Transferrin mRNA level in the mouse mammary gland is regulated by pregnancy and extracellular matrix.

Chen, LiHow; Bissell, Mina J.

doi:10.1016/s0021-9258(18)45366-5

Cited by 73 publications

(5 citation statements)

References 21 publications

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“…DNA Probes for Northern Blot Analysis. The mouse TF probe was isolated from a commercial mouse cDNA library using PCR primers complementary to the 5' end of exon 7 and the 3' end of exon 9 (Chen & Bissell, 1987). No crosshybridization of the mouse TF with human RNA was observed.…”

Section: Methodsmentioning

confidence: 99%

Posttranscriptional regulation of chimeric human transferrin genes by iron

Cox¹,

Adrian²

1993

Biochemistry

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Transferrin, the transferrin receptor, and ferritin are integral to the body's management of iron, an element required for life but highly toxic when present in excess. The transferrin receptor and ferritin are regulated posttranscriptionally by iron: the transferrin receptor by mRNA stability and ferritin by mRNA translation. Results described here indicate that transferrin, like ferritin, is regulated by iron at the level of translation. Chimeric genes introduced into the mouse genome were composed of the human transferrin 5' regulatory region fused to the chloramphenicol acetyl transferase (CAT) reporter gene. Iron administration to transgenic mice resulted in a significant decrease of transferrin-directed CAT enzyme activity and CAT protein in liver, but no significant decrease in human transferrin-CAT mRNA levels. Binding of specific RNA iron regulatory elements by proteins in cytoplasmic extracts have been shown to regulate ferritin and transferrin receptor synthesis. Similar results have been obtained with transferrin mRNA. A decreased binding of human transferrin 5'-untranslated region RNA by factors in cytoplasmic extracts of livers from mice receiving iron was found when compared to extracts from control mice. A human transferrin RNA-protein complex migrated electrophoretically with the same mobility as a ferritin iron responsive element RNA-iron responsive element binding protein complex. The ferritin iron responsive element RNA also competed with the human transferrin 5'-untranslated region RNA-protein complexes formed and vice versa. Therefore, iron modulation of human transferrin may share a factor common or similar to that observed in ferritin and transferrin receptor iron modulation.

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Section: Methodsmentioning

confidence: 99%

Posttranscriptional regulation of chimeric human transferrin genes by iron

Cox¹,

Adrian²

1993

Biochemistry

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“…High specific activity (1-3 x 109 cpm//zg) random-primed probes (20) were prepared using gelpurified insert sequences from plasmids kindly provided by M. Kurkinen (Robert Wood Johnson Medical School) (mouse type IV [al] collagen, pPE123 [34]), B. Hogan Vanderbilt University (mouse laminin BI, pPE47 [2], and R. Hynes (Massachusetts Institute of Technology) (human fibronectin, 3,rlf 1 [48]). Probes for milk gene sequences, mouse /~-casein (pBCL-I, a homemade subcione derived from a plasmid from L Rosen, Baylor College of Medicine), and mouse traasferrin (pMTf-5, from this laboratory [12]), were prepared by nick translation (specific activity = 5 x 108 cpm//~g). After a 2-h prehybridization step, hybridization was carded out overnight at 42°C in the presence of 6 x SSC (S$C is 150 mM NaCI, 15 mM sodium citrate), 1 #g/mi BSA, 1/~g/ml Ficol1400, 1 t~g/ml polyvinylpyrollidine, 0.1% SDS, 25 mM NaHePO4, 1.5 mM Na4P2OT, 50% deionized formamide, 100 #g/ml sheared calf thymus DNA, and 3-8 x l06 cpm of ECM probe or 1-2 x 106 cpm of milk probe per ml of hybridization so-Intion.…”

Section: Northern Blottingmentioning

confidence: 99%

“…Cells from pregnant mammary gland rapidly lose the ability to synthesize milk proteins if they are cultured on a plastic substratum, even when all lactogenic hormones are present (18,37). However, when plated onto an exogenous stromal (type I collagen) matrix which is then floated, or onto a basement membrane matrix reconstituted from Engelbreth-Holm-Swarm tumor, the cells reacquire many of their differentiated properties, including the capacity to assume a polarized morphology, to accumulate casein and transferrin mRNAs, and to secrete most of the milk proteins (7,12,13,(36)(37)(38). Furthermore, cells cultured on the basement membrane matrix undergo striking multicellular architectural restructuring, resemble mammary alveoli in vivo, and secrete milk proteins vectorially (1,13).…”

mentioning

confidence: 99%

Expression of extracellular matrix components is regulated by substratum.

