A. Hari Reddi

Last updated
A. Hari Reddi
Born
A. Hari Reddi

(1942-10-20) October 20, 1942 (age 82)
Chennai, India
Alma mater University of Delhi
Occupation Biologist
Known for Bone morphogenetic protein
Extracellular matrix
Tissue Engineering
Awards Marshall R. Urist Award
Scientific career
Institutions University of California
Johns Hopkins University
National Institutes of Health
University of Chicago

A. Hari Reddi (born October 20, 1942) is a University of California Distinguished Professor and holder of the Lawrence J. Ellison Endowed Chair in Musculoskeletal Molecular Biology at the University of California, Davis. [1] His research played an indispensable role in the identification, isolation and purification of bone morphogenetic proteins (BMPs) that are involved in bone formation and repair. [2] [3]

Contents

The molecular mechanism of bone induction studied by Professor Reddi led to the conceptual advance in tissue engineering that morphogens in the form of metabologens bound to an insoluble extracellular matrix scaffolding act in collaboration to stimulate stem cells to form cartilage and bone. [4] [5] [6] The Reddi laboratory has also made important discoveries unraveling the role of the extracellular matrix in bone and cartilage tissue regeneration and repair. [7] [8] [9] [10]

Professor Reddi was previously the Virginia M. and William A. Percy Chair and Professor in Orthopaedic Surgery, Professor of Biological Chemistry, and Professor of Oncology at the Johns Hopkins University School of Medicine. [11] He also past faculty member at the University of Chicago and senior scientist at the National Institutes of Health. [12]

Research

Professor Reddi discovered that bone induction is a sequential multistep cascade involving chemotaxis, mitosis, and differentiation. Early studies in his laboratory at the University of Chicago and National Institutes of Health unraveled the sequence of events involved in bone matrix-induce bone morphogenesis. [13] Using a battery of in vitro and in vivo bioassays for bone formation, a systematic study was undertaken in his laboratory to isolate and purify putative bone morphogenetic proteins. [14] Reddi and colleagues were the first to identify BMPs as pleiotropic regulators, acting in a concentration dependent manner. [15] They demonstrated first that BMPs bind the extracellular matrix, [16] [17] [18] [19] are present at the apical ectodermal ridge in the developing limb bud, [20] are chemotactic for human monocytes, [21] and have neurotropic potential. [22] His laboratory pioneered the use of BMPs in regenerative orthopedics and dentistry. [23] [24] [25] [26]

Professor Reddi's h-index is 109 with over 300 peer-reviewed manuscripts. [27] [28]

Education and Mentors

Hari Reddi received his PhD from the University of Delhi in reproductive endocrinology under the mentorship of M.R.N. Prasad. Reddi did postdoctoral work with Howard Guy Williams-Ashman at the Johns Hopkins University School of Medicine. Reddi was also a student of Charles Brenton Huggins, the winner of the 1966 Nobel Prize with Peyton Rous for the endocrine regulation of cancer.

International Conference of Bone Morphogenetic Proteins

Reddi is the founder of the International Conference on Bone Morphogenetic Proteins (BMPs). He organized the first conference at the Johns Hopkins University School of Medicine in 1994. The conference is held every two years rotating between the United States and an international venue. [29]

Awards and Honors

Related Research Articles

<span class="mw-page-title-main">Osteoblast</span> Cells secreting extracellular matrix

Osteoblasts are cells with a single nucleus that synthesize bone. However, in the process of bone formation, osteoblasts function in groups of connected cells. Individual cells cannot make bone. A group of organized osteoblasts together with the bone made by a unit of cells is usually called the osteon.

<span class="mw-page-title-main">Chondrocyte</span> Cell that composes 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.

Bone morphogenetic proteins (BMPs) are a group of growth factors also known as cytokines and as metabologens. Professor Marshall Urist and Professor Hari Reddi discovered their ability to induce the formation of bone and cartilage, BMPs are now considered to constitute a group of pivotal morphogenetic signals, orchestrating tissue architecture throughout the body. The important functioning of BMP signals in physiology is emphasized by the multitude of roles for dysregulated BMP signalling in pathological processes. Cancerous disease often involves misregulation of the BMP signalling system. Absence of BMP signalling is, for instance, an important factor in the progression of colon cancer, and conversely, overactivation of BMP signalling following reflux-induced esophagitis provokes Barrett's esophagus and is thus instrumental in the development of esophageal adenocarcinoma.

<span class="mw-page-title-main">Chondroblast</span> Mesenchymal progenitor cell that forms a chondrocyte

Chondroblasts, or perichondrial cells, is the name given to mesenchymal progenitor cells in situ which, from endochondral ossification, will form chondrocytes in the growing cartilage matrix. Another name for them is subchondral cortico-spongious progenitors. They have euchromatic nuclei and stain by basic dyes.

