The maturation of cortisone-treated embryonic duodenum in vitro. I. The villus

Development ◽  
1965 ◽  
Vol 14 (2) ◽  
pp. 161-168
Author(s):  
Raymond L. Hayes
Keyword(s):  
Alkaline Phosphatase ◽  
Chick Embryo ◽  
Enzymatic Activity ◽  
Physiological Activity ◽  
Muscle Fibers ◽  
Circular Muscle ◽  
Luminal Surface ◽  
Embryonic Chick ◽  
Duodenal Epithelium

Mitotic expansion of the mucosa coupled with contraction of intrinsic longitudinal and circular muscle fibers produces previllous ridges on the luminal surface of the embryonic chick duodenum by the thirteenth day of incubation. Subsequently, remodelling by periodic indentation of the mucosal surface yields primitive villi which expand and elongate to form the tall, finger-like projections characterizing the absorptive surface of the mature duodenum (Hilton, 1902; Pap, 1933; Coulombre & Coulombre, 1958). Coincident with the morphogenesis of the villus is the acquisition of enzymatic activity in its epithelium. As early as the 14th day of incubation of the chick embryo, alkaline phosphatase is detectable in the epithelial free border of the duodenum (Hancox & Hyslop, 1954), although other investigators report later appearances for this enzyme (Moog, 1950; Hébert, 1950). The onset of this physiological activity in the duodenal epithelium may be accelerated by exposure to adrenocorticoids as originally postulated by Hébert (1950).

scholarly journals Chick embryo anchored alkaline phosphatase and mineralization process in vitro. Influence of Ca2+ and nature of substrates

2003 ◽  
Vol 270 (9) ◽  
pp. 2082-2090 ◽  
Author(s):  
Eva Hamade ◽  
Gerard Azzar ◽  
Jacqueline Radisson ◽  
Rene Buchet ◽  
Bernard Roux
Keyword(s):  
Alkaline Phosphatase ◽  
Chick Embryo ◽  
Mineralization Process

scholarly journals In vitro stimulation of alkaline phosphatase activity in immature embryonic chick pelvic cartilage by adenosine

1982 ◽  
Vol 93 (2) ◽  
pp. 338-342 ◽  
Author(s):  
WM Burch ◽  
HE Lebovitz
Keyword(s):  
Alkaline Phosphatase ◽  
Cyclic Amp ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Maximal Response ◽  
Embryonic Chick ◽  
In Ovo ◽  
Developmental Age ◽  
Stimulation Of

Cyclic AMP content in embryonic chick pelvic cartilage increases significantly as the embryo ages from 8 to 10 d. This in ovo elevation in cyclic AMP content precedes maximal cartilage alkaline phosphatase activity by some 24 h. We studied whether this temporal relationship may be causally related, using an in vitro organ culture. Incubation of pelvic cartilage from 9- and 10-d embryos in medium containing monobutyryl cyclic AMP (BtcAMP) resulted in significant increases in alkaline phosphatase activity (220 and 66 percent, respectively) as compared to that of cartilages incubated in medium alone. This stimulation was both concentration- and time-dependent with maximal response at 0.5 mM BtcAMP and 4-h incubation, respectively. Similar incubations of cartilage in medium containing 1-methyl-3-isobutyl xanthine (MIX), 0.25 mM, also resulted in increased alkaline phosphatase activity (114 percent). However, pelvic cartilage from 11-d embryos incubated in medium containing BtcAMP or MIX showed no increase in alkaline phosphatase activity. We postulated that developmental age was the factor responsible for this difference in response and that immature cartilage (that with little or no alkaline phosphatase activity) would respond to BtcAMP whereas mature cartilage (that with significant alkaline phosphatase activity) would not. This was tested by incubating end sections of 11-d cartilage, which have little alkaline phosphatase activity, and center sections, which have significantly alkaline phosphatase activity, with both BtcAMP and MIX. Alkaline phosphatase activity in end sections (immature cartilage) was stimulated by BtcAMP and MIX, whereas it was not stimulated in the center sections. Actinomycin D and cycloheximide inhibited BtcAMP and MIX stimulation of alkaline phosphatase activity. Thus, the in vitro data suggest that cyclic AMP is a mediator for the stimulation of alkaline phosphatase activity in embryonic cartilage.

