Interleukin-1 alpha in human sweat is functionally active and derived from the eccrine sweat gland

1994 ◽  
Vol 266 (3) ◽  
pp. R950-R959 ◽  
Author(s):  
K. Sato ◽  
F. Sato
Keyword(s):  
Sweat Gland ◽  
Plasma Membranes ◽  
Sweat Rate ◽  
Interleukin 1 ◽  
Biologically Active ◽  
Sweat Test ◽  
Cultured Fibroblasts ◽  
Human Sweat ◽  
The Mean ◽  
Secretory Coil

We wished to establish the presence of interleukin-1 (IL-1) in human sweat (5) and clarify its origin and mechanism of secretion. IL-1 alpha concentration ([IL-1 alpha]) in clean sweat from the back increased with the sweat rate, plateauing at the maximal sweat rate ([IL-1 alpha]max). The mean [IL-1 alpha]max was 545 pg/ml (n = 17) for men and 1,324 pg/ml for women in back sweat. The mean [IL-1 alpha]max for axillary sweat in men was 1,568 (n = 6). Palmar sweat was 9.2 ng/ml (n = 5) for IL-1 alpha and 7.9 ng/ml for IL-1 beta. [IL-1 alpha]max decreased to one-third that of the first sweat test, when second sauna sweat tests were conducted after 2 h of continuous sweating on the same day. Western blot analysis of the purified sweat IL-1 alpha fraction revealed bands at 17, 29, and 33 kDa. Immunoreactive IL-1 alpha was localized mainly in the secretory coil lumen, intercellular canaliculi, cytoplasm, mitochondria, and near plasma membranes. Polymerase chain reaction revealed the presence of IL-1 alpha mRNA in the sweat gland and in cultured human eccrine secretory coil cells. Both sweat IL-1 alpha and human recombinant IL-1 alpha at 500 pg/ml strongly stimulated interleukin-6 and interleukin-8 production in cultured fibroblasts. We conclude that the IL-1 alpha-like immunoreactive substance in sweat is IL-1 alpha itself, is derived from the sweat gland, and is biologically active at concentrations normally present in fresh sweat.

Electrophysiologically distinct cell types in human sweat gland secretory coil

1992 ◽  
Vol 262 (2) ◽  
pp. C287-C292 ◽  
Author(s):  
M. M. Reddy ◽  
P. M. Quinton
Keyword(s):  
Sweat Gland ◽  
Basolateral Membrane ◽  
Cell Types ◽  
Membrane Potentials ◽  
Adrenergic Stimulation ◽  
Beta Adrenergic ◽  
Human Sweat ◽  
Distinct Cell ◽  
Secretory Coil ◽  
I Cells

The human sweat gland secretory coil consists of three histologically distinct cell types: myoepithelial (ME), light (or clear), and dark cells. The electrophysiological properties of all these cells are poorly defined. Employing electrophysiological techniques, we report distinct pharmacological responses of three different cell types from freshly isolated human sweat gland secretory coil. The superficial ME cells are characterized by 1) spontaneous depolarizing spikes (2 to 50 mV), 2) high cell membrane potentials [Vm = -68.6 +/- 3.9 (SE) mV; n = 21], 3) a K(+)-selective cell membrane (slope response = 54.2 +/- 6.7 mV per decade K+ concentration; n = 4), 4) depolarizing responses to cholinergic agonist mecholyl (delta Vm = 29.1 +/- 3.1 mV, n = 21), and 5) insensitivity to beta-adrenergic stimulation (n = 12). Two other types of cells, presumably secretory, were also observed. We arbitrarily labeled these cells as beta-adrenergic sensitive (beta-S) and beta-adrenergic insensitive (beta-I) cells based on their respective sensitivity to isoproterenol (IPR), a beta-adrenomimetic. Properties of the beta-S cells include 1) relatively higher basolateral membrane potentials (Vm = -57.3 +/- 3.1 mV; n = 13), 2) depolarizing responses to IPR (delta Vm = 16.8 +/- 2.6 mV; n = 9) inhibitable by the beta-adrenergic antagonist propranolol, and 3) hyperpolarizing responses to mecholyl (delta Vm = -21.8 +/- 2.0 mV; n = 13). The beta-I cells are characterized by 1) low basolateral membrane potentials (Vm = -23.6 +/- 2.1 mV; n = 16), 2) insensitivity to beta-adrenergic stimulation, and 3) hyperpolarizating responses to mecholyl (delta Vm = -16.1 +/- 2.1 mV; n = 16).