Streuli

Bissell

1990

The Journal of Cell Biology

Self Cite

327

184

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Abstract. Reconstituted basement membranes and extracellular matrices have been demonstrated to affect, positively and dramatically, the production of milk proteins in cultured mammary epithelial cells. Here we show that both the expression and the deposition of extracellular matrix components themselves are regulated by substratum. The steady-state levels of the laminin, type IV collagen, and fibronectin mRNAs in mammary epithelial cells cultured on plastic dishes and on type I collagen gels have been examined, as has the ability of these cells to synthesize, secrete, and deposit laminin and other extracellular matrix proteins. We demonstrate de novo synthesis of a basement membrane by cells cultured on type I collagen gels which have been floated into the medium. Expression of the mRNA and proteins of basement membranes, however, are quite low in these cultures. In contrast, the levels of laminin, type IV collagen, and fibronectin mRNAs are highest in cells cultured on plastic surfaces, where no basement membrane is deposited. It is suggested that the interaction between epithelial cells and both basement membrane and stromally derived matrices exerts a negative influence on the expression of mRNA for extracellular matrix components. In addition, we show that the capacity for lactational differentiation correlates with conditions that favor the deposition of a continuous basement membrane, and argue that the interaction between specialized epithelial cells and stroma enables them to create their own microenvironment for accurate signal transduction and phenotypic function.T HE synthesis and secretion of milk proteins in functional mammary epithelia are regulated by both hormones and extracellular matrix (ECM) ~ (3, 17), although the molecular mechanisms underlying the control of milk protein expression are not fully understood. A culture system is being used in our laboratory in which dissociated primary mouse mammary epithelial cells express high levels of milk products in response to prolactin, hydrocortisone, and insulin. Cells from pregnant mammary gland rapidly lose the ability to synthesize milk proteins if they are cultured on a plastic substratum, even when all lactogenic hormones are present (18, 37). However, when plated onto an exogenous stromal (type I collagen) matrix which is then floated, or onto a basement membrane matrix reconstituted from Engelbreth-Holm-Swarm tumor, the cells reacquire many of their differentiated properties, including the capacity to assume a polarized morphology, to accumulate casein and transferrin mRNAs, and to secrete most of the milk proteins (7,12,13,(36)(37)(38). Furthermore, cells cultured on the basement membrane matrix undergo striking multicellular architectural restructuring, resemble mammary alveoli in vivo, and secrete milk proteins vectorially (1, 13). The major conclusion from several years' study in this and other labora-1. Abbreviation used in this paper: ECM, extracellular matrix. tories is that the ECM plays a fundamental role in controlling cellular phe...

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“…Elles peuvent être d'origine sanguine comme les immunoglobulines et l'albumine sérique, ou néo-synthétisées par la glande mammaire, comme les caséines et les protéines du lactosérum : l'α-lactalbumine, la β-lactoglobuline, la WAP et la lactoferrine. La transferrine du lait présente la particularité de pouvoir être d'origine mammaire ou sanguine selon les espèces (Banfield et al, 1991 ;Chen & Bissell, 1987).…”

Section: Introductionunclassified

Organisation nucléaire et expression des gènes des protéines du lait

Chanat¹,

Aujean²,

Bâlteanu³

et al. 2006

J. Soc. Biol.

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Milk protein gene expression varies during the pregnancy/lactation cycle under the influence of lactogenic hormones which induce the activation of several transcription factors. Beyond this activation modifying the binding properties of these factors to their consensus sequences, their interactions with DNA is regulated by variations of the chromatin structure. In the nuclei of the mammary epithelial cell, the three dimensional organisation of the chromatin loops, located between matrix attachment regions, is now being studied. The main milk components are organised in supramolecular structures. Milk fat globules are made of a triglyceride core enwrapped by a tripartite membrane originating from various intracellular compartments. The caseins, the main milk proteins, form aggregates: the casein micelles. Their gradual aggregation in the secretory pathway is initiated as soon as from the endoplasmic reticulum. The mesostructures of the milk fat globule and of the casein micelle remain to be elucidated. Our goal is to make some progress into the understanding of the molecular and cellular mechanisms involved in the formation of these milk products.

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Transferrin mRNA level in the mouse mammary gland is regulated by pregnancy and extracellular matrix.

Cited by 73 publications

References 21 publications

Posttranscriptional regulation of chimeric human transferrin genes by iron

Posttranscriptional regulation of chimeric human transferrin genes by iron

Expression of extracellular matrix components is regulated by substratum.

Organisation nucléaire et expression des gènes des protéines du lait

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