Novel function of the skin in calcium metabolism in female and male chickens (Gallus domesticus)

Peltonen, L; Sankari, Satu; Kivimäki, Anneli; Autio, Pekka

doi:10.1016/j.cbpb.2006.04.003

Cited by 3 publications

(6 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Visual inspection of the male skin reveals 'a young or hydrated skin', as it is less transparent and its stereoscopic effect ('relief') is finer and less visible than that of coeval females, similar to humans (Zahouani and Vargiolu, 2004). Male skin is also thicker and more resilient (Peltonen et al, 2006;Peltonen and Mänttäri, 2008), implying a greater mass of collagen and elastic fibres in the ground substance. Furthermore, GAGs are present in high concentrations in males, especially in the combs and wattles, hyaluronan being the main species (Nakano and Sim, 1989;Nakano and Sim, 1991).…”

Section: Discussionmentioning

confidence: 99%

Ott's protein osmotic pressure of serum and interstitial fluid in chickens (Gallus gallus): effect of age and gender

Peltonen

Sankari

2011

Journal of Experimental Biology

Self Cite

View full text Add to dashboard Cite

SUMMARY Protein, or colloid, osmotic pressure (COP) is of sufficient magnitude to exert a powerful effect on Starling forces across the capillary wall. Although avian skin lacks active mechanisms for fluid transmission, such as sweating, it is now hypothesized that passive oncotic forces may regulate fluid flow and distribution in the skin and related phenomena. In this study, serum protein profiles, as well as COP in serum (COPs) and in suction blister fluid (COPsbf), were determined in juvenile, young and adult female and male chickens. For assessing COP, the Ott-Ahlqvist equation was applied. This equation can formulate the effects of multiple serum proteins on COP, according to their molecular mass. The COP values determined in chickens were lower than those previously found in mammals. COPs increased with age in males, and was higher in adult males than in adult females. In contrast, COPsbf decreased with age in females, although it was better preserved in adult males. The age-dependent decrease in COP was associated with a parallel decrease in the concentration of α1-globulin and albumin, and a positive correlation between packed cell volume (PCV) and COP was found. It is concluded that ageing affects Ott's COP around the vessel wall, and that an oncotic mechanism preserves plasma volume. The preservation of COPsbf in males suggests better maintenance of the interstitial ground substance. Females seem to lose more of a tissue's COPs counteracting force than males, probably as a result of gender-specific changes in the composition of the interstitial matrix. Further studies are required to elucidate the structure and function of avian lymphatics and their role in skin rheology.

show abstract

Section: Discussionmentioning

confidence: 99%

Ott's protein osmotic pressure of serum and interstitial fluid in chickens (Gallus gallus): effect of age and gender

Peltonen

Sankari

2011

Journal of Experimental Biology

Self Cite

View full text Add to dashboard Cite

show abstract

“…In addition to the uterus, skin may also contain calcium microenvironments. It was shown that in a regular 'layer's diet', the amount of ionic Ca 2+ in the cutaneous interstitial fluid of male chickens started to increase after the completion of growth, while in females the Ca 2+ remained in equilibrium between these compartments until they came out of lay (Peltonen et al, 2006). As shown in cardiomyocytes, calcium overload may cause enhanced calcium entry (Katra and Laurita, 2007).…”

Section: +mentioning

confidence: 99%

“…The chickens were given intramuscular ketamine (Ketalar ® , Pfizer, Espoo, Finland) in combination with xylazine (Rompun ® , Bayer, Leverkusen, Germany) in doses of 20·mg·kg -1 and 5·mg·kg -1 , respectively. SBF was collected by the method first developed for humans by Kiistala and Mustakallio (Kiistala and Mustakallio, 1964) and modified for birds by Peltonen et al (Peltonen et al, 2006). The suction cups were attached on the thoracic apterial skin.…”

Section: Sample Collectionmentioning

confidence: 99%

“…The concentration of ionized Ca 2+ in adult chickens (stage 1) was measured with ISE (ion-selective electrodes) in fresh whole blood and in SBF as previously described by Peltonen et al (Peltonen et al, 2006). In short, to maintain pH and ion concentration stability, fresh blood samples were stored in an ice bath without exposure to air until measured, within 2-4·h (Cao et al, 2001).…”

Section: Biochemical Analysesmentioning

confidence: 99%

“…Samples were analysed with a KONE Microlyte 3 device (Thermo Electron Inc., Clinical Chemistry and Automation Systems, Vantaa, Finland). In non-layers and coeval males (stage 2), we used our previous results for reference (Peltonen et al, 2006). Plasma and SBF activity of ALP were measured by Spotchem II analysing system (Arkray Inc., Kyoto, Japan).…”

Section: Biochemical Analysesmentioning

confidence: 99%

See 2 more Smart Citations

Is there life in the horny layer? Dihydropyridine and ryanodine receptors in the skin of female and male chickens (Gallus domesticus)

