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Histological observations on the failure of rachitic rat bones to respond to 1,25/OH)2D3 (1980)

Gallagher, J. A. ; Lawson, D. E. M.

Springer

Calcified tissue international 31 (1980), S. 215-223

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ISSN: 1432-0827

Keywords: Bone ; 1,25(OH)2D3 ; 25OHD3 ; Histology

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Physics

Notes: Summary Rachitic rats, maintained on diets with low or normal P contents, were given daily intraperitoneal doses of 1,25(OH)2D3 or 25OHD3 at levels of 100 or 200 ng. Plasma chemistry was measured and the ash content and histological appearance of the bones investigated. Using labeled material it was shown that the dosing levels of 1,25(OH)2D3 employed ensured a higher than normal plasma concentration of that metabolite over the period between doses. 1,25(OH)2D3 was not as effective as 25OHD3 in raising bone ash or reducing the amount of osteoid. The difference between the effects of the metabolites was evident at both dietary P levels, but more marked at the higher P level. In contrast, the metabolites reduced the width of the epiphyseal plate to an approximately similar degree, and this is possibly the reason why there are discrepancies between previous reports of the effectiveness of 1,25(OH)2D3 compared with 25OHD3 or vitamin D3. Dosing with 1,25(OH)2D3 failed to maintain a constant plasma Pi value over the period between doses in animals fed the low P diet.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02407184

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Cloning and sequencing of cDNAs encoding the actin cross-liking protein transgelin defines a new family of actin-associated proteins (1994)

Prinjha, R. K. ; Shapland, C. E. ; Hsuan, J. J. ; [et al.]

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 28 (1994), S. 243-255

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ISSN: 0886-1544

Keywords: cytoskeleton ; actin binding ; transgelin sequence ; gelation ; gene family ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: We have used degenerate oligonucleotides, derived from the amino acid sequence of transgelin peptides [Shapland et al., 1993: J. Cell Biol. 121:1065-1073], to isolate and sequence overlapping cDNA clones encoding this actin gelling protein. Primers with 5′ restriction enzyme sites directed against the N and C terminal amino acids present in these clones were then used to amplify and clone the entire transgelin coding region from reverse transcribed rat small intestine cDNA (RT-PCR). These studies have shown that transgelin is the product of a single gene which is conserved between yeast, Drosophila, molluscs, and humans. Transgelin is expressed as a single message that is regulated at the level of transcription in SV40 transformed 3T3 cells. Our data have shown that transgelin and several other proteins of unknown function, SM22α [Pearlstone et al., 1987: J. Biol. Chem. 262:5985-5991], mouse p27 [Almendral et al., 1989: Exp. Cell Res. 181:518-530], and human WS3-10 [Thweatt et al., 1992: Biochem. Biophys. Res. Commun. 187:1-7], share extensive homology. More limited regions of homology shared between transgelin and other proteins such as rat NP25 (unpublished), chicken calponins α and β [Takahashi and Nadal-Ginard, 1991: J. Biol. Chem. 266:13284-13288], and Drosophila mp20 [Ayme-Southgate et al., 1989: J. Cell Biol. 108:521-531] suggest that all of these proteins may be classified as members of a new transgelin multigene family. © 1994 Wiley-Liss, Inc.

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