Tissue‐nonspecific alkaline phosphatase participates in the establishment and growth of feather germs in embryonic chick skin cultures

Crawford, Karen; Weissig, Helge; Binette, François; Millán, José Luis; Goetinck, Paul F.

doi:10.1002/aja.1002040107

Cited by 11 publications

(7 citation statements)

References 45 publications

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“…In control combinations of chick skin epithelium and skin mesenchyme, mesenchymal AP activity was detected weakly in only 1 case of 20 in the feather germs that formed (Table 1), probably because feather germ AP activity is heat labile and therefore inactivated during embedding (32,34). Weak epithelial AP staining also was observed in five cases, including that in which the weak mesenchymal activity was observed (Table 1).…”

Section: Induction Of Distinct Epithelial Appendages In Heterotypic mentioning

confidence: 85%

“…The molecular markers we have used, Shh and AP, although consistent with a tooth fate, both are expressed in other developmental contexts, including developing feather germs (32,34). Although the structures that formed in the heterotypic recombinants do not resemble feather germs nor do they express the same heat-stable AP isoform, these markers are general to other epithelial-mesenchymal interactions.…”

Section: Discussionmentioning

confidence: 99%

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Conservation of early odontogenic signaling pathways in Aves

Chen

Zhang

Jiang

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

122

139

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Teeth have been missing from birds (Aves) for at least 60 million years. However, in the chick oral cavity a rudiment forms that resembles the lamina stage of the mammalian molar tooth germ. We have addressed the molecular basis for this secondary loss of tooth formation in Aves by analyzing in chick embryos the status of molecular pathways known to regulate mouse tooth development. Similar to the mouse dental lamina, expression of Fgf8, Pitx2, Barx1, and Pax9 defines a potential chick odontogenic region. However, the expression of three molecules involved in tooth initiation, Bmp4, Msx1, and Msx2, are absent from the presumptive chick dental lamina. In chick mandibles, exogenous bone morphogenetic protein (BMP) induces Msx expression and together with fibroblast growth factor promotes the development of Sonic hedgehog expressing epithelial structures. Distinct epithelial appendages also were induced when chick mandibular epithelium was recombined with a tissue source of BMPs and fibroblast growth factors, chick skin mesenchyme. These results show that, although latent, the early signaling pathways involved in odontogenesis remain inducible in Aves and suggest that loss of odontogenic Bmp4 expression may be responsible for the early arrest of tooth development in living birds.

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Section: Induction Of Distinct Epithelial Appendages In Heterotypic mentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Conservation of early odontogenic signaling pathways in Aves

Chen

Zhang

Jiang

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

122

139

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“…Four distinct genes encoding ALP have been identified in mammals, whereas two of these forms, IAP and TNAP, have been reported in birds (26). In DT40 cells, the TNAP mRNA alone was detected by RT-PCR and ALP activity in DT40 cells was completely inhibited by levamisole, a specific inhibitor of TNAP, which indicated that DT40 cells exclusively express TNAP of ALPs.…”

Section: Znt5 and Znt7 Are Essential For Alp Activitymentioning

confidence: 86%

Zinc Transporters, ZnT5 and ZnT7, Are Required for the Activation of Alkaline Phosphatases, Zinc-requiring Enzymes That Are Glycosylphosphatidylinositol-anchored to the Cytoplasmic Membrane

Suzuki

Ishihara

Migaki

et al. 2005

Journal of Biological Chemistry

154

144

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Numerous proteins are properly folded by binding with zinc during their itinerary in the biosynthetic-secretory pathway. Several transporters have been implicated in the zinc entry into secretory compartments from cytosol, but their precise roles are poorly understood. We report here that two zinc transporters (ZnT5 and ZnT7) localized in the secretory apparatus are responsible for loading zinc to alkaline phosphatases (ALPs) that are glycosylphosphatidylinositol-anchored membrane proteins exposed to the extracellular site. Disruption of the ZnT5 gene in DT40 cells decreased the ALP activity to 45% of that in the wild-type cells. Disruption of the ZnT7 gene lowered the ALP activity only by 20%. Disruption of both genes markedly decreased the ALP activity to <5%. Overexpression of human ZnT5 or ZnT7 in DT40 cells deficient in both ZnT5 and ZnT7 genes recovered the ALP activity to the level comparable to that in the wild-type cells. The inactive ALP protein in DT40 cells deficient in both ZnT5 and ZnT7 genes was transported to cytoplasmic membrane like the active ALP protein in the wild-type cells. Thus both ZnT5 and ZnT7 contribute to the conversion of apo-ALP to holo-ALP.

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“…These processes are most probably confined to the dermis because the activity measured in the epidermis was found to be less than 1% of the activity of the underlying dermis (Mier and van Rennes, 1982). In general, the cutaneous ALP seems to be of a tissue-non-specific type, present in the dermal condensations of developing feather germs, hair follicles, capillaries and sweat glands (Mier and van Rennes, 1982;Crawford et al, 1995;Saga and Morimoto, 1995). Furthermore, it is present in both a soluble and a membrane-bound form (Mier and van Rennes, 1982).…”

Section: M Peltonen and S Mänttärimentioning

confidence: 99%

“…Plasma ALP activity has been associated with boneforming activity by osteoblasts, and with other tissues that have high cellular turnover (Bell, 1971). Since the tissue-non-specific ALP is synthesized in the skin (Yamashita et al, 1987;Crawford et al, 1995;Hui and Tenenbaum, 1995), and may be involved in physiological and pathological mineralization in tissues other than bone or cartilage (Hui et al, 1997), we also measured its activity in the cutaneous interstitial fluid.…”

Section: +mentioning

confidence: 99%

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

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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.

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Tissue‐nonspecific alkaline phosphatase participates in the establishment and growth of feather germs in embryonic chick skin cultures

Cited by 11 publications

References 45 publications

Conservation of early odontogenic signaling pathways in Aves

Conservation of early odontogenic signaling pathways in Aves

Zinc Transporters, ZnT5 and ZnT7, Are Required for the Activation of Alkaline Phosphatases, Zinc-requiring Enzymes That Are Glycosylphosphatidylinositol-anchored to the Cytoplasmic Membrane

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

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