Peltonen

Mänttäri

2008

Journal of Experimental Biology

Self Cite

View full text Add to dashboard Cite

SUMMARY Previous findings in pigeons and chickens show that Ca2+ may be accumulated inside the cornified skin cells and that Ca 2+ microenvironments with a lower-or higher-than-blood concentration may exist in the skin. It has been suggested that the skin may function as a secretory pathway or a reservoir for Ca 2+ recycling. To test this hypothesis, we studied the dermis and epidermis of female and male chickens in vivo to find out whether cellular mechanisms exist for the accumulation, recycling or secretion of Ca 2+. For calcium influx and intracellular Ca 2+ release, respectively, the density of dihydropyridine receptors (DHPRs) and ryanodine receptors (RyRs) was examined, using high-affinity (-)-enantiomers of dihydropyridine and ryanodine labelled with fluorophores. To investigate Ca 2+ utilization in the skin, the systemic and local activity of the enzyme alkaline phosphatase (ALP) and the concentration of ionic Ca 2+ were measured in plasma and in cutaneous extracellular fluid, collected by suction blister technique. We found that both DHPRs and RyRs were present in all skin layers from dermis to horny layer. However, receptor densities were highest in the surface layers. With a basic calcium-rich diet, receptor densities were higher in males, particularly in the dermis and mid-epidermis. After a reduction in the nutritional Ca 2+ input, receptor densities in males decreased to the same level as in females, in which the receptor densities were not affected by the amount of Ca 2+ in the diet or that resulting from coming out of lay. The extracellular concentration of ionic Ca 2+ per se was not found to affect the density of DHPRs and RyRs in the skin. Spatially, RyRs seem to be located in the periphery of the sebokeratinocyte. ALP activity was shown to be lower in the extracellular fluid than in the plasma in both sexes. However, activity in both extracellular domains increased significantly in females that had come out of lay. This was probably connected with the increased osteoblast activity related to the reformation of structural bone. In conclusion, voltage-sensitive L-type Ca 2+ channels for ion influx and RyRs for Ca 2+ release are present in the cells of the skin of female and male chickens. Higher densities in the males receiving excessive Ca 2+ imply an increased capacity for Ca 2+ influx and intracellular processing. Even though the functional interactions between DHPRs and RyRs in the sebokeratinocytes could not be demonstrated, peripheral colocation and high receptor densities at the level of exocytosis of the lamellar bodies point to their role as part of a signalling pathway for secretion. The finding that DHPRs and RyRs are present in the horny layer implies that the function of the outermost skin might be more active than had been previously thought and that this function might be both secretory and sensory.

show abstract

Calcium‐dependent inactivation of calcium channels in cochlear hair cells of the chicken

Lee

Briklin

Hiel

et al. 2007

The Journal of Physiology

View full text Add to dashboard Cite

Voltage-gated calcium channels support both spontaneous and sound-evoked neurotransmitter release from ribbon synapses of cochlear hair cells. A variety of regulatory mechanisms must cooperate to ensure the appropriate level of activity in the restricted pool of synaptic calcium channels (∼100) available to each synaptic ribbon. One potential feedback mechanism, calcium-dependent inactivation (CDI) of voltage-gated, L-type calcium channels, can be modulated by calmodulin-like calcium-binding proteins. CDI of voltage-gated calcium current was studied in hair cells of the chicken's basilar papilla (analogous to the mammalian cochlea) after blocking the predominant potassium conductances. For inactivating currents produced by 2.5 s steps to the peak of the current-voltage relation (1 mM EGTA internal calcium buffer), single exponential fits yielded an average decay time constant of 1.92 ± 0.18 s (mean ± S.E.M., n = 12) at 20-22• C, while recovery occurred with a half-time of ∼10 s. Inactivation produced no change in reversal potential, arguing that the observed relaxation did not result from alternative processes such as calcium accumulation or activation of residual potassium currents. Substitution of external calcium with barium greatly reduced inactivation, while inhibition of endoplasmic calcium pumps with t-benzohydroquinone (BHQ) or thapsigargin made inactivation occur faster and to a greater extent. Raising external calcium 10-fold (from 2 to 20 mM) increased peak current 3-fold, but did not alter the extent or time course of CDI. However, increasing levels of internal calcium buffer consistently reduced the rate and extent of inactivation. With 1 mM EGTA buffering and in 2 mM external calcium, the available pool of calcium channels was half-inactivated near the resting membrane potential (−50 mV). CDI may be further regulated by calmodulin-like calcium-binding proteins (CaBPs). mRNAs for several CaBPs are expressed in chicken cochlear tissue, and antibodies to CaBP4 label hair cells, but not supporting cells, equivalent to the pattern seen in mammalian cochlea. Thus, molecular mechanisms that underlie CDI appeared to be conserved across vertebrate species, may provide a means to adjust calcium channel open probability, and could serve to maintain the set-point for spontaneous release from the ribbon synapse.

show abstract

Novel function of the skin in calcium metabolism in female and male chickens (Gallus domesticus)

Cited by 3 publications

References 38 publications

Ott's protein osmotic pressure of serum and interstitial fluid in chickens (Gallus gallus): effect of age and gender

Ott's protein osmotic pressure of serum and interstitial fluid in chickens (Gallus gallus): effect of age and gender

Is there life in the horny layer? Dihydropyridine and ryanodine receptors in the skin of female and male chickens (Gallus domesticus)

Calcium‐dependent inactivation of calcium channels in cochlear hair cells of the chicken

Contact Info

Product

Resources

About