<span class="mw-page-title-main">Bone morphogenetic protein 2</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 2 or BMP-2 belongs to the TGF-β superfamily of proteins.

<span class="mw-page-title-main">Bone morphogenetic protein 4</span> Human protein and coding gene

Bone morphogenetic protein 4 is a protein that in humans is encoded by BMP4 gene. BMP4 is found on chromosome 14q22-q23.

<span class="mw-page-title-main">Bone morphogenetic protein 8B</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 8B is a protein that in humans is encoded by the BMP8B gene.

<span class="mw-page-title-main">Bone morphogenetic protein 6</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 6 is a protein that in humans is encoded by the BMP6 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 1</span> Mammalian protein found in Homo sapiens

Bone morphogenetic protein 1, also known as BMP1, is a protein which in humans is encoded by the BMP1 gene. There are seven isoforms of the protein created by alternate splicing.

<span class="mw-page-title-main">Bone morphogenetic protein 3</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 3, also known as osteogenin, is a protein in humans that is encoded by the BMP3 gene.

<span class="mw-page-title-main">BMPR1A</span> Bone morphogenetic protein receptor

The bone morphogenetic protein receptor, type IA also known as BMPR1A is a protein which in humans is encoded by the BMPR1A gene. BMPR1A has also been designated as CD292.

Growth differentiation factors (GDFs) are a subfamily of proteins belonging to the transforming growth factor beta superfamily that have functions predominantly in development.

<span class="mw-page-title-main">GDF3</span> Protein-coding gene in humans

Growth differentiation factor-3 (GDF3), also known as Vg-related gene 2 (Vgr-2) is protein that in humans is encoded by the GDF3 gene. GDF3 belongs to the transforming growth factor beta (TGF-β) superfamily. It has high similarity to other TGF-β superfamily members including Vg1 and GDF1.

<span class="mw-page-title-main">GDF5</span> Protein-coding gene in the species Homo sapiens

Growth/differentiation factor 5 is a protein that in humans is encoded by the GDF5 gene.

<span class="mw-page-title-main">GDF6</span> Protein-coding gene in the species Homo sapiens

Growth differentiation factor 6 (GDF6) is a protein that in humans is encoded by the GDF6 gene.

<span class="mw-page-title-main">GDF10</span> Protein-coding gene in the species Homo sapiens

Growth differentiation factor 10 (GDF10) also known as bone morphogenetic protein 3B (BMP-3B) is a protein that in humans is encoded by the GDF10 gene.

<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">Collagen, type IV, alpha 2</span>

Collagen alpha-2(IV) chain is a protein that in humans is encoded by the COL4A2 gene.

<span class="mw-page-title-main">CDH15</span> Protein-coding gene in humans

Cadherin-15 is a protein that in humans is encoded by the CDH15 gene.

<span class="mw-page-title-main">FREM2</span> Protein-coding gene in the species Homo sapiens

FRAS1-related extracellular matrix protein 2 is a protein that in humans is encoded by the FREM2 gene.

