Bibliographies thématiques / Extracellular matrix proteins

Littérature scientifique sur le sujet « Extracellular matrix proteins »

Auteur : Grafiati
Publié le 4 juin 2021
Mis à jour le 21 février 2023

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Articles de revues sur le sujet "Extracellular matrix proteins"

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Ruggiero, Florence, et Manuel Koch. « Making recombinant extracellular matrix proteins ». Methods 45, no 1 (mai 2008) : 75–85. http://dx.doi.org/10.1016/j.ymeth.2008.01.003.

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GOLDFARB, RONALD H., et LANCE A. LIOTTA. « Thrombin Cleavage of Extracellular Matrix Proteins ». Annals of the New York Academy of Sciences 485, no 1 Bioregulatory (décembre 1986) : 288–92. http://dx.doi.org/10.1111/j.1749-6632.1986.tb34590.x.

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Coito, Ana J., et Jerzy W. Kupiec-Weglinski. « EXTRACELLULAR MATRIX PROTEINS IN ORGAN TRANSPLANTATION1 ». Transplantation 69, no 12 (juin 2000) : 2465–73. http://dx.doi.org/10.1097/00007890-200006270-00001.

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Giomarelli, Barbara, Livia Visai, Karolin Hijazi, Simonetta Rindi, Michela Ponzio, Francesco Iannelli, Pietro Speziale et Gianni Pozzi. « Binding ofStreptococcus gordoniito extracellular matrix proteins ». FEMS Microbiology Letters 265, no 2 (décembre 2006) : 172–77. http://dx.doi.org/10.1111/j.1574-6968.2006.00479.x.

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Moran, A. P., P. Kuusela et T. U. Kosunen. « Interaction ofHelicobacter pyloriwith extracellular matrix proteins ». Journal of Applied Bacteriology 75, no 2 (août 1993) : 184–89. http://dx.doi.org/10.1111/j.1365-2672.1993.tb02765.x.

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Hedley, S. J., D. J. Gawkrodger, A. P. Weetman et S. MacNeil. « Extracellular matrix proteins stimulate melanocyte tyrosinase ». Melanoma Research 5 (septembre 1995) : 38. http://dx.doi.org/10.1097/00008390-199509001-00068.

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Campbell, N. E., L. Kellenberger, J. Greenaway, R. A. Moorehead, N. M. Linnerth-Petrik et J. Petrik. « Extracellular Matrix Proteins and Tumor Angiogenesis ». Journal of Oncology 2010 (2010) : 1–13. http://dx.doi.org/10.1155/2010/586905.

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Tumor development is a complex process that relies on interaction and communication between a number of cellular compartments. Much of the mass of a solid tumor is comprised of the stroma which is richly invested with extracellular matrix. Within this matrix are a host of matricellular proteins that regulate the expression and function of a myriad of proteins that regulate tumorigenic processes. One of the processes that is vital to tumor growth and progression is angiogenesis, or the formation of new blood vessels from preexisting vasculature. Within the extracellular matrix are structural proteins, a host of proteases, and resident pro- and antiangiogenic factors that control tumor angiogenesis in a tightly regulated fashion. This paper discusses the role that the extracellular matrix and ECM proteins play in the regulation of tumor angiogenesis.
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Patel, Trushar R., et Joerg Stetefeld. « Solution Conformation of Extracellular Matrix Proteins ». Biophysical Journal 102, no 3 (janvier 2012) : 381a. http://dx.doi.org/10.1016/j.bpj.2011.11.2086.

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Pakianathan, Deepika R. « Extracellular matrix proteins and leukocyte function ». Journal of Leukocyte Biology 57, no 5 (mai 1995) : 699–702. http://dx.doi.org/10.1002/jlb.57.5.699a.

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Flinn, Barry S. « Plant extracellular matrix metalloproteinases ». Functional Plant Biology 35, no 12 (2008) : 1183. http://dx.doi.org/10.1071/fp08182.