Secretion of Ions and Pharmacological Responsiveness in the Mouse Paw Sweat Gland

1994 ◽  
Vol 86 (2) ◽  
pp. 133-139 ◽  
Author(s):  
K. Sato ◽  
S. Cavallin ◽  
K. T. Sato ◽  
F. Sato
Keyword(s):  
Cyclic Amp ◽  
Sweat Gland ◽  
Sweat Rate ◽  
Eccrine Sweat Gland ◽  
Sweat Secretion ◽  
Cl Channels ◽  
Functional Features ◽  
Secretory Coil ◽  
Rat Paw

1. Some of the basic functional features of the mouse paw eccrine sweat gland were delineated to allow comparison with those of transgenic mice in the future. 2. The mouse sweat secretory coil responds to methacholine, elaborating a K+-rich (> 120 mmol/l), Na+-poor (< 70 mmol/l) primary fluid as does the rat paw sweat gland, as previously reported. The methacholine-induced sweat rate increases with age in parallel with the growth of the sweat gland over the first 6 weeks of life. 3. The sweating response to cyclic AMP-elevating agents, such as isoprenaline or forskolin, is as much as 40% of the methacholine-induced sweat rate at 1 week of age, but falls to 10% by 6 weeks of age despite the fact that the agonist-induced tissue accumulation of cyclic AMP expressed on a per μg of protein basis triples with age over the same period. 4. A marked K+ outflux was also noted in response to methacholine and a small K+ outflux was seen in response to cyclic AMP-elevating agonists in super-fused adult mouse secretory coils in vitro. 5. Since sweat secretion is usually associated with activation of either K+ channels or Cl− channels or both, and since the sweating occurred in response to cyclic AMP-elevating agonists, we speculate that the cyclic AMP-activated Cl− channels (the mouse version of the cystic fibrosis transmembrane conductance regulator) may also occur in the mouse sweat gland, but that the degree of their expression may be influenced by the age of the mice.

NKCC1 and NHE1 are abundantly expressed in the basolateral plasma membrane of secretory coil cells in rat, mouse, and human sweat glands

2005 ◽  
Vol 289 (2) ◽  
pp. C333-C340 ◽  
Author(s):  
Lene N. Nejsum ◽  
Jeppe Praetorius ◽  
Søren Nielsen
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Protein Localization ◽  
Sweat Glands ◽  
Acid Base ◽  
Human Sweat ◽  
Sweat Secretion ◽  
Basolateral Plasma Membrane ◽  
Immunoperoxidase Labeling ◽  
Secretory Coil

In isolated sweat glands, bumetanide inhibits sweat secretion. The mRNA encoding bumetanide-sensitive Na+-K+-Cl− cotransporter (NKCC) isoform 1 (NKCC1) has been detected in sweat glands; however, the cellular and subcellular protein localization is unknown. Na+/H+ exchanger (NHE) isoform 1 (NHE1) protein has been localized to both the duct and secretory coil of human sweat duct; however, the NHE1 abundance in the duct was not compared with that in the secretory coil. The aim of this study was to test whether mRNA encoding NKCC1, NKCC2, and Na+-coupled acid-base transporters and the corresponding proteins are expressed in rodent sweat glands and, if expressed, to determine the cellular and subcellular localization in rat, mouse, and human eccrine sweat glands. NKCC1 mRNA was demonstrated in rat palmar tissue, including sweat glands, using RT-PCR, whereas NKCC2 mRNA was absent. Also, NHE1 mRNA was demonstrated in rat palmar tissue, whereas NHE2, NHE3, NHE4, electrogenic Na+-HCO3− cotransporter 1 NBCe1, NBCe2, electroneutral Na+-HCO3− cotransporter NBCn1, and Na+-dependent Cl−/HCO3− exchanger NCBE mRNA were not detected. The expression of NKCC1 and NHE1 proteins was confirmed in rat palmar skin by immunoblotting, whereas NKCC2, NHE2, and NHE3 proteins were not detected. Immunohistochemistry was performed using sections from rat, mouse, and human palmar tissue. Immunoperoxidase labeling revealed abundant expression of NKCC1 and NHE1 in the basolateral domain of secretory coils of rat, mouse, and human sweat glands and low expression was found in the coiled part of the ducts. In contrast, NKCC1 and NHE1 labeling was absent from rat, mouse, and human epidermis. Immunoelectron microscopy demonstrated abundant NKCC1 and NHE1 labeling of the basolateral plasma membrane of mouse sweat glands, with no labeling of the apical plasma membranes or intracellular structures. The basolateral NKCC1 of the secretory coils of sweat glands would most likely account for the observed bumetanide-sensitive NaCl secretion in the secretory coils, and the basolateral NHE1 is likely to be involved in Na+-coupled acid-base transport.

