<b>Vertebrate non‐receptor protein–tyrosine kinase families</b>

Neet, Kellie; Hunter, Tony

doi:10.1046/j.1365-2443.1996.d01-234.x

Cited by 139 publications

(102 citation statements)

References 119 publications

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“…Adam et al [28] have reported TIAM1as a target of Heregulin-beta 1 signaling and related to inhibition or promotion of cell migration in a cell type-dependent manner. The rest of the table lists other proteins that have been associated with breast and related cancer such as the oncoproteins n-myc and a-myb from the c-myc gene and the ras related proteins RAB-9L and RAB-6B [1][2][3][4][5]. Other protein markers of potential interest such as DAP-kinase, mitogen-activated kinase, TNF, tumor-specific antigen, and focal adhesion kinase are also listed.…”

Section: Resultsmentioning

confidence: 99%

“…A clear example of a successful marker is the use of HER-2 human receptor protein kinase, or c-ERBB-2 in breast cancer. This protein was originally discovered as a receptor tyrosine kinase (RTK) that is related to the epidermal growth factor receptor (EGFR) and subsequently found to be an oncoprotein for breast cancer [1,5]. Slamon et al [6] have shown that HER-2 overexpression is associated with significantly poorer prognosis in node-positive breast cancer patients.…”

Section: Introductionmentioning

confidence: 99%

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An approach to the proteomic analysis of a breast cancer cell line (SKBR‐3)

Wu¹,

Hancock²,

Goodrich

et al. 2003

Proteomics

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An approach to the proteomic analysis of a breast cancer cell line (SKBR-3)This report describes the profiling of proteins in a sample prepared by laser capture microdissection (LCM) from a breast cancer cell line (SKBR-3). This experimental approach serves as a model system for proteomic studies on selected tissue samples and for studies of specific cell types. The captured cells were isolated in a dehydrated and reduced state and solubilized with a denaturing buffer. After dilution the protein mixture was digested with trypsin and the resulting peptide mixture was fractionated by reversed phase HPLC (RPLC) and analyzed on an ion trap mass spectrometer. A key part of this study is the combination of the LCM process with an extraction/digestion procedure that allowed effective solubilization of a significant part of the cellular sample in a single step. The identity of the peptides was determined by tandem mass spectrometry measurements in which the resulting spectra were compared with genomic and proteomic databases and protein identifications were made. While only peptides with a high probability assignment were used, the interpretation of mass spectral fragmentation patterns were also confirmed by manual interpretation of the spectra. Also, for the more abundant proteins the initial protein assignment from the best match peptide was strengthened by the observation of additional confirmatory peptide identifications. Another selection criteria was correlation of the mass spectrometric studies with clinical and genomic studies of potential cancer markers in tumor samples. This proteomic study allowed identification of the following proteins: human receptor protein kinase HER-2 or ERBB-2 and related kinases HER-3 and HER-4, the gene products from breast cancer type I and II susceptibility genes and cytoskeletal components such as cytokeratins 8, 18 and 19. Other proteins include fibroblast growth factor receptor variants (FGFR-2&4) and T-lymphoma invasion and metastasis inducing protein 1 (TIAM1). In addition several nonreceptor protein kinases YES, FAK and JAK-1 and 3 were identified. Since the study was performed on a limited number of cells (approximately 10 000) it raises the possibility of such studies being performed on individual patient samples prepared by needle biopsy.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An approach to the proteomic analysis of a breast cancer cell line (SKBR‐3)

Wu¹,

Hancock²,

Goodrich

et al. 2003

Proteomics

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“…However, upstream targets of ACK- 1 have not yet been identified. Downstream targets of ACK-1 that are involved in transformation of ACK-1 is a member of the non -receptor tyrosine kinase family (54). Mechanisms of signal transduction involving members of this family seem to be more complex than anticipated previously.…”

Section: Discussionmentioning

confidence: 93%

Requirement of Activated Cdc42-Associated Kinase for Survival of v-Ras-Transformed Mammalian Cells

Nur‐E‐Kamal

Zhang

Keenan

et al. 2005

Molecular Cancer Research

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Activated Cdc42-associated kinase (ACK) has been shown to be an important effector molecule for the small GTPase Cdc42. We have shown previously an essential role for Cdc42 in the transduction of Ras signals for the transformation of mammalian cells. In this report, we show that the ACK-1 isoform of ACK plays a critical role in transducing Ras-Cdc42 signals in the NIH 3T3 cells. Overexpression of a dominant-negative (K214R) mutant of ACK-1 inhibits Ras-induced up-regulation of c-fos and inhibits the growth of v-Ras-transformed NIH 3T3 cells. Using small interfering RNA, we knocked down the expression of ACK-1 in both v-Ha-Ras-transformed and parental NIH 3T3 cells and found that down-regulation of ACK-1 inhibited cell growth by inducing apoptosis only in v-Ha-Ras-transformed but not parental NIH 3T3 cells. In addition, we studied the effect of several tyrosine kinase inhibitors and found that PD158780 inhibits the kinase activity of ACK-1 in vitro. We also found that PD158780 inhibits the growth of v-Ha-Ras-transformed NIH 3T3 cells. Taken together, our results suggest that ACK-1 kinase plays an important role in the survival of v-Ha-Ras-transformed cells, suggesting that ACK-1 is a novel target for therapies directed at Ras-induced cancer. (Mol Cancer Res 2005;3(5):297 -305)

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“…Non-receptor protein tyrosine kinases play an essential role in important intracellular functions, such as cell proliferation and differentiation, by relaying signals from the cell-surface receptors to intracellular targets (Bolen, 1993;Neet and Hunter, 1996). The human full-length cDNA of PTK6 was cloned from breast carcinoma cells (Mitchell et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Purification and Spectroscopic Characterization of the Human Protein Tyrosine Kinase-6 SH3 Domain

Koo¹,

Kim²,

Lee³

et al. 2002

BMB Reports

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The human protein tyrosine kinase-6 (PTK6) polypeptide that is deduced from the cDNA sequence contains a Src homology (SH) 3 domain, SH2 domain, and catalytic domain of tyrosine kinase. We initiated biochemical and NMR characterization of PTK6 SH3 domain in order to correlate the structural role of the PTK6 using circular dichroism and heteronuclear NMR techniques. The circular dichroism data suggested that the secondary structural elements of the SH3 domain are mainly composed of β-sheet conformations. It is most stable when the pH is neutral based on the pH titration data. In addition, a number of cross peaks at the low-field area of the proton chemical shift of the NMR spectra indicated that the PTK6 SH3 domain retains a unique and folded conformation at the neutral pH condition. For other pH conditions, the SH3 domain became unstable and aggregated during NMR measurements, indicating that the structural stability is very sensitive to pH environments. Both the NMR and circular dichroism data indicate that the PTK6 SH3 domain experiences a conformational instability, even in an aqueous solution.

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Vertebrate non‐receptor protein–tyrosine kinase families

Cited by 139 publications

References 119 publications

An approach to the proteomic analysis of a breast cancer cell line (SKBR‐3)

An approach to the proteomic analysis of a breast cancer cell line (SKBR‐3)

Requirement of Activated Cdc42-Associated Kinase for Survival of v-Ras-Transformed Mammalian Cells

Purification and Spectroscopic Characterization of the Human Protein Tyrosine Kinase-6 SH3 Domain

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