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The plant extracellular matrix (ECM) includes a variety of proteins with critical roles in the regulation of plant growth, development, and responses to pests and pathogens. Several studies have shown that various ECM proteins undergo proteolytic modification. In mammals, the extracellular matrix metalloproteinases (MMPs) are known modifiers of the ECM, implicated in tissue architecture changes and the release of biologically active and/or signalling molecules. Although plant MMPs have been identified, little is known about their activity and function. Plant MMPs show structural similarity to mammalian MMPs, including the presence of an auto-regulatory cysteine switch domain and a zinc-binding catalytic domain. Plant MMPs are differentially expressed in cells and tissues during plant growth and development, as well as in response to several biotic and abiotic stresses. The few gene expression and mutant analyses to date indicate their involvement in plant growth, morphogenesis, senescence and adaptation and response to stress. In order to gain a further understanding of their function, an analysis and characterisation of MMP proteins, their activity and their substrates during plant growth and development are still required. This review describes plant MMP work to date, as well as the variety of genomic and proteomic methodologies available to characterise plant MMP activity, function and potential substrates.
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Thèses sur le sujet "Extracellular matrix proteins"

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Yi, Ming. « Extracellular matrix proteins and angiogenesis / ». Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2003. http://wwwlib.umi.com/cr/ucsd/fullcit?p3091204.

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Wendel, Mikael. « Skeletal tissue proteins isolation and characterization of novel extracellular matrix proteins / ». Lund : Dept. of Medical and Physiological Chemistry, University of Lund, 1994. http://books.google.com/books?id=zvtqAAAAMAAJ.

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Chan, Cheuk-ming. « Controlled protein release from collagen matrix ». Click to view the E-thesis via HKUTO, 2007. http://sunzi.lib.hku.hk/HKUTO/record/B3955868X.

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Avella, Charlotte Sinclair. « Strain related differential regulation of tendon extracellular matrix proteins ». Thesis, Royal Veterinary College (University of London), 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.558956.

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Garcia, John Francis. « The role of extracellular matrix proteins in epithelial tumorigenesis / ». May be available electronically:, 2008. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.

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Shen, Zhenxin. « Expression and localization of extracellular matrix proteins in skeletal development ». Lund : Dept. of Cell and Molecular Biology, Section for Connective Tissue Biology, Lund University, 1998. http://books.google.com/books?id=Xe9qAAAAMAAJ.

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St, John Joni J. Cheung H. Tak. « Characterization of the adhesion of lymphocytes to extracellular matrix proteins ». Normal, Ill. Illinois State University, 1989. http://wwwlib.umi.com/cr/ilstu/fullcit?p8918625.

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Thesis (Ph. D.)--Illinois State University, 1989.
Title from title page screen, viewed October 12, 2005. Dissertation Committee: H. Tak Cheung (chair), David W. Borst, Herman E. Brockman, Arlan G. Richardson, Brian J. Wilkinson. Includes bibliographical references (leaves 145-156) and abstract. Also available in print.
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Burnier, Julia. « Regulation of site-specific liver metastasis by extracellular matrix proteins ». Thesis, McGill University, 2010. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=86657.