An Immunoembryological Study of the Chick Iris

Development ◽  
1963 ◽  
Vol 11 (3) ◽  
pp. 483-491
Author(s):  
Harry Maisel ◽  
Charles Harmison
Keyword(s):  
Chick Embryo ◽  
Embryonic Chick ◽  
Vertebrate Species ◽  
Immunological Analysis ◽  
Lens Regeneration ◽  
Lens Cells ◽  
Alpha Beta ◽  
Common Antigens

Using immunological techniques it has been shown that in all major vertebrate species the lens, iris and pigment retina of the eye share common antigens (Langman & Prescott, 1959; Maisel & Langman, 1961; Flickinger & Stone, 1960; Maisel, 1962). These data are of particular interest since in certain animals the iris has the ability to form a lens or lens cells in the absence of the original lens. Indeed, lens regeneration from the dorsal iris is well documented in the genus Triturus (Stone, 1952; Reyer, 1954). Although McKeehan (1961) and Woerdeman (1962) did not record lens regeneration in the chick embryo in vivo, other observers have reported on the formation of lens cells from embryonic chick pigment retina and iris explanted in vitro (Dorris, 1938; van Deth, 1940; Reinhold, 1958). Immunological analysis of the chick iris and pigment retina using anti-lens serum has revealed that these tissues contain proteins with antigenic (surface reactive) groupings similar to lens alpha, beta and gamma crystallins.

Diazepam induces relaxation of chick embryo muscle fibers in vitro and inhibits myosin synthesis

1979 ◽  
Vol 123 (2) ◽  
pp. 285-291 ◽  
Author(s):  
Charles R. Walker ◽  
Everett Bandman ◽  
Richard C. Strohman
Keyword(s):  
Chick Embryo ◽  
Muscle Fibers

scholarly journals Purified lectin from skeletal muscle inhibits myotube formation in vitro.

1980 ◽  
Vol 85 (3) ◽  
pp. 617-625 ◽  
Author(s):  
R G MacBride ◽  
R J Przybylski
Keyword(s):  
Skeletal Muscle ◽  
Chick Embryo ◽  
Culture Medium ◽  
Horse Serum ◽  
Pectoral Muscle ◽  
Embryonic Chick ◽  
Myotube Formation ◽  
Chick Embryo Extract ◽  
Muscle Cultures

A lactose-extractable lectin obtained from 14--16-d embryonic chick pectoral muscle and myotube muscle cultures by affinity chromatography inhibited myotube formation in culture. When applied to muscle cultures at 0.09 micrograms/ml, the purified lectin produced variable effects on the inhibition of myotube formation related to the time and length of application, suggesting that components of the culture medium and/or temperature produced inactivation. Hemagglutination assays showed that the lectin was inactivated by horse serum and by chick embryo extract but not by L-15 salt solution at 4 degrees C. Incubation in L-15 solution at 37 degrees C with or without 2 mM dithiothreitol resulted in inactivation in 2--3 h. To maximize the effect of the lectin on the inhibition of myotube formation, primary muscle cultures were grown in low [Ca+2] medium to inhibit fusion, and then [Ca+2] was increased to elicit fusion in the absence and presence of lectin with solution renewal every 2 h. Without lectin, myotube formation was normal, whereas, with lectin, it was inhibited by 93%. Continued incubation at 37 degrees C. without renewal of lectin resulted in myotube formation, suggesting reversibility by lectin inactivation.

In Situ Localization of PPAR Gamma and Uncoupling Protein in Mouse Embryo Sections Using Digoxigenin-Labeled Riboprobes

1996 ◽  
Vol 54 ◽  
pp. 32-33
Author(s):  
C. Jennermann ◽  
S. A. Kliewer ◽  
D. C. Morris
Keyword(s):  
Alkaline Phosphatase ◽  
Room Temperature ◽  
Uncoupling Protein ◽  
Ppar Gamma ◽  
Nuclear Hormone Receptor ◽  
Full Length ◽  
Northern Analysis ◽  
Peroxisome Proliferator

