Acidic fibroblast growth factor (FGF) from bovine brain: amino-terminal sequence and comparison with basic FGF.

Bőhlen, Peter; Esch, Frederick; Baird, Andrew; Gospodarowicz, Denis

doi:10.1002/j.1460-2075.1985.tb03876.x

Cited by 168 publications

(68 citation statements)

References 31 publications

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“…These differences are summarized in table 1. The high degree of structural homology (97.9%) thus far observed for bFGFs implies a strong evolutionary selection pressure for maintenance of biological function and is consistent with the biological cross-reactivity across species of bFGF [3,9,10]. In contrast to the cDNAdeduced primary structures reported for bovine [6] and human bFGF [5], the ovine bFGF structure reported in fig.1 lacks a 9-residue amino acid terminal extension.…”

Section: Resultssupporting

confidence: 58%

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Primary structure of ovine pituitary basic fibroblast growth factor

et al. 1987

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The complete amino acid sequence of basic FGF (146 residues) from ovine pituitary glands has been established. This has been achieved by the sequence analysis of subnanomole amounts of the intact molecule and of peptides derived by enzymatic digestions with clostripain, chymotrypsin, pepsin and Staphylococcus aureus V8 protease. Microbore HPLC, employing 1-2 mm i.d. columns, was used to purify, concentrate and buffer-exchange the FGF peptides. A novel application of ion-pairing chromatography was employed to isolate peptides which were not retained on conventional reversed-phase systems. There is only one positional difference between the ovine and bovine basic FGFs, but there are 3 positional differences between ovine and human basic FGFS.

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Section: Resultssupporting

confidence: 58%

“…Ovine bFGF was prepared from pituitary glands as in [4,10]. bFGF mitogenic activity was determined using mouse 3T3 fibroblasts as described [11].…”

Section: Basic Fgf Isolationmentioning

confidence: 99%

Primary structure of ovine pituitary basic fibroblast growth factor

et al. 1987

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“…It is apparent from the deduced sequence of int-1 protein (7,34) and the results presented in these papers that int-1 does not belong to proto-oncogene families that encode nuclear proteins, tyrosine or serine-threonine kinases, or signal-transducing GTPases (35), but int-I can be grouped with other genes and their relatives that encode secreted growth and differentiation factors, such as TGF-,B (25), platelet-derived growth factor (10), fibroblast growth factor (1,9), transforming growth factor cx (26), or granulocytemacrophage colony-stimulating factor (13). Functional and structural studies of int-1 proteins, including a search for cell surface receptors specific for int-1 products, will be required to evaluate this assignment.…”

Section: Discussionmentioning

confidence: 99%

The int-1 proto-oncogene products are glycoproteins that appear to enter the secretory pathway.

Papkoff¹,

Brown²,

Varmus³

1987

Mol. Cell. Biol.

129

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The int-l proto-oncogene encodes a primary product of 370 amino acids, is normally expressed in mid-gestational embryos and adult testis, and is activated by proviral insertions during mammary carcinogenesis. Polyclonal and monoclonal antibodips directed against int-l-specific synthetic peptides immunoprecipitate up to five forms of int-l protein, ranging in size from 36,000 to 44,000 Mr, from cell lines that express cloned int-l DNA introduced by transfection or infection with retroviral vectors. Pulse-chase labeling experiments and glycosidase digestions suggested that the smallest of the int-l proteins is the primary translation product lacking its signal peptide and that it is modified to produce the larger species'of sequential glycosylation. Subcellular fractionations demonstrated that all immunoprecipitable forms of int-l are mainly associated with membranes. int-l proteins in crude microsomal preparations are resistant to proteolysis and extractable at elevated pH, suggesting that they are sequestered within cytoplasmic vesicles in a manner consistent with the behavior of secretory products. However, we were unable to identify secreted int-i products in extracellular fluids.The int-1 proto-oncogene was discovered as a target for insertional activation of transcription in mammary carcinomas induced by the mouse mammary tumor virus (18, 19), and it is expressed in normal mice only in the neural tube of the mid-gestational embryo and in postmeiotic cells in the mature testis (12,28,37). We are attempting to identify, characterize, and determine the subcellular location of the protein products of int-1 to understand the function of this unusual proto-oncogene.In the accompanying report, we describe the identification of the int-i-encoded proteins p36, p38, p40, and p42 by immunoprecipitation of radiolabeled proteins from lysates of cells bearing int-i expression vectors, using antibodies directed against different int-i-specific peptides (2). Only the int-1 product p36 was immunoprecipitated after cells were labeled in the presence of tunicamycin, suggesting that the three larger forms are glycosylated.In this report, we further characterize these four and one additional int-1 protein, p44, and determine their subcellular location. The higher-molecular-weight forms have the sensitivity to glycosidases expected of proteins with N-linked glycosylations and, based on kinetic labeling studies, appear to represent sequentially modified forms of p36, the unglycosylated product. While we did not identify an int-1 product in the culture medium of these cells, we demonstrated that the intracellular forms of int-1 protein have the'subcellular location expected of a secretory product.MATERIALS AND METHODS Cells and antibodies. The derivations of the 7dT and MV7int-1/3T3 cell lines that express int-1 cDNA have been described previously (3). MV7int-1/3T3 cells were infected with clone 1 murine leukemia virus (MLV) (6) The monoclonal and polyclonal antisera directed against int-i-specific peptides as well as the'control ...

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“…All other products were purchased from Sigma (St. Louis, MO). Basic FGF was purified from bovine brain as in [11,12]. Lipocortin from pig lung was prepared as in [13] and kindly provided by Drs Josette Fauvel and Hugues Chap 0d 101 INSERM, Toulouse).…”

Section: Methodsmentioning

confidence: 99%

Influence of fibroblast growth factor on phosphorylation and activity of a 34 kDa lipocortin‐like protein in bovine epithelial lens cells

1988

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We examined the effect of basic fibroblast growth factor (FGF) on phosphorylation and lipocortin-like activity of the 34 kDa protein present in the basal membrane of epithelial peripheral cells which initiate growth and differentiation in the bovine lens. We found that: (i) the 34 kDa protein possesses anti-phospholipase A 2 (PL/%) activity of lipocortin; (ii) in response to FGF, the anti-PLA 2 activity of this protein is enhanced whereas its phosphorylation is markedly decreased. It is suggested that the 34 kDa protein might represent an important biological activity in controlling FGF induction of growth and differentiation in the adult eye lens.

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Acidic fibroblast growth factor (FGF) from bovine brain: amino-terminal sequence and comparison with basic FGF.

Cited by 168 publications

References 31 publications

Primary structure of ovine pituitary basic fibroblast growth factor

Primary structure of ovine pituitary basic fibroblast growth factor

The int-1 proto-oncogene products are glycoproteins that appear to enter the secretory pathway.

Influence of fibroblast growth factor on phosphorylation and activity of a 34 kDa lipocortin‐like protein in bovine epithelial lens cells

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