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Metastatic disease remains the main cause of death from cancer. Few therapeutic options for patients have demonstrated potential in curing metastatic disease. The molecular mechanisms underlying site-specific metastasis and the factors mediating tumor cell homing remain largely unknown. Based on a murine Lewis lung carcinoma tumour model of site-specific metastasis mediated by the expression of the insulin-like growth factor - I receptor (IGF-IR), we identified ECM components that show particular promise in regulating metastasis to a specific site. Specifically, we identified collagen IVα1 and α2 as differentially expressed in liver- and lung-colonizing cells. The overexpression of these genes caused major changes to cell structure and function including differences in cellular morphology, anchorage-independent growth, and resulted in a switch from a lung- to a liver-metastasizing phenotype. These changes were at least in part due to α2-integrin-mediated activation of focal adhesion kinase (FAK) and protection from anoikis. Collagen IV α1 suppression resulted in increased anoikis and decreased tumour cell colonization of the liver, making it an essential and sufficient gene in liver metastasis in our model. Moreover, type IV collagen overexpression resulted in major changes to ECM and ECM-degradation genes decreasing MMP-3, MMP-9, MMP-13, and collagen type III. Uveal melanoma cells with distinct metastatic phenotypes also showed major changes to these genes. Finally, by analyzing human specimens of metastatic disease, collagen IV was shown to be expressed only in metastatic and specifically hepatic metastases when compared to primary tumours and metastases to other organs. Collectively, these findings implicate collagen IV as a clinically relevant marker and potential target against site-specific metastasis to the liver.
Le cancer métastatique ne présente que peu d'options thérapeutiques et de ce fait constitue la cause principale de décès chez les patients qui en sont atteints. Par ailleurs, les mécanismes moléculaires responsables de l'atteinte d'organes-cibles de la métastase par les cellules cancéreuses demeurent largement méconnus. La thèse qui suit présente l'identification d'un marqueur moléculaire qui apparait comme étant un facteur crucial dans l'atteinte des organes-cibles par les cellules métastatiques. En effet, la constituante de la matrice extracellulaire collagene IVα1 et α2, semble être exprimée de manière distinctive chez les cellules colonisant le foie et les poumons. Nous basant sur un modèle murin de métastase provenant de carcinome pulmonaire et véhiculée par l'expression de IGF-IR, nous avons identifié des changements majeurs quant à la structure et à la fonction des cellules cancéreuses, suite à la surexpression des gènes du Collagene IVα1 et α2. Ces changements comprennent, entre autre, des différences au niveau de la morphologie et la croissance cellulaire et ont aussi pour résultat la mutation du phénotype métastatique de pulmonaire à hépatique. Ces changements sont en partie conséquence de l'activation de la kinase d'adhésion focale (FAK) et de la protection de l'anoikis. Par contre, la suppression de l'expression du Collagène IV accroit l'anoikis et diminue la colonisation du foie par les cellules cancéreuses. En outre, la surexpression du Collagène IV apporte des changements majeurs au niveau de la matrice extracellulaire et aux gènes de dégradation de celle-ci, diminuant MMP-3, MMP-9, MMP-13 et le collagène III. Les cellules de mélanome uvéale à phénotype métastatique distinct présentent aussi des changements importants quant à l'expression ces gènes. Finalement, après analyse de spécimens humains, le collagène IV semble être exprimé exclusivement au niveau des tumeurs métastatiques et en
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Chan, Cheuk-ming, et 陳卓銘. « Controlled protein release from collagen matrix ». Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2007. http://hub.hku.hk/bib/B3955868X.

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Xu, Qian Angela. « Matrix proteins gene expression by mesenchymal cells ». Thesis, The University of Sydney, 1997. https://hdl.handle.net/2123/27663.

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Chondrocytes from articular cartilage (AC) of diarthrodial joints and smooth muscle cells (SMCs) derived from blood vessels are both of mesenchymal origin. In this study, the mRNA expression by these cells of matrix proteoglycan (PG) and collagen was examined in vitro and in vivo. Since the expression of matrix components by mesenchymal cells is influenced by their interaction with growth factors and cytokines, experiments were also undertaken in vitro to determine the effect of transforming growth factor B1 (TGF-B1) and interleukin -1B (IL-1B) on PG and collagen gene expression by these cells.
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Livres sur le sujet "Extracellular matrix proteins"

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Even-Ram, Sharona. Extracellular matrix protocols. 2e éd. New York : Humana Press, 2009.

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Woessner, J. F. Matrix metalloproteinases and TIMPs. New York : Oxford University Press, 2000.

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Ayad, Shirley. The extracellular matrix factsbook. 2e éd. San Diego : Academic Press, 1998.

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Derek, Chadwick, Goode Jamie et Novartis Foundation, dir. The biology of extracellular molecular chaperones. Chichester, England : John Wiley, 2008.

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Thomas, Kreis, et Vale Ronald, dir. Guidebook to the extracellular matrix and adhesion proteins. Oxford : Oxford University Press, 1993.

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C, Parks William, et Mecham Robert P, dir. Matrix metalloproteinases. San Diego : Academic Press, 1998.

