High-level production of human type I collagen in the yeastPichia pastoris

Yeast ◽  
2001 ◽  
Vol 18 (9) ◽  
pp. 797-806 ◽  
Author(s):  
Minna Nokelainen ◽  
Hongmin Tu ◽  
Annamari Vuorela ◽  
Holger Notbohm ◽  
Kari I. Kivirikko ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Human Type ◽  
High Level ◽  
Level Production

scholarly journals Functional analysis of cis-acting DNA sequences controlling transcription of the human type I collagen genes.

1990 ◽  
Vol 265 (22) ◽  
pp. 13351-13356
Author(s):  
S Boast ◽  
M W Su ◽  
F Ramirez ◽  
M Sanchez ◽  
E V Avvedimento
Keyword(s):  
Functional Analysis ◽  
Dna Sequences ◽  
Type I Collagen ◽  
Type I ◽  
Cis Acting ◽  
Human Type ◽  
Collagen Genes

Regulatory elements in the 5'-flanking region and the first intron contribute to transcriptional control of the mouse alpha 1 type I collagen gene

1989 ◽  
Vol 9 (5) ◽  
pp. 2224-2227
Author(s):  
R A Rippe ◽  
S I Lorenzen ◽  
D A Brenner ◽  
M Breindl
Keyword(s):  
Transcriptional Control ◽  
Type I Collagen ◽  
Regulatory Elements ◽  
Regulatory Sequences ◽  
Type I ◽  
Col1a1 Gene ◽  
First Intron ◽  
Flanking Region ◽  
Specific Regulation ◽  
High Level

We have identified two blocks of regulatory sequences located in the 5'-flanking region and the first intron of the mouse alpha 1 type I collagen (COL1A1) gene. Both blocks were found to contain positive as well as negative regulatory elements. Sequences located within 222 base pairs upstream of the transcription start site showed a strong stimulatory effect on the COL1A1 promoter and were sufficient for tissue-specific regulation of the COL1A1 gene. The combined upstream and intron regulatory sequences showed a marked inhibition of COL1A1 promoter activity in fibroblasts. This finding suggests that additional, more remote regulatory sequences may be required for establishing the high level of activity of the endogenous COL1A1 gene in fibroblastoid cells.

scholarly journals A Novel Role of Annexin A2 in Human Type I Collagen Gene Expression

2015 ◽  
Vol 116 (3) ◽  
pp. 408-417 ◽  
Author(s):  
Georgia Schäfer ◽  
Jessica K. Hitchcock ◽  
Tamlyn M. Shaw ◽  
Arieh A. Katz ◽  
M. Iqbal Parker
Keyword(s):  
Gene Expression ◽  
Type I Collagen ◽  
Annexin A2 ◽  
Type I ◽  
Collagen Gene ◽  
Human Type ◽  
Collagen Gene Expression

Association of Functional Microsatellites in the Human Type I Collagen α2 Chain (COL1A2) Gene with Systemic Sclerosis

2000 ◽  
Vol 272 (1) ◽  
pp. 36-40 ◽  
Author(s):  
Ryu-Ichiro Hata ◽  
Jun Akai ◽  
Akinori Kimura ◽  
Osamu Ishikawa ◽  
Masataka Kuwana ◽  
...  
Keyword(s):  
Systemic Sclerosis ◽  
Type I Collagen ◽  
Type I ◽  
Human Type ◽  
Col1a2 Gene

scholarly journals Molecular Mechanochemistry: Low Force Switch Slows Enzymatic Cleavage of Human Type I Collagen Monomer

2011 ◽  
Vol 133 (11) ◽  
pp. 4073-4078 ◽  
Author(s):  
Robert J. Camp ◽  
Melody Liles ◽  
John Beale ◽  
Nima Saeidi ◽  
Brendan P. Flynn ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Enzymatic Cleavage ◽  
Human Type

scholarly journals Separate cis-acting DNA elements of the mouse pro-alpha 1(I) collagen promoter direct expression of reporter genes to different type I collagen-producing cells in transgenic mice.

