A Soluble Form of K-sam FGFR2 Protein in the Culture Medium of Human Gastric Cancer Cells

Kishi, Tatsuya; Yoshida, Tetsu; Terada, Masanaka

doi:10.1006/bbrc.1994.2084

Cited by 14 publications

(1 citation statement)

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“…The membrane was blocked for 1 h with phosphate-buffered saline containing 5% ovalbumin or 5% skim milk. The K-sam proteins were probed with anti-K-sam polyclonal antibody PK1-2, which was raised against a synthetic oligopeptide corresponding to the 16 amino acids just downstream of the signal peptide in the extracellular region of the K-sam-II products (26). The tyrosine-phosphorylated proteins were probed with mouse antiphosphotyrosine monoclonal antibody PY-20 (ICN) or PY-69 (ICN) or a mouse antiphosphotyrosine polyclonal antibody (Zymed) and detected by the ECL system (Amersham).…”

Section: Cells Induction Of Differentiation and Determination Of Thmentioning

confidence: 99%

A Truncated K-sam Product Lacking the Distal Carboxyl-Terminal Portion Provides a Reduced Level of Autophosphorylation and Greater Resistance against Induction of Differentiation

Ishii

Yoshida²,

et al. 1995

Molecular and Cellular Biology

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The K-sam gene was originally cloned from KATO-III human gastric cancer cells and is identical to the bek or keratinocyte growth factor (KGF) receptor (KGFR) or fibroblast growth factor receptor 2 gene. K-sam generates several variant transcripts by alternative splicing, and the most abundant K-sam transcript in KATO-III cells was cloned as the K-sam-IIC3 cDNA, which has the KGF-binding motif and a short carboxyl terminus lacking a putative phospholipase C-gamma 1 association site, Tyr-769. The K-sam-IIC3 cDNA was distinct from the K-sam-IIC1 cDNA, which was the same as the previously reported KGFR cDNA. The K-sam-IIC1 product contains a long carboxyl terminus with Tyr-769. K-sam-IIC3 showed greater transforming activity in NIH 3T3 cells than did K-sam-IIC1, and in gastric cancer cell lines in general, the level of K-sam-IIC3 mRNA was greater than that of K-sam-IIC1 mRNA. Here we report that the K-sam-IIC3 product was less autophosphorylated than the K-sam-IIC1 product in NIH 3T3 transfectants. K-sam-IIC3-transfected keratinocytes showed a stronger mitogenic response to KGF than did K-sam-IIC1 transfectants. Moreover, K-sam-IIC3-transfected L6 myoblast cells hardly differentiated when cultured in differentiation-inducing medium and growth was not significantly affected, while K-sam-IIC1 transfectants showed a differentiated phenotype with a reduced growth rate. These data indicate the difference in the signal transduction mediated by two KGFR-type K-sam variants generated by alternative splicing which might be involved in certain differentiation and carcinogenesis scenarios.

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Section: Cells Induction Of Differentiation and Determination Of Thmentioning

confidence: 99%

A Truncated K-sam Product Lacking the Distal Carboxyl-Terminal Portion Provides a Reduced Level of Autophosphorylation and Greater Resistance against Induction of Differentiation

Ishii

Yoshida²,

et al. 1995

Molecular and Cellular Biology

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Identification of a Novel Alternative Splicing of Human FGF Receptor 4: Soluble-Form Splice Variant Expressed in Human Gastrointestinal Epithelial Cells

Takaishi

Sawada

Morita

et al. 2000

Biochemical and Biophysical Research Communications

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Among four closely related members of the FGF receptor family, FGFR 1, 2, and 3 have alternative splicing forms encoded by different exons for the C-terminal half of the third Ig-like domain, but FGFR 4 has no such alternative exon. Furthermore, FGFR 1, 2, and 3 have another splice variant of nontransmembrane type; however, such a variant has not been reported for FGFR 4. While searching for a novel receptor-type tyrosine kinase by RT-PCR, we identified a non-transmembrane-type receptor of FGFR 4 in human intestinal epithelial cell lines (Intestine 407 and Caco-2). Sequence analysis of this receptor revealed that exon 9 coding the single transmembrane domain was displaced by intron 9. Consequently, this variant form was 120 bp shorter than the normal form and had no transmembrane portion. Moreover, the signal sequence in exon 2 was maintained, suggesting that this splice variant is a soluble receptor. This soluble receptor was detected in human gastrointestinal epithelial cells and pancreas, and also in gastric, colon, and pancreatic cancer cell lines. Single cell RT-PCR showed that this soluble receptor was expressed simultaneously with the transmembrane-type receptor in the same cell. Western blot analysis revealed that this receptor was secreted from the transfected COS7 cells. Thus, a soluble-form splice variant of FGFR 4 was identified in human gastrointestinal epithelial cells and cancer cells. This is the first report of alternative splicing of FGFR 4.

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Retroviruses and Oncogenes

Rasheed

1995

The Retroviridae

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A Soluble Form of K-sam FGFR2 Protein in the Culture Medium of Human Gastric Cancer Cells

Cited by 14 publications

References 0 publications

A Truncated K-sam Product Lacking the Distal Carboxyl-Terminal Portion Provides a Reduced Level of Autophosphorylation and Greater Resistance against Induction of Differentiation

A Truncated K-sam Product Lacking the Distal Carboxyl-Terminal Portion Provides a Reduced Level of Autophosphorylation and Greater Resistance against Induction of Differentiation

Identification of a Novel Alternative Splicing of Human FGF Receptor 4: Soluble-Form Splice Variant Expressed in Human Gastrointestinal Epithelial Cells

Retroviruses and Oncogenes

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