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International, EBSA Symposium (2nd 1988 Gwatt Switzerland). Cytoskeletal and extracellular proteins : Structure, interaction, and assembly. Berlin : Springer-Verlag, 1989.

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Inhibitors of Metalloproteinases Conference (1996 Banff, Alta.). Tissue inhibitors of metalloproteinases in development and disease : Proceedings of the Inhibitors of Metalloproteinases Conference, Banff, Alberta, Canada, September 25-29, 1996. Sous la direction de Hawkes Susan P, Edwards Dylan R et Khokha Rama. Australia : Harwood Academic, 2000.

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Clark, Ian M. Matrix metalloproteinase protocols. 2e éd. New York, N.Y : Humana Press, 2010.

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Aebi, U. Cytoskeletal and Extracellular Proteins : Structure, Interactions and Assembly The 2nd International EBSA Symposium. Berlin, Heidelberg : Springer Berlin Heidelberg, 1989.

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Chapitres de livres sur le sujet "Extracellular matrix proteins"

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Roberts, David D., et Lester F. Lau. « Matricellular Proteins ». Dans The Extracellular Matrix : an Overview, 369–413. Berlin, Heidelberg : Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-16555-9_11.

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Butler, William T., Helena H. Ritchie et Antonius L. J. J. Bronckers. « Extracellular Matrix Proteins of Dentine ». Dans Ciba Foundation Symposium 205 - Dental Enamel, 107–17. Chichester, UK : John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515303.ch8.

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Jimenez-Mallebrera, Cecilia, A. Reghan Foley et Carsten G. Bönnemann. « Proteins of the Extracellular Matrix ». Dans Muscle Disease, 102–7. Oxford, UK : John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118635469.ch9.

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Segade, Fernando. « Molecular Evolution of the Microfibril-Associated Proteins : The Fibulins and the MAGPs ». Dans Evolution of Extracellular Matrix, 163–90. Berlin, Heidelberg : Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36002-2_6.

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Loopstra, Carol A. « Proteins of the Conifer Extracellular Matrix ». Dans Molecular Biology of Woody Plants, 287–97. Dordrecht : Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-017-2311-4_11.

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Clemmons, David R. « IGF Binding Proteins and Extracellular Matrix ». Dans The IGF System, 273–79. Totowa, NJ : Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-712-3_12.

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Arzate, Higinio, et Margarita Zeichner-David. « Cementum Proteins Beyond Cementum ». Dans Extracellular Matrix Biomineralization of Dental Tissue Structures, 157–217. Cham : Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-76283-4_7.

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Çelebi-Saltik, Betül, et Betül Çelebi-Saltik. « Extracellular Matrix Proteins for Stem Cell Fate ». Dans Advanced Surfaces for Stem Cell Research, 1–21. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119242642.ch1.

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Engel, J. « Networks of Extracellular Matrix and Adhesion Proteins ». Dans Dynamical Networks in Physics and Biology, 131–38. Berlin, Heidelberg : Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-03524-5_11.

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Zaręba, Tomasz W., Corina Pascu, Waleria Hryniewicz et Torkel Wadstrom. « Binding of Enterococci to Extracellular Matrix Proteins ». Dans Streptococci and the Host, 721–23. Boston, MA : Springer US, 1997. http://dx.doi.org/10.1007/978-1-4899-1825-3_169.

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Actes de conférences sur le sujet "Extracellular matrix proteins"

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Freytes, Donald O., Samuel Kolman, Sachin S. Velankar et Stephen F. Badylak. « Rheological Properties of Extracellular Matrix Derived Gels ». Dans ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176537.

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Bioscaffolds composed of extracellular matrix (ECM) have been used for the repair of a variety of tissues often leading to tissue-specific constructive remodeling [1]. ECM scaffolds are typically prepared by decellularization of tissues and are composed of the structural proteins (e.g. collagen) and functional proteins (e.g. growth factors) that characterize the native ECM. However, for certain applications, the use of ECM scaffolds can be limited by the native two-dimensional sheet form in which they are harvested.
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Januskevicius, Andrius, Ieva Janulaityte, Reinoud Gosens, Virginija Kalinauskaite-Zukauske, Rokas Stonkus et Kestutis Malakauskas. « Eosinophils contribute to extracellular matrix remodeling by enhancing pulmonary fibroblasts proliferation, differentiation and extracellular matrix proteins production in asthma ». Dans ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa968.

