Ruth Chiquet-Ehrismann

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Ruth Chiquet-Ehrismann
Born(1954-11-09)9 November 1954
Zürich, Switzerland
Died4 September 2015(2015-09-04) (aged 60)
Pratteln, Switzerland
Education ETH, Zürich (Ph.D. 1981)
Known forMatricellular proteins
AwardsHuggenberger-Bischoff Prize for Cancer Research, 1990
Scientific career
FieldsBiochemistry, cell biology
Institutions Johns Hopkins University, Baltimore; Friedrich Miescher Institute for Biomedical Research Basel; University of Basel
Doctoral advisors Hans M. Eppenberger; David C. Turner

Ruth Chiquet-Ehrismann (9 November 1954 – 4 September 2015) was a Swiss biochemist and cell biologist working on interactions in the extracellular matrix. [1] [2] [3]

Contents

Life

Ruth Chiquet-Ehrismann was born in Zürich. She received her Ph.D. from the ETH Zürich in 1981. Her mentors were Hans M. Eppenberger and David C. Turner. As a postdoctoral fellow she worked with Robert Dottin at the Johns Hopkins University in Baltimore, US. In 1984 she joined the Friedrich Miescher Institute for Biomedical Research in Basel as a Junior group leader and was promoted to Senior group leader in 1993.

In 2006 she was appointed as Adjunct Professor (Titularprofessorin) at the University of Basel. She was a board member of the Swiss Cancer League and the Cancer League of Basel, and chaired the Swiss Society for Connective Tissue Research. She served as a Council Member of the International Society for Matrix Biology. At the age of 60, she suffered a sudden death at her home in Pratteln, near Basel. [4]

Career

Ruth Chiquet-Ehrismann's research focused on the influence of the extracellular matrix on cell behavior, a very new field at the time. Today it is recognized that different matrix proteins influence cell adhesion, cell growth and migration, tissue morphology and signal transduction in specific and decisive ways. Chiquet-Ehrismann contributed pioneering work on the tenascin gene family of matricellular proteins, of which some members were discovered, cloned and sequenced by her group. Different tenascins have related domain organisations and their 3-6 subunits oligomerize into star-like structures ("hexabrachion"). Tenascin C interferes with the adhesion of many cells to fibronectin, which led to the concept that it is anti-adhesive[1, 2]. Tenascin C accumulates in the stroma of carcinomas and is a sensitive tumor marker that is involved in cancer metastasis. More recently, Ruth Chiquet-Ehrismann and her group discovered roles for tenascin C and tenascin W in stem cell[3] and cancer metastatic niches[4], and elucidated how tenascin C expression is controlled by the transcription factor MKL1, that links cellular mechanosensation to fibrosis and cancer progression[5]. Chiquet-Ehrismann and her group also discovered the teneurin gene family[6, 7]. These type II trans-membrane proteins are conserved throughout animals and function in germ cell development, neuronal pathfinding and CNS development. The cleaved intracellular domain functions in transcriptional regulation[8]. During 31 years of work at the Friedrich Miescher Institute, Chiquet-Ehrismann guided a very active research group. Many excellent Ph.D. students and postdoctoral fellows emerged from this group, who continue to develop the interesting field of matrix research. Her group had a high international reputation and collaborated with many scientists around the world [key publications 1-8]. She won the Huggenberger-Bischoff Prize for Cancer Research in 1990.

Key publications

Related Research Articles

<span class="mw-page-title-main">Fibronectin</span> Protein involved in cell adhesion, cell growth, cell migration and differentiation

Fibronectin is a high-molecular weight glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. It is approved for marketing as a topical solution in India by Central Drugs Standard Control organization in 2020 under the brand name FIBREGA for chronic wounds. Fibronectin also binds to other extracellular matrix proteins such as collagen, fibrin, and heparan sulfate proteoglycans.