References

  1. ↑ "Dr. A. Hari Reddi, M.S., Ph.D. For UC Davis Health".
  2. ↑ Scientists Succeed In Growing Bone, The New York Times, Oct. 22, 1996
  3. ↑ Hopkins grows its own bone orchard, The Baltimore Sun, Jan. 24, 1992
  4. ↑ Khouri R, Koudsi B, Reddi H. Tissue Transformation Into Bone In Vivo: A Potential Practical Application. Journal of the American Medical Association JAMA. 1991;266(14):1953-1955
  5. ↑ Sampath TK, Nathanson MA, Reddi AH. In vitro transformation of mesenchymal cells derived from embryonic muscle into cartilage in response to extracellular matrix components of bone. Proc Natl Acad Sci U S A 1984; 81:3419-23.
  6. ↑ Muscle Is Turned Into Bone By Researchers in St. Louis, The New York Times, Oct. 9, 1991
  7. ↑ Reddi AH, Gay R, Gay S, Miller EJ. Transitions in collagen types during matrix-induced cartilage, bone, and bone marrow formation. Proc Natl Acad Sci U S A 1977; 74:5589-92.
  8. ↑ Weiss RE, Reddi AH. Synthesis and localization of fibronectin during collagenous matrix- mesenchymal cell interaction and differentiation of cartilage and bone in vivo. Proc Natl Acad Sci U S A 1980; 77:2074-8.
  9. ↑ Sampath TK, Reddi AH. Importance of geometry of the extracellular matrix in endochondral bone differentiation. J Cell Biol 1984; 98:2192-7.
  10. ↑ Vukicevic S, Luyten FP, Kleinman HK, Reddi AH. Differentiation of canalicular cell processes in bone cells by basement membrane matrix components: regulation by discrete domains of laminin. Cell 1990; 63:437-45.
  11. ↑ "Johns Hopkins Gazette: April 15, 1996".
  12. ↑ Furchgott, Roy (1993-04-04). "Technology; Urging the Bones to Heal". The New York Times. ISSN   0362-4331 . Retrieved 2024-07-28.
  13. ↑ Reddi, A. H.; Huggins, C. (1972). "Biochemical Sequences in the Transformation of Normal Fibroblasts in Adolescent Rat". PNAS 69 (6): 1601–1605. doi:10.1073/pnas.69.6.1601.
  14. ↑ Sampath TK, Reddi AH. Dissociative extraction and reconstitution of extracellular matrix components involved in local bone differentiation. Proc Natl Acad Sci U S A 1981; 78:7599-603.
  15. ↑ Reddi AH. Bone and cartilage differentiation. Curr Opin Genet Dev 1994; 4:737-44.
  16. ↑ Sampath TK, Reddi AH. Homology of bone-inductive proteins from human, monkey, bovine, and rat extracellular matrix. Proc Natl Acad Sci U S A 1983; 80:6591-5.
  17. ↑ Sampath TK, Muthukumaran N, Reddi AH. Isolation of osteogenin, an extracellular matrix-associated, bone- inductive protein, by heparin affinity chromatography. Proc Natl Acad Sci U S A 1987; 84:7109-13.
  18. ↑ Paralkar VM, Nandedkar AK, Pointer RH, Kleinman HK, Reddi AH. Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen. J Biol Chem 1990; 265:17281-4.
  19. ↑ Paralkar VM, Vukicevic S, Reddi AH. Transforming growth factor beta type 1 binds to collagen IV of basement membrane matrix: implications for development. Dev Biol 1991; 143:303-8.
  20. ↑ Carrington JL, Chen P, Yanagishita M, Reddi AH. Osteogenin (bone morphogenetic protein-3) stimulates cartilage formation by chick limb bud cells in vitro. Dev Biol 1991; 146:406-15.
  21. ↑ Cunningham NS, Paralkar V, Reddi AH. Osteogenin and recombinant bone morphogenetic protein 2B are chemotactic for human monocytes and stimulate transforming growth factor beta 1 mRNA expression. Proc Natl Acad Sci U S A 1992; 89:11740-4.
  22. ↑ Paralkar VM, Weeks BS, Yu YM, Kleinman HK, Reddi AH. Recombinant human bone morphogenetic protein 2B stimulates PC12 cell differentiation: potentiation and binding to type IV collagen. J Cell Biol 1992; 119:1721-8.
  23. ↑ Ripamonti U, Ma S, Cunningham NS, Yeates L, Reddi AH. Initiation of bone regeneration in adult baboons by osteogenin, a bone morphogenetic protein. Matrix 1992; 12:369-80.
  24. ↑ Ripamonti U, Heliotis M, van den Heever B, Reddi AH. Bone morphogenetic proteins induce periodontal regeneration in the baboon (Papio ursinus) [published erratum appears in J Periodontal Res 1995 Mar;30(2):149-51]. J Periodontal Res 1994; 29:439-45.
  25. ↑ Reddi AH. Role of morphogenetic proteins in skeletal tissue engineering and regeneration. Nat Biotechnol. 1998 Mar;16(3):247-52.
  26. ↑ Nakashima M, Reddi AH. The application of bone morphogenetic proteins to dental tissue engineering. Nature Biotechnology. 2003 Sept; 21(9):1025-1032.
  27. ↑ "A. Hari Reddi". scholar.google.com. Retrieved 2024-10-26.
  28. ↑ "reddi ah - Search Results - PubMed". PubMed. Retrieved 2024-10-26.
  29. ↑ http://userpage.fu-berlin.de/bmp/
  30. ↑ "Kappa Delta Awards and OREF Clinical Research Award - American Academy of Orthopaedic Surgeons". www.aaos.org. Retrieved 2024-07-29.
  31. ↑ "ORS Marshall R. Urist, MD Award". Orthopedic Research Society. Retrieved 13 June 2024.
  32. ↑ "Nicolas Andry Lifetime Achievement Award Winners". The Association of Bone and Joint Surgeons. Retrieved 13 June 2024.
  33. ↑ "13 UC innovators elected to the National Academy of Inventors". University of California Newsroom. Retrieved 24 June 2024.
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