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Mueller, Catharina, Annika Andersson-Sjöland, Hans Henrik Schultz, Claus B. Andersen, Martin Iversen et Gunilla Westergren-Thorsson. « Mapping of extracellular matrix proteins in different compartments of transplanted lungs ». Dans ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa2543.

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Kleiman, Ross, Michelle Previtera, Sharan Parikh, Devendra Verma, Rene Schloss et Noshir Langrana. « The Effects of Extracellular Matrix Proteins and Stiffness on Neuronal Cell Adhesion ». Dans ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53596.

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Spinal cord injuries have spurred research interests in finding ways to repair or replace damaged neurons. We are looking to find novel ways to promote proliferation and differentiation of stem cells in order to replace damaged spinal cord neurons. While previous studies have shown that the mechanical properties of the cellular environment influence proliferation and differentiation, these studies have only been performed on polyacrylamide and agarose gels (1, 2). Collagen gels provide the opportunity to promote neuronal precursor cell (NPCs) proliferation and differentiation in a more natural environment by utilizing the mechanical properties of the gel. In this study, we examine the effects of 2D collagen matrices of varying stiffness on proliferation and differentiation of rat, spinal cord NPCs in order to create a more biocompatible tissue-engineered platform.
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de Vries, Maaike, Alen Faiz, Dirkje S. Postma, Don D. Sin, Yohan Bossé, David C. Nickle, Wim Timens, Maarten van den Berge et Corry-Anke Brandsma. « A potential role for extracellular matrix proteins in lung ageing in COPD ». Dans ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa3404.

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Vyas-Read, Shilpa, Jennifer Colvocoresses-Dodds, Theresa W. Gauthier et Lou Ann Brown. « Hyperoxia Decreases Junctional Proteins And Promotes Extracellular Matrix In Alveolar Epithelial Cells ». Dans American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3938.

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Chung, Eunna, et M. N. Rylander. « Thermal Preconditioning Protocols for Cartilage Tissue Engineering ». Dans ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-193107.

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Successful creation of cartilaginous engineered tissues is often limited by insufficient cellular proliferation and formation of extracellular matrix. Stress conditioning protocols using heat have been shown to induce up-regulation of molecular chaperones called heat shock proteins (HSP) [1]. These proteins have been linked to enhanced cell proliferation and collagen synthesis which is critical for formation of the extracellular matrix. Therefore, identification of effective thermal stress preconditioning protocols that enhance HSP expression could substantially advance development of replacement tissues for cartilaginous tissues [2]. Our project focused on identifying thermal preconditioning protocols that enhance HSP70 expression while minimizing cellular injury for ultimate use in improving cell proliferation and extracellular matrix formation for cartilage.
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Sharma, Alpana, Rehan Khan, Suhasini Joshi, Manoj Sharma et Lalit Kumar. « Abstract B43 : Role of angiogenic factors and extracellular matrix proteins in multiple myeloma ». Dans Abstracts : AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Dec 6–9, 2009 ; Houston, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-09-b43.

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Krimmer, David I., Janette K. Burgess, Judith L. Black et Brian G. Oliver. « Cigarette Smoke Extract Induced Production Of Extracellular Matrix Proteins Is Attenuated By Simvastatin ». Dans American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a6054.

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Charo, I. F., L. A. Fitzgerald, D. Meyer, L. S. Bekeart et D. R. Phillips. « PLATELET GLYCOPROTEIN IIb-IIIa-LIKE PROTEINS MEDIATE ENDOTHELIAL CELL ATTACHMENT TO ADHESIVE MATRIX PROTEINS AND ARE UP-REGULATED BY PHORBOL ESTERS ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642816.