Evidence of two distinct epithelial cell types in primary cultures from human sweat gland secretory coil

1992 ◽  
Vol 262 (4) ◽  
pp. C891-C898 ◽  
Author(s):  
M. M. Reddy ◽  
C. L. Bell ◽  
P. M. Quinton
Keyword(s):  
Epithelial Cells ◽  
Primary Culture ◽  
Sweat Gland ◽  
Primary Cultures ◽  
Membrane Potentials ◽  
Secretory Cells ◽  
Beta Adrenergic ◽  
Human Sweat ◽  
Secretory Coil ◽  
I Cells

The human sweat gland secretory coil (SC) is comprised of myoepithelial (ME) and two types of secretory epithelial cells. The secretory cells include beta-adrenergic-sensitive (beta-S) cells [responsive to the beta-adrenergic agonist isoproterenol (IPR)] and beta-adrenergic insensitive (beta-I) cells. We have grown segments of SC in primary culture and found that under the conditions described here, only epithelial cells form outgrowths as indicated by morphological and physiological properties. As in the native SC epithelium, the secretory cells in primary culture were comprised of polygonal epithelial cells with a characteristic hyperpolarization of cell potentials (Vm) to cholinergic stimulation by mecholyl (magnitude of change of Vm = delta Vm = 21.5 +/- 1.3 mV, mean +/- SE, n = number of cells = 44). We have found both beta-S and beta-I cells as determined by unstimulated membrane potentials, sensitivity to IPR, and K+ conductance (GK+). The frequency distribution of unstimulated cells indicated two distinct populations of cells, one with high membrane potentials (Vm = -63 +/- 2.6 mV), which correlated with beta-S cells, and a second with low membrane potentials (Vm = -22 +/- 1.5 mV), which correlated with the beta-I cells. IPR depolarized the Vm of beta-S cells (delta Vm = 11.0 +/- 0.8 mV, n = 25) without affecting the Vm of beta-I cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Functional design of microvilli in the Malpighian tubules of the insect Rhodnius prolixus

1983 ◽  
Vol 60 (1) ◽  
pp. 117-135
Author(s):  
T.J. Bradley
Keyword(s):  
Plasma Membranes ◽  
Current Knowledge ◽  
Morphological Difference ◽  
Rhodnius Prolixus ◽  
Malpighian Tubules ◽  
Free Standing ◽  
Narrow Channels ◽  
Morphological Specialization ◽  
Mitochondrial Volume ◽  
The Mean

The Malpighian tubules of Rhodnius prolixus are divided into two regions; the upper tubule, which is the site of isosmotic secretion and haemolymph filtration, and the lower tubule where water and KCl are resorbed. In the upper tubule the microvilli are arranged in clumps consisting of several hundred microvilli lying closely parallel. The microvillar plasma membranes do not touch but are held approximately equal to 16 nm apart along the full length of the microvilli. As a consequence, the extracellular space between the microvilli consists of long narrow channels. A morphometric analysis of extracellular, cytoplasmic, endoplasmic reticular and mitochondrial volume within the clumps was conducted. Using the secretion rate of the epithelium and the channel dimensions, it was calculated that the mean residence time for secreted fluid in the intermicrovillar spaces was approximately equal to 0.4s. In view of our current knowledge of the physiology and morphology of the upper tubule, it is argued: (1) that osmotically driven water passes principally through the cells, not the junctional spaces; and (2) that the microvillar clumps are a morphological specialization, which serves to maximize solute-water coupling in the upper tubule. The microvilli in the lower tubule are free-standing, with no pattern of clumping as in the upper tubule. The axopods are about twice as long as the microvilli (10-14 micron) and are found in all regions of the lower tubule. This is in agreement with the proposal that the motile axopods serve to propel uric acid crystals through the lower tubule. No morphological difference was found between the upper and lower halves of the lower tubule, although the two portions are known to be physiologically distinct.