1995 ◽  
Vol 129 (5) ◽  
pp. 1421-1432 ◽  
Author(s):  
J Rossert ◽  
H Eberspaecher ◽  
B de Crombrugghe
Keyword(s):  
Transgenic Mice ◽  
Type I Collagen ◽  
Cell Types ◽  
Proximal Promoter ◽  
Type I ◽  
High Level Expression ◽  
Cis Acting ◽  
High Level ◽  
Different Cell Types ◽  
Beta Galactosidase

The genes coding for the two type I collagen chains, which are active selectively in osteoblasts, odontoblasts, fibroblasts, and some mesenchymal cells, constitute good models for studying the mechanisms responsible for the cell-specific activity of genes which are expressed in a small number of discrete cell types. To test whether separate genetic elements could direct the activity of the mouse pro-alpha 1(I) collagen gene to different cell types in which it is expressed, transgenic mice were generated harboring various fragments of the proximal promoter of this gene cloned upstream of the Escherichia coli beta-galactosidase gene. During embryonic development, X-gal staining allows for the precise identification of the different cell types in which the beta-galactosidase gene is active. Transgenic mice harboring 900 bp of the pro-alpha 1(I) proximal promoter expressed the transgene at relatively low levels almost exclusively in skin. In mice containing 2.3 kb of this proximal promoter, the transgene was also expressed at high levels in osteoblasts and odontoblasts, but not in other type I collagen-producing cells. Transgenic mice harboring 3.2 kb of the proximal promoter showed an additional high level expression of the transgene in tendon and fascia fibroblasts. The pattern of expression of the lacZ transgene directed by the 0.9- and 2.3-kb pro-alpha 1(I) proximal promoters was confirmed by using the firefly luciferase gene as a reporter gene. The pattern of expression of this transgene, which can be detected even when it is active at very low levels, paralleled that of the beta-galactosidase gene. These data strongly suggest a modular arrangement of separate cell-specific cis-acting elements that can activate the mouse pro-alpha(I) collagen gene in different type I collagen-producing cells. At least three different types of cell-specific elements would be located in the first 3.2 kb of the promoter: (a) an element that confers low level expression in dermal fibroblasts; (b) a second that mediates high level expression in osteoblasts and odontoblasts; and (c) one responsible for high level expression in tendon and fascia fibroblasts. Our data also imply that other cis-acting cell-specific elements which direct activity of the gene to still other type I collagen-producing cells remain to be identified.

Radioimmunoassay of the carboxyterminal propeptide of human type I procollagen

1990 ◽  
Vol 36 (7) ◽  
pp. 1328-1332 ◽  
Author(s):  
J Melkko ◽  
S Niemi ◽  
L Risteli ◽  
J Risteli
Keyword(s):  
Type I Collagen ◽  
Soft Tissues ◽  
Polyacrylamide Gel Electrophoresis ◽  
Primary Cultures ◽  
Sodium Dodecyl ◽  
Type I ◽  
Lectin Affinity Chromatography ◽  
Human Type ◽  
Serum Antigen ◽  
Type I Procollagen

Abstract Type I collagen is the most abundant collagen type in soft tissues and the only type found in mineralized bone. We established a rapid equilibrium radioimmunoassay for the carboxyterminal propeptide of human type I procollagen (PICP), to be used as an indicator of the synthesis of type I collagen. We isolated type I procollagen from the medium of primary cultures of human skin fibroblasts, digested the protein with highly purified bacterial collagenase, and purified PICP by lectin-affinity chromatography, gel filtration, and ion-exchange separation on HPLC. The purity of the protein was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by N-terminal amino acid sequencing of its component chains. The final radioimmunoassay was established with polyclonal rabbit antibodies. Material antigenically related to PICP is readily detected in human serum. There is only one form of the serum antigen, its molecular size and affinity to the antibodies being similar to those of the isolated propeptide. Intra- and interassay CVs are 3% and 5%, respectively. Preliminary reference intervals for healthy adults (18 to 61 years of age) are 38-202 micrograms/L for men and 50-170 micrograms/L for women: in men the concentration is inversely related to age. The serum antigen is stable during storage and after repeated thawing.

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