Biosynthesis and secretion of laminin and S‐laminin by human prostate carcinoma cell lines

Rabinovitz, Isaac; Cress, Anne E.; Nagle, Ray B.

doi:10.1002/pros.2990250207

Cited by 20 publications

(12 citation statements)

References 42 publications

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“…In agreement with this conclusion, Mitostatin-depleted PC3 cells showed an increased capacity to adhere to laminin (Figure 4B). On the other hand, the lack of significant differences in cell adhesion to laminin observed in the LNCaP cells could be partly explained by their documented low adhesive ability in vitro [22], [23].…”

Section: Resultsmentioning

confidence: 99%

Mitostatin Is Down-Regulated in Human Prostate Cancer and Suppresses the Invasive Phenotype of Prostate Cancer Cells

et al. 2011

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MITOSTATIN, a novel putative tumor suppressor gene induced by decorin overexpression, is expressed in most normal human tissues but is markedly down-regulated in advanced stages of mammary and bladder carcinomas. Mitostatin negatively affects cell growth, induces cell death and regulates the expression and activation levels of Hsp27. In this study, we demonstrated that ectopic expression of Mitostatin in PC3, DU145, and LNCaP prostate cancer cells not only induced a significant reduction in cell growth, but also inhibited migration and invasion. Moreover, Mitostatin inhibited colony formation in soft-agar of PC3 and LNCaP cells as well as tumorigenicity of LNCaP cells in nude mice. Conversely, targeting endogenous Mitostatin by siRNA and anti-sense strategies in PC3 and DU145 prostate cancer cells enhanced the malignant phenotype in both cell lines. In agreement of these anti-oncogenic roles, we discovered that Mitostatin was absent in ∼35% (n = 124) of prostate tumor samples and its overall reduction was associated with advanced cancer stages. Collectively, our findings indicate that MITOSTATIN may acts as a tumor suppressor gene in prostate cancer and provide a novel cellular and molecular mechanism to be further exploited and deciphered in our understanding of prostate cancer progression.

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Section: Resultsmentioning

confidence: 99%

Mitostatin Is Down-Regulated in Human Prostate Cancer and Suppresses the Invasive Phenotype of Prostate Cancer Cells

et al. 2011

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“…This selected a number of clones encoding 37LRP, as well as Hsp60 (heat-shock protein 60) molecular chaperones. The surface expression of functional 37LRP/67LR appears to be a prerequisite for both binding and internalization of PrP, as 37LRP mutants lacking the putative transmembrane domain (residues [86][87][88][89][90][91][92][93][94][95][96][97][98][99][100][101] were not retained at the membrane, but mutated 37LRP was isolated from the extracellular space. Tissues with high levels of PrP sc (the modified pathogenic form of PrP) accumulation displayed correspondingly high levels of 37LRP, in particular the brain and pancreatic tissue [128].…”

Section: Prp Interactionsmentioning

confidence: 99%

The 67 kDa laminin receptor: structure, function and role in disease

et al. 2008

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The 67LR (67 kDa laminin receptor) is a cell-surface receptor with high affinity for its primary ligand. Its role as a laminin receptor makes it an important molecule both in cell adhesion to the basement membrane and in signalling transduction following this binding event. The protein also plays critical roles in the metastasis of tumour cells. Isolation of the protein from either normal or cancerous cells results in a product with an approx. molecular mass of 67 kDa. This protein is believed to be derived from a smaller precursor, the 37LRP (37 kDa laminin receptor precursor). However, the precise mechanism by which cytoplasmic 37LRP becomes cell-membrane-embedded 67LR is unclear. The process may involve post-translational fatty acylation of the protein combined with either homo- or hetero-dimerization, possibly with a galectin-3-epitope-containing partner. Furthermore, it has become clear that acting as a receptor for laminin is not the only function of this protein. 67LR also acts as a receptor for viruses, such as Sindbis virus and dengue virus, and is involved with internalization of the prion protein. Interestingly, unmodified 37LRP is a ribosomal component and homologues of this protein are found in all five kingdoms. In addition, it appears to be strongly associated with histones in the eukaryotic cell nucleus, although the precise role of these interactions is not clear. Here we review the current understanding of the structure and function of this molecule, as well as highlighting areas requiring further research.

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“…In the present study, we evaluated the transcriptional activities of genes coding BM components (␣1 chain of collagen IV, S-laminin, and laminin ␤1 chain) in benign prostate tissue, premalignant lesions (high grade prostatic intraepithelial neoplasia), and primary and metastatic cancer using in situ hybridization (ISH). We chose S-laminin for ISH evaluation because recent data have reported considerable amounts of surface-bound S-laminin in the highly tumorigenic DU 145 prostate cancer cell line [33].…”

Section: Introductionmentioning

confidence: 99%

In situ hybridization analysis of genes coding collagen IV α1 chain, laminin β1 chain, and s-laminin in prostate tissue and prostate cancer: Increased basement membrane gene expression in high-grade and metastatic lesions

et al. 1998

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BACKGROUND Recent immunohistochemical data have shown that invasive prostate cancer cells are separated from the host tissue by basement membranes (BM), and express associated adhesive molecules that bind to these de novo synthesized extracellular matrices. METHODS In the present study, we used in situ hybridization techniques to determine steady‐state levels of genes coding BM components (α1 chain of collagen IV, laminin β1 chain, and S‐laminin) in prostate tissue obtained from 15 radical prostatectomy specimens and 5 lymph node metastases of common prostatic adenocarcinomas. RESULTS In benign prostate tissue, transcripts of these genes were detected predominantly in the basal cell layer, indicating that components of epithelial BMs are synthesized by basal cells and not bey stromal cells. The cancerous lesions investigated revealed increasing collagen IV, laminin β1 chain, and S‐laminin mRNA levels when compared with benign prostate tissue. The highest steady‐state levels were found in high grade (primary Gleason grade 4 and 5) carcinoma and lymph node metastases, and were predominantly localized in epithelial compartments of the cancerous tissue. CONCLUSIONS These findings indicate that neoplastic BM in prostatic adenocarcinoma derive from tumor cells and not from the host tissue. Increasing transcriptional activities of genes coding BM components detected in poorly differentiated and metastatic lesions may accelerate the BM‐forming process, which probably contributes to the ability of tumor cells to penetrate the extracellular matrix during the process of stromal invasion and metastasis. Prostate 36:143–150, 1998. © 1998 Wiley‐Liss, Inc.

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Biosynthesis and secretion of laminin and S‐laminin by human prostate carcinoma cell lines

Cited by 20 publications

References 42 publications

Mitostatin Is Down-Regulated in Human Prostate Cancer and Suppresses the Invasive Phenotype of Prostate Cancer Cells

Mitostatin Is Down-Regulated in Human Prostate Cancer and Suppresses the Invasive Phenotype of Prostate Cancer Cells

The 67 kDa laminin receptor: structure, function and role in disease

In situ hybridization analysis of genes coding collagen IV α1 chain, laminin β1 chain, and s-laminin in prostate tissue and prostate cancer: Increased basement membrane gene expression in high-grade and metastatic lesions

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