EMMPRIN (basigin/CD147) expression is not correlated with MMP activity during adult mouse mammary gland development

Szymanowska, Małgorzata; Hendry, K. A. K.; Robinson, Claire; Kolb, Andreas

doi:10.1002/jcb.21975

Cited by 15 publications

(12 citation statements)

References 39 publications

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“…Similarly, Szymanowska et al . reported that MMP‐3 and MMP‐12 were not correlated with EMMPRIN in mammary gland. EMMPRIN is not the only inducer of MMPs .…”

Section: Discussionmentioning

confidence: 96%

Temporal expression of metalloproteinase‐8 and ‐13 and their relationships with extracellular matrix metalloproteinase inducer in the development of ligature‐induced periodontitis in rats

Dong

Wang

et al. 2012

J of Periodontal Research

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“…Similarly, Szymanowska et al . reported that MMP‐3 and MMP‐12 were not correlated with EMMPRIN in mammary gland. EMMPRIN is not the only inducer of MMPs .…”

Section: Discussionmentioning

confidence: 96%

Temporal expression of metalloproteinase‐8 and ‐13 and their relationships with extracellular matrix metalloproteinase inducer in the development of ligature‐induced periodontitis in rats

Dong

Wang

et al. 2012

J of Periodontal Research

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“…Western blots were done after semi-dry transfer of the proteins to a nitrocellulose membrane as described [25]. Mouse a-casein protein was detected using a rabbit-anti a-casein antiserum (Santa Cruz Biotechnology sc-98699) and a horse-radish-peroxidase linked goat anti-rabbit serum (Cell Signalling Technologies #7074).…”

Section: Observationmentioning

confidence: 99%

Milk Lacking α-Casein Leads to Permanent Reduction in Body Size in Mice

et al. 2011

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The major physiological function of milk is the transport of amino acids, carbohydrates, lipids and minerals to mammalian offspring. Caseins, the major milk proteins, are secreted in the form of a micelle consisting of protein and calcium-phosphate.We have analysed the role of the milk protein α-casein by inactivating the corresponding gene in mice. Absence of α-casein protein significantly curtails secretion of other milk proteins and calcium-phosphate, suggesting a role for α-casein in the establishment of casein micelles. In contrast, secretion of albumin, which is not synthesized in the mammary epithelium, into milk is not reduced. The absence of α-casein also significantly inhibits transcription of the other casein genes. α-Casein deficiency severely delays pup growth during lactation and results in a life-long body size reduction compared to control animals, but has only transient effects on physical and behavioural development of the pups. The data support a critical role for α-casein in casein micelle assembly. The results also confirm lactation as a critical window of metabolic programming and suggest milk protein concentration as a decisive factor in determining adult body weight.

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“…EMMPRIN may be engaged in distinct signaling pathways, directly promoting the invasive behavior of prostate cancer cells towards metastasis. This notion gains support from evidence indicating lack of correlation between EMMPRIN expression and MMP activity during adult mouse mammary gland development (30). Moreover, EMMPRIN has been shown to directly promote insoluble fibronectin assembly (21).…”

Section: Discussionmentioning

confidence: 67%

EMMPRIN regulates cytoskeleton reorganization and cell adhesion in prostate cancer

et al. 2011

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Background Proteins on cell surface play important roles during cancer progression and metastasis via their ability to mediate cell-to-cell interactions and navigate the communication between cells and the microenvironment. Methods In this study a targeted proteomic analysis was conducted to identify the differential expression of cell surface proteins in human benign (BPH-1) vs. malignant (LNCaP and PC-3) prostate epithelial cells. We identified EMMPRIN (extracellular matrix metalloproteinase inducer) as a key candidate and shRNA functional approaches were subsequently applied to determine the role of EMMPRIN in prostate cancer cell adhesion, migration, invasion as well as cytoskeleton organization. Results EMMPRIN was found to be highly expressed on the surface of prostate cancer cells compared to BPH-1 cells, consistent with a correlation between elevated EMMPRIN and metastasis found in other tumors. No significant changes in cell proliferation, cell cycle progression or apoptosis were detected in EMMPRIN knockdown cells compared to the scramble controls. Furthermore, EMMPRIN silencing markedly decreased the ability of PC-3 cells to form filopodia, a critical feature of invasive behavior, while it increased expression of cell-cell adhesion and gap junction proteins. Conclusions Our results suggest that EMMPRIN regulates cell adhesion, invasion and cytoskeleton reorganization in prostate cancer cells. This study identifies a new function for EMMPRIN as a contributor to prostate cancer cell-cell communication and cytoskeleton changes towards metastatic spread, and suggests its potential value as a marker of prostate cancer progression to metastasis.

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EMMPRIN (basigin/CD147) expression is not correlated with MMP activity during adult mouse mammary gland development

Cited by 15 publications

References 39 publications

Temporal expression of metalloproteinase‐8 and ‐13 and their relationships with extracellular matrix metalloproteinase inducer in the development of ligature‐induced periodontitis in rats

Temporal expression of metalloproteinase‐8 and ‐13 and their relationships with extracellular matrix metalloproteinase inducer in the development of ligature‐induced periodontitis in rats

Milk Lacking α-Casein Leads to Permanent Reduction in Body Size in Mice

EMMPRIN regulates cytoskeleton reorganization and cell adhesion in prostate cancer

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