Peroxisome proliferator-activated receptor gamma (PPARg) is a member of the nuclear hormone receptor superfamily and has been shown in vitro to regulate genes involved in lipid metabolism and adipocyte differentiation. By Northern analysis, we and other researchers have shown that expression of this receptor predominates in adipose tissue in adult mice, and appears first in whole-embryo mRNA at 13.5 days postconception. In situ hybridization was used to find out in which developing tissues PPARg is specifically expressed.Digoxigenin-labeled riboprobes were generated using the Genius™ 4 RNA Labeling Kit from Boehringer Mannheim. Full length PPAR gamma, obtained by PCR from mouse liver cDNA, was inserted into pBluescript SK and used as template for the transcription reaction. Probes of average size 200 base pairs were made by partial alkaline hydrolysis of the full length transcripts. The in situ hybridization assays were performed as described previously with some modifications. Frozen sections (10 μm thick) of day 18 mouse embryos were cut, fixed with 4% paraformaldehyde and acetylated with 0.25% acetic anhydride in 1.0M triethanolamine buffer. The sections were incubated for 2 hours at room temperature in pre-hybridization buffer, and were then hybridized with a probe concentration of 200μg per ml at 70° C, overnight in a humidified chamber. Following stringent washes in SSC buffers, the immunological detection steps were performed at room temperature. The alkaline phosphatase labeled, anti-digoxigenin antibody and detection buffers were purchased from Boehringer Mannheim. The sections were treated with a blocking buffer for one hour and incubated with antibody solution at a 1:5000 dilution for 2 hours, both at room temperature. Colored precipitate was formed by exposure to the alkaline phosphatase substrate nitrobluetetrazoliumchloride/ bromo-chloroindlylphosphate.

Electron microscopic study of the membrane glycoproteins in the rat kidney after cisplatin treatment

1989 ◽  
Vol 47 ◽  
pp. 912-913
Author(s):  
S.K. Aggarwal
Keyword(s):  
Alkaline Phosphatase ◽  
Rat Kidney ◽  
Light And Electron Microscopy ◽  
Kidney Tissue ◽  
Membrane Glycoproteins ◽  
Electron Microscopic ◽  
Before And After ◽  
Interstrand Cross Links ◽  
Cross Links

The proposed primary mechanism of action of the anticancer drug cisplatin (Cis-DDP) is through its interaction with DNA, mostly through DNA intrastrand cross-links or DNA interstrand cross-links. DNA repair mechanisms can circumvent this arrest thus permitting replication and transcription to proceed. Various membrane transport enzymes have also been demonstrated to be effected by cisplatin. Glycoprotein alkaline phosphatase was looked at in the proximal tubule cells before and after cisplatin both in vivo and in vitro for its inactivation or its removal from the membrane using light and electron microscopy.Outbred male Swiss Webster (Crl: (WI) BR) rats weighing 150-250g were given ip injections of cisplatin (7mg/kg). Animals were killed on day 3 and day 5. Thick slices (20-50.um) of kidney tissue from treated and untreated animals were fixed in 1% buffered glutaraldehyde and 1% formaldehyde (0.05 M cacodylate buffer, pH 7.3) for 30 min at 4°C. Alkaline phosphatase activity and carbohydrates were demonstrated according to methods described earlier.

STEROID HORMONE METABOLISM IN RESPONSIVE TISSUES IN VITRO

1971 ◽  
Vol 68 (1_Suppl) ◽  
pp. S279-S294 ◽  
Author(s):  
Paul Robel
Keyword(s):  
Steroid Hormone ◽  
Physiological Activity ◽  
Physiological State ◽  
Target Cells ◽  
Target Tissue ◽  
Hormone Metabolism ◽  
Metabolizing Enzymes ◽  
Relationship Of

ABSTRACT Of the information available on steroid hormone metabolism in responsive tissues, only that relating hormone metabolism to physiological activity is reviewed, i. e. metabolite activity in isolated in vitro systems, binding of metabolites to target tissue receptors, specific steroid hormone metabolizing enzymes and relationship of hormone metabolism to target organ physiological state. Further, evidence is presented in the androgen field, demonstrating 5α-reduced metabolites, formed inside the target cells, as active compounds. This has led to a consideration of testosterone as a »prehormone«. The possibility that similar events take place in tissues responding to progesterone is discussed. Finally, the role of hormone metabolism in the regulation of hormone availability and/or renewal in target cells is discussed. In this context, reference is made to the potential role of plasma binding proteins and cytosol receptors.

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