Bonnie Sloane

Last updated
Bonnie F. Sloane
Alma materRutgers University
Scientific career
Thesis Alterations in lysosomal enzyme activity in rat uterine muscle as affected by the hormonal state of the muscle  (1976)

Bonnie Fiedorek Sloane was a distinguished professor at Wayne State University known for her research on cancer. In 2021 she was elected a fellow of the American Association for the Advancement of Science.

Contents

Education and Career

Sloane was born in 1944 in Pittsburgh, Pennsylvania. [1] Sloane has a B.S. (1966) [1] and an M.A. (1968) from Duke University (1966). She earned her Ph.D. from Rutgers University in 1976. Following her Ph.D. she did postdoctoral work at the University of Pennsylvania, [2] and in 1979 was an assistant professor at the University of Pennsylvania. She then moved to Michigan State University where she was an assistant professor from 1979 until 1980 when she moved to Wayne State University as an assistant professor in the Department of Pharmacology. She was promoted to associate professor in 1984 and to professor in 1989, and in 2005 she was named distinguished professor. [1] From 1995 until 2015, she served as chair of the Department of Pharmacology, the first woman to serve as chair of a department in the Wayne State University School of Medicine.

From 2009 until 2011, Sloane was president of the Association of Medical Pharmacology, the first woman to serve in this role. [3]

Research

Sloane is known for her research on cancer, especially breast cancer. Her research has examined cathepsins [4] [5] and proteases [6] associated with cancer. She has also used imaging with fluorescent probes to track the activity of proteases. [7]

Selected Publications

Awards and Honors

In 1996, Sloane was elected to the Wayne State University Academy of Scholars. In 2021 Sloane was named a fellow of the American Association for the Advancement of Science. [8]

Related Research Articles

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<span class="mw-page-title-main">Cathepsin</span> Family of proteases

Cathepsins are proteases found in all animals as well as other organisms. There are approximately a dozen members of this family, which are distinguished by their structure, catalytic mechanism, and which proteins they cleave. Most of the members become activated at the low pH found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. Cathepsins have a vital role in mammalian cellular turnover.

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

Cathepsin S is a protein that in humans is encoded by the CTSS gene. Transcript variants utilizing alternative polyadenylation signals exist for this gene.

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

Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in intracellular proteolysis. In humans, cathepsin B is encoded by the CTSB gene. Cathepsin B is upregulated in certain cancers, in pre-malignant lesions, and in various other pathological conditions.

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

Cathepsin D is a protein that in humans is encoded by the CTSD gene. This gene encodes a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to degrade proteins and activate precursors of bioactive proteins in pre-lysosomal compartments. This proteinase, which is a member of the peptidase A1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of the CTSD gene is initiated from several sites, including one that is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease. Homozygous deletion of the CTSD gene leads to early lethality in the postnatal phase. Deficiency of CTSD gene has been reported an underlying cause of neuronal ceroid lipofuscinosis (NCL).

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

Cathepsin H is a protein that in humans is encoded by the CTSH gene.

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

Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of the cysteine cathepsin family of cysteine proteases, which has 11 members. As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in cancer malignancy and inflammation.

<span class="mw-page-title-main">Cathepsin F</span> Protein-coding gene in the species Homo sapiens (Humans)

Cathepsin F is a protein that in humans is encoded by the CTSF gene.

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<span class="mw-page-title-main">Papain-like protease</span> Protein family of cysteine protease enzymes

Papain-like proteases are a large protein family of cysteine protease enzymes that share structural and enzymatic properties with the group's namesake member, papain. They are found in all domains of life. In animals, the group is often known as cysteine cathepsins or, in older literature, lysosomal peptidases. In the MEROPS protease enzyme classification system, papain-like proteases form Clan CA. Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile.

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References

  1. 1 2 3 "Bonnie Fiedorek Sloane | WorldCat.org". www.worldcat.org. Retrieved 2022-12-31.
  2. "Bonnie Sloane". Wayne State University. 2013-10-03. Retrieved 2022-12-30.
  3. "People making news". Detroit Free Press. 2008-09-21. p. 58. Retrieved 2022-12-31.
  4. Sloane, Bonnie F.; Dunn, John R.; Honn, Kenneth V. (1981-06-05). "Lysosomal Cathepsin B: Correlation with Metastatic Potential". Science. 212 (4499): 1151–1153. Bibcode:1981Sci...212.1151S. doi:10.1126/science.7233209. ISSN   0036-8075. PMID   7233209. S2CID   33974450.
  5. Mohamed, Mona Mostafa; Sloane, Bonnie F. (2006). "multifunctional enzymes in cancer". Nature Reviews Cancer. 6 (10): 764–775. doi:10.1038/nrc1949. ISSN   1474-175X. PMID   16990854. S2CID   26463930.
  6. Koblinski, Jennifer E; Ahram, Mamoun; Sloane, Bonnie F (2000-02-15). "Unraveling the role of proteases in cancer". Clinica Chimica Acta. 291 (2): 113–135. doi:10.1016/S0009-8981(99)00224-7. ISSN   0009-8981. PMID   10675719.
  7. Blum, Galia; Mullins, Stefanie R; Keren, Kinneret; Fonovič, Marko; Jedeszko, Christopher; Rice, Mark J; Sloane, Bonnie F; Bogyo, Matthew (2005-09-01). "Dynamic imaging of protease activity with fluorescently quenched activity-based probes". Nature Chemical Biology. 1 (4): 203–209. doi:10.1038/nchembio728. ISSN   1552-4450. PMID   16408036. S2CID   9606676.
  8. "2021 AAAS Fellows approved by the AAAS Council". Science. 375 (6579): 393–397. 2022-01-28. Bibcode:2022Sci...375..393.. doi:10.1126/science.ada0325. ISSN   0036-8075. S2CID   246359998.