Marian Young

Last updated
Marian Young
Marian Young.jpg
Alma mater State University of New York at Oneonta
University of Connecticut
Scientific career
FieldsDevelopmental biology
Institutions National Institute of Dental and Craniofacial Research
Thesis Serum Protein Synthesis in the Extraembryonic Endoderm of the Early Chick Embryo  (1981)

Marian Frances Young is an American developmental biologist researching the function of extracellular matrix proteins in skeletal tissues. She is the deputy scientific director of the division of intramural research at the National Institute of Dental and Craniofacial Research.

Contents

Education

Young completed a bachelor's degree at State University of New York at Oneonta. [1] She earned a Ph.D. in developmental biology from the University of Connecticut in the department of genetics and cell biology. [2] Her 1981 dissertation was titled, Serum Protein Synthesis in the Extraembryonic Endoderm of the Early Chick Embryo. [3] In 1981, Young came to the National Institute of Dental and Craniofacial Research (NIDCR) as a postdoctoral fellow to work with George Martin, the chief of the lab of craniofacial and developmental anomalies (LDBA) branch. Her postdoctoral work in the LDBA ranch from 1981 to 1983 investigated the structure, function, and regulation of matrix genes made by cartilage tissue. [1]

Career

Postbaccalaureate researcher Andrew Donald (left) and Young (right) examining the temporomandibular joint in a plastic replica of the craniofacial bones in a human skull in 2012 Andrew Donald and Marian Young in 2012.jpg
Postbaccalaureate researcher Andrew Donald (left) and Young (right) examining the temporomandibular joint in a plastic replica of the craniofacial bones in a human skull in 2012

Young became staff fellow/tenure-track investigator in 1983 in the mineralized tissue branch (MTB) led by John Termine. [1] There, she began investigations on the molecular biology and function of extracellular matrix (ECM) proteins in skeletal tissues. [2] In 1990, Young became a tenured senior investigator of the molecular biology of bones and teeth section in the MTB which subsequently became the craniofacial and skeletal diseases branch led by Pamela Robey. [1]

Young has organized symposia and scientific conferences on the topic of bones and teeth, mineralization, and the ECM including the Gordon Research Conference (GRC) on Bones and Teeth (1997), a symposium on the ECM in the Craniofacial Complex, AADR (2004) and the GRC on Proteoglycans (2010). Young has served on numerous committees at the NIH related to promotion and tenure action, oversight of animal facilities, and coordination of summer student research. She has supervised dozens of research fellows and students. [2]

As of 2018, Young was a senior investigator and chief of the molecular biology of bones and teeth section. [1] In August 2018, she was appointed deputy scientific director of the NIDCR division of intramural research. [2]

Research

Marian Young’s research section explores the function of ECM proteins found in skeletal tissues. The focus is on the small leucine-rich proteoglycans (SLRPs) biglycan (bgn), decorin (dcn), and fibromodulin (fmod), and the Wnt target gene known as WISP1. Young’s research explores how these ECM components control skeletal tissue function via both anabolic (through differentiation and formation) and catabolic (breakdown or resorption) mechanisms which, in some cases, work by modulating growth factor availability. The group also investigates how stem cell fate can be regulated by the ECM in multiple skeletal sites including bones, teeth, cartilage, and tendon. The ultimate purpose of the research is to develop practical applications for these ECM components in ameliorating diseases such as osteopenia, osteoarthritis, and ectopic bone formation in soft tissues. [2]

Awards

Young received an honorary doctorate from her undergraduate alma mater State University of New York (SUNY) at Oneonta in 1998. In 2012, she was awarded the NIH Directors Award for Mentorship. [1] In 2014, Young received a Ruth L. Kirschstein Mentoring award. [2] In 2018, Young received the Stephen M. Krane Award from the American Society for Bone and Mineral Research in recognition of outstanding achievements in basic, translational, or clinical research in inflammation and/or skeletal matrix biology. [1]

Related Research Articles

<span class="mw-page-title-main">Tendon</span> Type of tissue that connects muscle to bone

A tendon or sinew is a tough band of dense fibrous connective tissue that connects muscle to bone. It sends the mechanical forces of muscle contraction to the skeletal system, while withstanding tension.

<span class="mw-page-title-main">Cartilage</span> Resilient and smooth elastic tissue in animals

Cartilage is a resilient and smooth type of connective tissue. It is a semi-transparent and non-porous type of tissue. It is usually covered by a tough and fibrous membrane called perichondrium. In tetrapods, it covers and protects the ends of long bones at the joints as articular cartilage, and is a structural component of many body parts including the rib cage, the neck and the bronchial tubes, and the intervertebral discs. In other taxa, such as chondrichthyans, but also in cyclostomes, it may constitute a much greater proportion of the skeleton. It is not as hard and rigid as bone, but it is much stiffer and much less flexible than muscle. The matrix of cartilage is made up of glycosaminoglycans, proteoglycans, collagen fibers and, sometimes, elastin. It usually grows quicker than bone.

