possible that the cytoplasmic extensions are significantly involved with mechanotransduction within the PC.     

Mg, Ca-activated ATP-ase of Pacinian corpuscles]

Adenosine triphosphatase (ATPase) activated by Mg2+ or Ca2+ ions was detected in single mechanoreceptors (Pacini's corpuscles) of cat; addition of Ca2+ (10(-5)M) to Mg-ATP-ase increased the activity by the factor of 1.6. The activity optimum of Mg- or Co-ATPase was in the alkaline pH zone. A high substrate specificity of Mg, Ca-ATPase was shown. Parachlorinemercury-benzoate (5muM) considerably reduced the activity of Mg, Ca-ATPase, whereas oubain (10(-5)M) failed to affect it significantly. It is supposed that Mg, Ca-ATPase of Pacini's corpuscles was close to actomyosine -like proteins.     

Immunocytochemical identification of proteins within the Pacinian corpuscle

Light- and electron-microscopic immunocytochemistry (ICC) was performed on Pacinian corpuscles (PCs) obtained from cat mesentery to determine the presence and location of various proteins within the accessory capsule and the neurite. Antibodies to tubulin, neurofilament 200, actin, collagen II and V, glial fibrillary acidic protein (GFAP) and S-100 were used. Type II collagen was localized only in the outer core of the accessory capsule, which is composed of an inner core, an intermediate layer or growth zone, an outer core and an external capsule. Type V collagen was found only in the intermediate growth zone. Intermediate filaments labeled with anti-GFAP were only found in the inner core. The calcium-binding protein that was labeled by anti-S-100 was found only in the inner core. Diffuse and variable staining for actin is present throughout the accessory capsule. The differences in distribution of these various proteins within the capsule suggest different structural/functional properties of the various capsule regions. The neurite was found to contain microtubules (i.e., tubulin) and neurofilaments throughout, but these cellular inclusions were not found within the cytoplasmic extensions (filopodia) that project from the neurite into the hemilamellar clefts formed by the inner-core hemilamellae. The extensions, however, were found to contain actin in a much greater density than that seen in the neurite proper. The presence of actin, but apparent lack of other cytostructural elements within the extensions, is highly reminiscent of the composition of stereocilia found on vestibular and auditory hair cells. Since stereocilia have been shown to play a role in hair-cell mechanotransduction, it is possible that the cytoplasmic extensions are significantly involved with mechanotransduction within the PC.     

A re-evaluation of the cytology of cat Pacinian corpuscles

Summary The aesthetascs of the spiny lobster, Panulirus argus, are hair sensilla located on the lateral filaments of the antennules. Each hair is about 0.8 mm long and innervated by about 320 bipolar sensory neurons, the dendrites of which project as a bundle into the hair shaft. Each of the dendrites develops two cilia. Within a very short distance each of these cilia branches repetitively and dichotomously resulting in 8000 to 10000 outer dendritic segments per hair, or about 20 to 30 branches per neuron. The branches intertwine frequently before running to the tip of the hair. Each hair also possesses inner and outer auxiliary cells. The inner auxiliary cells surround the bundle of dendrites, extending distally to the origin of the ciliary segments. Extensions of these cells project into the bundle of dendrites, separating groups of dendrites into discrete clusters. Outer auxiliary cells wrap the inner ones, but do not extend beyond the base of the hair.     

Structure of maize protein bodies and immunocytochemical localization of zeins

Summary Zeins, the seed storage proteins of maize (Zea mays L.), are synthesized by membrane-bound polyribosomes and transported into the lumen of the endoplasmic reticulum in developing endosperm, where they assemble into protein bodies. To better understand the organization of protein bodies and the mechanism by which zeins are assembled, we have used immunolocalization to study their distribution within isolated protein bodies. In sections stained with uranyl acetate and lead citrate, the protein body matrix consists of light- and dark-staining regions with the darker stain predominating at the periphery and the lighter stain in the central region. Immunogold staining of the storage proteins in isolated protein bodies reveals a distinct segregation with -zein localized in the light-staining region and - and -zein localized in the dark-staining regions. However, the relative amounts and distribution of these proteins varies substantially among different protein bodies. These results indicate a more complex internal organization than has been previously observed, and suggest that spatial and/or temporal differences in zein synthesis account for this complexity.Abbreviations BSA bovine serum albumin - IgG immunoglobulin G - PB phosphate buffer - SDS sodium dodecyl sulfate - SDS-PAGE sodium dodecyl sulfate-polyacrylamide gel electrophoresis - TTBS Tween-20/tris-buffered saline - TBS-T Tris-buffered saline/Tween-20 - TBS-T-B Tris-buffered saline/Tween-20/bovine serum albumin     

Survival of Pacinian corpuscles after denervation in adult rats

Summary The ultrastructure of Pacinian corpuscles located on the crural interosseous membrane was studied in adult rats 6 h to 10 months after transection of the right sciatic nerve. Axon terminals degenerated one day after transection and were engulfed and resorbed by cells of the inner core within one week. The axial space left after removal of the axonal debris was closed by the lamellae of the inner core. The main structural features of the inner core and capsule remained preserved after denervation throughout the period of study. The denervated inner cores, however, became atrophic 10 months after neurotomy, their mean diameter being reduced by 17.5% compared with that of contralateral control corpuscles. The number of capsular lamellae was unaltered, and perineurial pathways of the peripheral nerve stump remained preserved. Schwann cells proliferated and formed Büngner bands during the first month after denervation, but retracted their processes and became atrophic at later stages after neurotomy.Survival of Pacinian corpuscles after long-term denervation in adult rats is in contrast to their rapid degeneration within several days after nerve section in neonates.     

Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies

The promyelocytic leukaemia (PML) tumour suppressor protein epitomizes the PML-nuclear body (PML-NB) and is crucially required for the proper assembly of this macromolecular nuclear structure. Unlike other, more specialized subnuclear structures such as Cajal and Polycomb group bodies, PML-NBs are functionally promiscuous and have been implicated in the regulation of diverse cellular functions. PML-NBs are dynamic structures that favour the sequestration and release of proteins, mediate their post-translational modifications and promote specific nuclear events in response to various cellular stresses. Recent data suggest that PML-NBs may be heterogeneous in composition, mobility and function.     

A re-evaluation of the cytology of cat Pacinian corpuscles

Summary The ultrastructure of cat mesenteric Pacinian corpuscles in cross and longitudinal sections has been examined. The terminal ends of lamellar cells of the inner core have been identified in longitudinal sections through the proximal portion of the inner core. These terminal bulbous expansions contain characteristic concentric membranes of rough endoplasmic reticulum and in some cases masses of oval membranous inclusions. The central axon as seen in cross section is oval in profile, having X-(short) and Y-(long) axes, and each axonal face is characterized by specializations of the axolemma. At the X-axis, the inner lamellae of the inner core tightly abut a smooth axolemma, with no intervening connective tissue matrix, in a manner reminiscent of a neuroepithelium. The axolemma of the Y-axis has numerous axonal spines (microspikes) that project into the cleft in the inner core. The extent of the axolemma having axonal spines can only be appreciated in longitudinal sections. The clefts contain a specialized connective tissue with elastic and collagen fibrils. The connective tissue compartment of fibers and matrix separating individual inner core lamellae is unique, in that it contains extremely thin collagen fibrils measuring approximately 15 nm in diameter. The diameter of collagen fibrils increases as the cleft is approached. Here the fibrils resemble typical endoneural collagen.