scholarly journals The Sweat Glands and Hair Follicles of European Cattle

1972 ◽  
Vol 25 (3) ◽  
pp. 585 ◽  
Author(s):  
D Mcewan Jenkinson ◽  
T Nay
Keyword(s):  
Hair Follicle ◽  
Sweat Gland ◽  
Hair Follicles ◽  
Sweat Glands ◽  
Mean Values ◽  
The Mean ◽  
European Cattle

Measurements were made on the skins of 1363 cattle from different European breeds. The mean values of these measurements have been tabulated for each breed and the skin types present in each breed or group of breeds have been determined using sweat gland shape (LID) and hair follicle depth (FrY) as the principal bases of comparison.

scholarly journals Keratinocyte growth factor, tumor necrosis factor-alpha and interleukin-1 beta gene expression in cultured fibroblasts and keratinocytes from burned patients

2013 ◽  
Vol 28 (8) ◽  
pp. 551-558 ◽  
Author(s):  
Alfredo Gragnani ◽  
Bruno Rafael Müller ◽  
Ismael Dale Contrim Guerreiro da Silva ◽  
Samuel Marcos Ribeiro de Noronha ◽  
Lydia Masako Ferreira
Keyword(s):  
Gene Expression ◽  
Tumor Necrosis ◽  
Keratinocyte Growth Factor ◽  
Interleukin 1 ◽  
Interleukin 1 Beta ◽  
Necrosis Factor Alpha ◽  
Cultured Fibroblasts ◽  
Factor Alpha ◽  
Beta Gene ◽  
Necrosis Factor

Generation and transit pathway of H+ is critical for inhibition of palmar sweating by iontophoresis in water

1993 ◽  
Vol 75 (5) ◽  
pp. 2258-2264 ◽  
Author(s):  
K. Sato ◽  
D. E. Timm ◽  
F. Sato ◽  
E. A. Templeton ◽  
D. S. Meletiou ◽  
...  
Keyword(s):  
Sweat Rate ◽  
Tap Water ◽  
Inhibitory Effect ◽  
Sweat Glands ◽  
Galvanic Current ◽  
Silicone Grease ◽  
Secretory Coil ◽  
Cathodal Current ◽  
Palmar Sweating

Passing galvanic current across the skin (known as "tap water iontophoresis" or TWI) inhibits sweating; however, its mechanism of action is unclear. Using improved methods, we confirmed that anodal current has more of an inhibitory effect than cathodal current, water is superior to saline, and the inhibitory effect is a function of the amperage used. To address the importance of current flowing through the pores, a layer of silicone grease was placed on the skin to reduce the shunt pathway across the epidermis. With silicone, total skin conductance decreased 60% without the sweat pores being occluded, swelling of the stratum corneum and collapse of the poral lumen was prevented, and current-induced inhibition of sweating was enhanced, most likely because of an increase in current density in the pores. The pH of anodal water, but not of saline, dropped to 3, whereas that of cathodal water increased to 10 during passage of current through the skin. Acidified anodal water was superior to alkaline water. Sweat glands isolated from TWI-induced anhidrotic palmar skin responded to methacholine in vitro, but the sweat rate and pharmacological sensitivity were slightly lowered. Thus the strong acidity generated by hydrolysis of water in the anodal bath and the further accumulation of H+ in the sweat duct by anodal current may be responsible for TWI-induced inhibition of sweating due to an unknown lesion(s) in the duct or sweat pore. The secretory coil function may also be altered because of exposure to intense acidity during TWI. The importance of H+ movement into the sweat pore for inhibition of sweating could be further exploited to develop new strategies for the control of sweating.

