A tyrosine kinase profile of prostate carcinoma.

Robinson, Dan R.; He, Feng; Pretlow, T. G.; Kung, Hsing Jien

doi:10.1073/pnas.93.12.5958

Cited by 207 publications

(203 citation statements)

References 45 publications

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“…Other studies however have failed to confirm a close correlation between ERBB3 and ERBB4 in prostate cancers 253 and in prostate cancer cell lines ERBB4 is frequently not expressed. [257][258][259] ERBB3 may be activated in prostate cancer cells by NRG, leading to formation of ERBB2/ ERBB3 hetero-dimers. ERBB2 has been strongly implicated in prostate cancer.…”

Section: Prostate Cancermentioning

confidence: 99%

The ERBB3 receptor in cancer and cancer gene therapy

2008

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ERBB3, a member of the epidermal growth factor receptor (EGFR) family, is unique in that its tyrosine kinase domain is functionally defective. It is activated by neuregulins, by other ERBB and nonERBB receptors as well as by other kinases, and by novel mechanisms. Downstream it interacts prominently with the phosphoinositol 3-kinase/AKT survival/mitogenic pathway, but also with GRB, SHC, SRC, ABL, rasGAP, SYK and the transcription regulator EBP1. There are likely important but poorly understood roles for nuclear localization and for secreted isoforms. Studies of ERBB3 expression in primary cancers and of its mechanistic contributions in cultured cells have implicated it, with varying degrees of certainty, with causation or sustenance of cancers of the breast, ovary, prostate, certain brain cells, retina, melanocytes, colon, pancreas, stomach, oral cavity and lung. Recent results link high ERBB3 activity with escape from therapy targeting other ERBBs in lung and breast cancers. Thus a wide and centrally important role for ERBB3 in cancer is becoming increasingly apparent. Several approaches for targeting ERBB3 in cancers have been tested or proposed. Small inhibitory RNA (siRNA) to ERBB3 or AKT is showing promise as a therapeutic approach to treatment of lung adenocarcinoma.

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Section: Prostate Cancermentioning

confidence: 99%

The ERBB3 receptor in cancer and cancer gene therapy

2008

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“…The amplification of the erbB-2 gene is found in several human cancers and elevated expression of ErbB-2 protein is strongly correlated with their poor prognosis (Slamon et al, 1989). In most prostate epithelia, only three members of this family, but not ErbB-4, are expressed (Robinson et al, 1996). In prostate carcinomas, the erbB-2 gene is not amplified and its protein level is elevated in some advanced tumors during androgen ablation therapy (Signoretti et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

ErbB-2 via PYK2 upregulates the adhesive ability of androgen receptor-positive human prostate cancer cells

et al. 2007

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Aberrant regulation in the adhesive ability of cancer cells is closely associated with their metastatic activity. In this study, we examine the role of ErbB-2 in regulating the adhesive ability of androgen receptor (AR)-positive human prostate cancer (PCa) cells, the major cell population of PCa. Utilizing different LNCaP and MDA PCa2b cells as model systems, we found that ErbB-2 activity was correlated with PYK2 activity and adhesive ability in those cells. Increased ErbB-2 expression or activity in LNCaP C-33 cells enhanced PYK2 activation and cell adhesion, while the high PYK2 activity and the rapid adhesion of LNCaP C-81 cells were decreased by diminishing ErbB-2 expression or activity. Knockdown studies revealed the predominant role of ErbB-2 in regulating LNCaP C-81 cell adhesion. Coimmunoprecipitation showed that C-81 cells had increased interaction between ErbB-2 and PYK2. Elevated ErbB-2 activity in LNCaP cells correlated with increased ERK/MAPK activity and enhanced adhesive ability, which were abolished by the expression of K457A-PYK2 mutant or the treatment of PD98059, a MEK inhibitor. In summary, our data suggested that ErbB-2, via PYK2-ERK/MAPK, upregulates the adhesive ability of AR-positive human PCa cells.

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“…The role that ErbB4 plays in tumorigenesis has yet to be well defined. ErbB4 is expressed in normal prostate tissue but most prostate tumors lack ErbB4 expression [11][12][13]. In several tumor types, ErbB4 expression correlates with less aggressive behavior and better patient prognosis [5,14].…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of ErbB4 on Tyr1056 is critical for inhibition of colony formation by prostate tumor cell lines

Gallo

Bryant

Fry

et al. 2006

Biochemical and Biophysical Research Communications

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Correspondence to: David J. Riese II, Purdue Cancer Research Center, 201 S. University Street, West Lafayette, Indiana, 47907-2064, Tel (765) FAX (765) We have previously demonstrated that the constitutively-active Q646C mutant of the ErbB4 receptor tyrosine kinase inhibits colony formation by human prostate tumor cell lines. Here we use ErbB4 mutants to identify ErbB4 functions critical for inhibiting colony formation. A derivative of ErbB4 Q646 that lacks kinase activity fails to inhibit colony formation by prostate tumor cells. Likewise, an ErbB4 Q646C mutant in the context of the CT-b splicing isoform fails to inhibit colony formation. Mutation of tyrosine 1056 to phenylalanine abrogates inhibition of colony formation whereas an ErbB4 mutant that lacks all of the putative sites of tyrosine phosphorylation except for tyrosine 1056 still inhibits colony formation. Given that tyrosine 1056 is missing in the CT-b isoform, these results suggest that phosphorylation of tyrosine 1056 is critical for function. Indeed, an ErbB4 mutant that lacks kinase activity but has a glutamate phosphomimic residue substituted for tyrosine 1056 inhibits colony formation. Finally, one-dimensional phosphopeptide mapping indicates that ErbB4 Q646C is phosphorylated on tyrosine 1056. These data suggest that phosphorylation of ErbB4 tyrosine 1056 is critical for coupling ErbB4 to prostate tumor suppression.

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A tyrosine kinase profile of prostate carcinoma.

Abstract: (20). Fifty micrograms of total cellular RNA was used for reverse

Cited by 207 publications

References 45 publications

The ERBB3 receptor in cancer and cancer gene therapy

The ERBB3 receptor in cancer and cancer gene therapy

ErbB-2 via PYK2 upregulates the adhesive ability of androgen receptor-positive human prostate cancer cells

Phosphorylation of ErbB4 on Tyr1056 is critical for inhibition of colony formation by prostate tumor cell lines

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