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Human endothelial cells (EC) express glycoproteins that are similar to the platelet glycoprotein IIb-IIIa complex (GP IIb-IIIa), the platelet receptor for adhesive proteins. Although GP IIb—IIIa is abundant in both platelets and EC, its only known function is to mediate platelet aggregation. The present study tests the hypotheses that EC attachment to adhesive proteins in the extracellular matrix is mediated by the GP IIb-IIIa-1ike proteins. Endothelial cells attached well to glass slides that were previously coated with adhesive proteins, but not albumin. To determine whether GP IIb-IIIa was involved, EC adherence was measured in the presence and absence of a GP IIb-IIIa monoclonal antibody (7E3) which inhibits fibrinogen (Fg) binding to platelets. The attachment of EC to Fg and von Willebrand factor (vWf), but not fibronectin (Fn) coated slides, was completely inhibited by 7E3. Attachment to vitronectin was partially inhibited. In contrast, EC attachment to Fn was specifically inhibited by a Fn-receptor antibody. Endothelial cell adherence to vWf was also inhibited by a monoclonal antibody (Mab9) against the GP IIb-IIIa binding domain of vWf, but not by antibodies agains.t other portions of vWf. We have further found that 7E3 disrupts monolayers of endothelial cells by detaching the cells from their extracellular matrix. EC incubated in phorbol myris-tate.acetate (PMA) increase in size and appear more tightly adherent to their extracellular matrix. To determine if PMA increases synthesis of cellular receptors for matrix proteins, we have used cDNA probes to measure the mRNA levels of the large subunit of the Fn-receptor (FnRα) and GP IIIa in EC. After a 4 hour incubation in the presence of PMA (10 nM), there was a 2-fold increase in the mRNA levels of both FnRα and GP IIIa, as well as increased cell spreading on the matrix. We conclude: i) the GP Ilb-IIIa complex in EC is a surface receptor for specific adhesive proteins, and is distinct from the FnR, and ii) both GP IIIa and FnRα synthesis are increased by PMA, which causes a concomittant change in cell morphology.
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Rapports d'organisations sur le sujet "Extracellular matrix proteins"

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Taylor, Mary. Extracellular Matrix Proteins of the Nurse Cell Capsule in Trichinella spiralis Infections. Portland State University Library, janvier 2000. http://dx.doi.org/10.15760/etd.6666.

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Barash, Itamar, J. Mina Bissell, Alexander Faerman et Moshe Shani. Modification of Milk Composition via Transgenesis : The Role of the Extracellular Matrix in Regulating Transgene Expression. United States Department of Agriculture, juillet 1995. http://dx.doi.org/10.32747/1995.7570558.bard.

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Altering milk composition via transgenesis depends on three main factors. (1) The availability of an efficient regulatory sequences for targeting transgene(s) to the mammary gland; (2) a reliable in vitro model to test the expression of transgenes prior to their introduction to the animal genome; and (3) better understanding of the major factors which determine the rate of gene expression and protein synthesis. The current studies provide the necessary means and knowledge to alter milk protein composition via transgenesis. The following specific goals were achieved: a: Identifying regulatory regions in the b-lactoglobulin (BLG) gene and the cross-talk between elements which enabled us to construct an efficient vector for the expression of desirable cDNA's in the mammary gland. b: The establishment of a sheep mammary cell line that serves as a model for the analysis of endogenous and exogenous milk protein synthesis in the mammary gland of livestock. c: An accurate comparison of the potency of the 5' regulatory sequences from the BLG and whey acidic protein (WAP) promoters in directing the expression of human serum albumin (HSA) to the mammary gland in vitro and in vivo. In this study we have also shown that sequences within the coding region may determine a specific pattern of expression for the transgene, distinct from that of the native milk protein genes. d: Characterizing the dominant role of ECM in transgene expression in mammary epithelial cells. e: Further characterization of the BCE-1 enhancer element in the promoter of the b-casein gene as a binding site for the c/EBP-b and Stat5. Identifying its interaction with chromatin and its up regulation by inhibitors of histone deacetylation. f: Identifying a mechanism of translational control as a mediator for the synergistic effect of insulin and prolactin on protein synthesis in the mammary gland.
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