Hepatic Subcellular Storage of Beta-Carotene in Rats Following Diet Supplementation

1999 ◽  
Vol 69 (1) ◽  
pp. 3-7 ◽  
Author(s):  
Bianchi-Santamaria ◽  
Stefanelli ◽  
Cembran ◽  
Gobbi ◽  
Peschiera ◽  
...  
Keyword(s):  
Liver Tissue ◽  
Plasma Membranes ◽  
Beta Carotene ◽  
Subcellular Fractions ◽  
Organ Distribution ◽  
Total Liver ◽  
Opposite Behavior ◽  
The Mean ◽  
White Fat ◽  
And Storage

Beta-carotene (BC) storage was measured in liver and its subcellular fractions (plasma membranes, mitochondria, microsomes and nuclei) of rats fed BC added to diet. The BC supplementation dose was about 350 mg/week/rat. After 15 weeks of this supplementation, rats were killed and their livers were immediately excised and processed to obtain total liver tissue and its subcellular fractions. Their BC contents were measured by HPLC as pmols/mg protein. Intact BC was found to be stored in all the above subcellular fractions, thus showing that BC is probably taken up by liver cell lipid moiety. Interestingly, the mean BC concentrations in plasma membranes and mitochondria were significantly higher than that in total liver tissue. Our data confirmed that rodents are a good animal model for the study of BC metabolism and its effects on several pathologies, and cancer prevention and treatment in humans in spite of the fact that rodents are classified as white-fat animals because of their poor BC absorption and storage in fat and blood plasma, whereas humans are classified as yellow-fat organisms because of their opposite behavior in BC uptake and organ distribution.

scholarly journals Gamma-interferon modulates human monocyte/macrophage transferrin receptor expression

Blood ◽  
1988 ◽  
Vol 71 (6) ◽  
pp. 1590-1595 ◽  
Author(s):  
R Taetle ◽  
JM Honeysett
Keyword(s):  
Binding Sites ◽  
Blood Cells ◽  
Interleukin 1 ◽  
Human Monocyte ◽  
Gamma Interferon ◽  
Receptor Expression ◽  
Biologically Active ◽  
Gm Csf ◽  
Fe Content ◽  
Slot Blot Analysis

Although circulating human monocytes do not express transferrin (Tf) receptors, cultured adherent blood cells display high-affinity Tf binding sites. In the present studies, effects of various cytokines and biologically active proteins on human monocyte/macrophage Tf receptors were investigated. After culture, Tf receptor expression by adherent blood cells was time dependent and plateaued by 7 days. The addition of interleukin-1 (IL-1), alpha-interferon (alpha-IFN), granulocyte/macrophage-colony stimulating factor (GM-CSF), or human IgG to macrophages cultured for 4 days did not alter Tf receptor expression. Fe-saturated, human Tf caused a significant, dose-dependent decrease in receptor expression. At a dose of 100 U/mL, gamma- interferon (gamma-IFN) significantly increased Tf receptor expression by macrophages cultured for 4 (230% +/- 51% of control) or 7 days (150% +/- 22%). Scatchard analyses showed increased binding sites but no change in receptor affinity. Northern and slot blot analysis of cellular mRNA from macrophages cultured for 4 to 7 days and exposed to gamma-IFN showed a two- to fivefold increase in Tf receptor mRNA, but less than or equal to 30% increase in beta-actin mRNA. Ferritin content of gamma-IFN-treated macrophages was 47% to 63% of control cells. Net uptake of 59Fe from Tf by gamma-IFN-treated cells was 10% to 17% of control, but uptake of radiolabeled Tf was comparable. When macrophages were labeled with 59Fe and then exposed to gamma-IFN, cell-associated Fe was reduced by 43%, indicating that gamma-IFN caused macrophage Fe release. gamma-IFN specifically modulates Tf receptor display by inducing Fe release and reducing cellular Fe content. Regulation of Tf receptor expression in macrophages is controlled by cellular Fe content and is thus similar to regulatory mechanisms in dividing cells.

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