Biological crosstalk refers to instances in which one or more components of one signal transduction pathway affects another. This can be achieved through a number of ways with the most common form being crosstalk between proteins of signaling cascades. In these signal transduction pathways, there are often shared components that can interact with either pathway. A more complex instance of crosstalk can be observed with transmembrane crosstalk between the extracellular matrix (ECM) and the cytoskeleton.

<span class="mw-page-title-main">Versican</span> Protein-coding gene in the species Homo sapiens

Versican is a large extracellular matrix proteoglycan that is present in a variety of human tissues. It is encoded by the VCAN gene.

<span class="mw-page-title-main">Tenascin</span>

Tenascins are extracellular matrix glycoproteins. They are abundant in the extracellular matrix of developing vertebrate embryos and they reappear around healing wounds and in the stroma of some tumors.

Teneurins are a family of phylogenetically conserved single-pass transmembrane glycoproteins expressed during pattern formation and morphogenesis. The name refers to "ten-a" and "neurons", the primary site of teneurin expression. Ten-m refers to tenascin-like protein major.

<span class="mw-page-title-main">Syndecan</span>

Syndecans are single transmembrane domain proteins that are thought to act as coreceptors, especially for G protein-coupled receptors. More specifically, these core proteins carry three to five heparan sulfate and chondroitin sulfate chains, i.e. they are proteoglycans, which allow for interaction with a large variety of ligands including fibroblast growth factors, vascular endothelial growth factor, transforming growth factor-beta, fibronectin and antithrombin-1. Interactions between fibronectin and some syndecans can be modulated by the extracellular matrix protein tenascin C.

<span class="mw-page-title-main">Tenascin X</span> Protein-coding gene in the species Homo sapiens

A member of the tenascin family, tenascin X (TN-X) also known as flexillin or hexabrachion-like protein is a 450kDa glycoprotein that is expressed in connective tissues. TN-X possesses a modular structure composed, from the N- to the C-terminal part by a Tenascin assembly domain (TAD), a series of 18.5 repeats of epidermal growth factor (EGF)-like motif, a high number of Fibronectin type III (FNIII) module, and a fibrinogen (FBG)-like globular domain. In humans, tenascin X is encoded by the TNXB gene.

<span class="mw-page-title-main">MMP7</span> Protein-coding gene in humans

Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme has also been known as matrin, putative metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP). Human MMP-7 has a molecular weight around 30 kDa.

<span class="mw-page-title-main">Tenascin C</span> Human protein-coding gene

Tenascin C (TN-C) is a glycoprotein that in humans is encoded by the TNC gene. It is expressed in the extracellular matrix of various tissues during development, disease or injury, and in restricted neurogenic areas of the central nervous system. Tenascin-C is the founding member of the tenascin protein family. In the embryo it is made by migrating cells like the neural crest; it is also abundant in developing tendons, bone and cartilage.

<span class="mw-page-title-main">CUTL1</span> Protein-coding gene in the species Homo sapiens

Cux1 is a homeodomain protein that in humans is encoded by the CUX1 gene.

<span class="mw-page-title-main">Collagen, type XIV, alpha 1</span> Protein found in humans

Collagen alpha-1(XIV) chain is a protein that in humans is encoded by the COL14A1 gene. It likely plays a role in collagen binding and cell-cell adhesion.

<span class="mw-page-title-main">Integrin alpha 9</span> Protein-coding gene in the species Homo sapiens

Integrin alpha-9 is a protein that in humans is encoded by the ITGA9 gene. Cytogenetic location: 3p22.2

<span class="mw-page-title-main">Integrin alpha 8</span> Protein-coding gene in the species Homo sapiens

Integrin alpha-8 is a protein that in humans is encoded by the ITGA8 gene.

<span class="mw-page-title-main">Laminin subunit gamma-3</span> Protein-coding gene in the species Homo sapiens

Laminin subunit gamma-3 also known as LAMC3 is a protein that in humans is encoded by the LAMC3 gene.