<span class="mw-page-title-main">Extracellular matrix</span> Network of proteins and molecules outside cells that provides structural support for cells

In biology, the extracellular matrix (ECM), also called intercellular matrix, is a network consisting of extracellular macromolecules and minerals, such as collagen, enzymes, glycoproteins and hydroxyapatite that provide structural and biochemical support to surrounding cells. Because multicellularity evolved independently in different multicellular lineages, the composition of ECM varies between multicellular structures; however, cell adhesion, cell-to-cell communication and differentiation are common functions of the ECM.

The National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS) is one of the institutes and centers that make up the National Institutes of Health, an agency of the United States Department of Health and Human Services (HHS).

In biology, matrix is the material in between an eukaryotic organism's cells.

<span class="mw-page-title-main">Chondrocyte</span> Cell that makes up cartilage

Chondrocytes are the only cells found in healthy cartilage. They produce and maintain the cartilaginous matrix, which consists mainly of collagen and proteoglycans. Although the word chondroblast is commonly used to describe an immature chondrocyte, the term is imprecise, since the progenitor of chondrocytes can differentiate into various cell types, including osteoblasts.

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

Ameloblasts are cells present only during tooth development that deposit tooth enamel, which is the hard outermost layer of the tooth forming the surface of the crown.

<span class="mw-page-title-main">Human tooth development</span> Process by which teeth form

Tooth development or odontogenesis is the complex process by which teeth form from embryonic cells, grow, and erupt into the mouth. For human teeth to have a healthy oral environment, all parts of the tooth must develop during appropriate stages of fetal development. Primary (baby) teeth start to form between the sixth and eighth week of prenatal development, and permanent teeth begin to form in the twentieth week. If teeth do not start to develop at or near these times, they will not develop at all, resulting in hypodontia or anodontia.

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

The dental follicle, also known as dental sac, is made up of mesenchymal cells and fibres surrounding the enamel organ and dental papilla of a developing tooth. It is a vascular fibrous sac containing the developing tooth and its odontogenic organ. The dental follicle (DF) differentiates into the periodontal ligament. In addition, it may be the precursor of other cells of the periodontium, including osteoblasts, cementoblasts and fibroblasts. They develop into the alveolar bone, the cementum with Sharpey's fibers and the periodontal ligament fibers respectively. Similar to dental papilla, the dental follicle provides nutrition to the enamel organ and dental papilla and also have an extremely rich blood supply.

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

Perlecan (PLC) also known as basement membrane-specific heparan sulfate proteoglycan core protein (HSPG) or heparan sulfate proteoglycan 2 (HSPG2), is a protein that in humans is encoded by the HSPG2 gene. The HSPG2 gene codes for a 4,391 amino acid protein with a molecular weight of 468,829. It is one of the largest known proteins. The name perlecan comes from its appearance as a "string of pearls" in rotary shadowed images.

<span class="mw-page-title-main">Mesenchyme</span> Type of animal embryonic connective tissue

Mesenchyme is a type of loosely organized animal embryonic connective tissue of undifferentiated cells that give rise to most tissues, such as skin, blood or bone. The interactions between mesenchyme and epithelium help to form nearly every organ in the developing embryo.

FACIT collagen is a type of collagen and also a proteoglycan that have two or more triple-helical domains that connect to collagen fibrils and share protein domains with non-collagen matrix molecules. FACIT collagens derive their name from their association and interaction with fibrillar collagens. Unlike fibrillar collagens, which form long fibers.

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

Dermatopontin also known as tyrosine-rich acidic matrix protein (TRAMP) is a protein that in humans is encoded by the DPT gene. Dermatopontin is a 22-kDa protein of the noncollagenous extracellular matrix (ECM) estimated to comprise 12 mg/kg of wet dermis weight. To date, homologues have been identified in five different mammals and 12 different invertebrates with multiple functions. In vertebrates, the primary function of dermatopontin is a structural component of the ECM, cell adhesion, modulation of TGF-β activity and cellular quiescence). It also has pathological involvement in heart attacks and decreased expression in leiomyoma and fibrosis. In invertebrate, dermatopontin homologue plays a role in hemagglutination, cell-cell aggregation, and expression during parasite infection.

<span class="mw-page-title-main">Laminin 111</span>

Laminin–111 is a protein of the type known as laminin isoforms. It was among the first of the laminin isoforms to be discovered. The "111" identifies the isoform's chain composition of α1β1γ1. This protein plays an important role in embryonic development. Injections of this substance are used in treatment for Duchenne muscular dystrophy, and its cellular action may potentially become a focus of study in cancer research.

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Pamela Gehron Robey is an American cell biologist. She is a senior investigator in the skeletal biology section at the National Institute of Dental and Craniofacial Research.

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References

  1. 1 2 3 4 5 6 7 "NIDCR Names Deputy Scientific Director". National Institute of Dental and Craniofacial Research. August 2018. Retrieved 2021-03-21.PD-icon.svg This article incorporates text from this source, which is in the public domain .
  2. 1 2 3 4 5 6 "Marian Young, PhD". National Institute of Dental and Craniofacial Research. Retrieved 2021-03-21.PD-icon.svg This article incorporates text from this source, which is in the public domain .
  3. Young, Marian Frances (1981). Serum Protein Synthesis in the Extraembryonic Endoderm of the Early Chick Embryo (Ph.D. thesis). University of Connecticut. OCLC   63578318.
PD-icon.svg This article incorporates public domain material from websites or documents of the National Institutes of Health.