<span class="mw-page-title-main">Friedrich Miescher Institute for Biomedical Research</span> Facility in Basel, Switzerland

The Friedrich Miescher Institute for Biomedical Research (FMI) is a biomedical research institute founded in 1970. Based in Basel, Switzerland, the FMI is affiliated with the University of Basel and the Novartis Institutes for BioMedical Research (NIBR). It is named after Friedrich Miescher. As of 2021, the FMI has around 340 collaborators, of which 20 are research group leaders, over 80 are postdoctoral collaborators and over 80 are postgraduate students participating in the FMI International PhD Program. The FMI is directed by Dirk Schübeler.

<span class="mw-page-title-main">TENM3</span> Protein-coding gene in the species Homo sapiens

Teneurin-3, also known as Ten-m3, Odz3, Ten-m/Odz3, Tenascin-like molecule major 3 or Teneurin transmembrane protein 3, is a protein that, in humans, is encoded by the TENM3, or ODZ3, gene. Ten-m3 is a ~300 kDa type II transmembrane glycoprotein that is a member of the teneurin/Ten-m/Odz family. The teneurin family currently consists of four members: Ten-m1-Ten-m4. Ten-ms are conserved across both vertebrate and invertebrate species. They are expressed in distinct, but often interconnected, areas of the developing nervous system and in some non-neural tissues. Like the Ten-m family, Ten-m3 plays a critical role in regulating connectivity of the nervous system, particularly in axon pathfinding and synaptic organisation in the motor and visual system. Mutation in the TENM3/ODZ3 gene in humans has been associated with the eye condition, microphthalmia.

Susan M. Gasser is a Swiss molecular biologist. From 2004 to 2019 she was the director of the Friedrich Miescher Institute for Biomedical Research in Basel, Switzerland, where she also led a research group from 2004 until 2021. She was in parallel professor of molecular biology at the University of Basel until April 2021. Since January 2021, Susan Gasser is director of the ISREC Foundation, which supports translational cancer research. She is also professor invité at the University of Lausanne in the department of fundamental microbiology. She is an expert in quantitative biology and studies epigenetic inheritance and genome stability. Recipient of multiple swiss and European awards, she was named member of the US Academy of Sciences in 2022.

<span class="mw-page-title-main">Dirk Schübeler</span> German molecular biology researcher (born 1969)

Dirk Schübeler is a German researcher, Director of the Friedrich Miescher Institute for Biomedical Research (FMI) and professor at the University of Basel. He is an expert in gene regulation.

<span class="mw-page-title-main">Nicolas H. Thomä</span> German structural and chemical biologist

Nicolas H. Thomä is a German researcher, full professor at the EPFL School of Life Sciences and Director of the Paternot Chair for Cancer Research in Lausanne, Switzerland. He is a biochemist and structural biologist and a leading researcher in the fields of ubiquitin ligase biology and DNA repair.

<span class="mw-page-title-main">Prisca Liberali</span> Italian chemist

Prisca Liberali is an Italian chemist who is a senior group leader at the Friedrich Miescher Institute for Biomedical Research. Her research takes a systems biology approach to understand the behaviour of multi-cellular systems. She was awarded the EMBO Gold Medal and EMBO Membership in 2022.

References

  1. "Ruth Chiquet-Ehrismann". FMI. Archived from the original on 25 April 2016. Retrieved 17 April 2016.
  2. FMI. "Obituary Ruth Chiquet-Ehrismann (1954 - 2015)". www.fmi.ch. Retrieved 2024-01-17.
  3. Matthias, Gabriele Yvonne. "The Gender Gap In Science Is Still Very Real". Forbes. Retrieved 17 April 2016.
  4. "Memorial: Ruth Chiquet-Ehrismann: Tenascin Pioneer" (PDF). The Matrix Letter. 14 (2): 7–8. Retrieved 17 April 2016.