Alan Krensky is executive for development at Northwestern Medicine and vice dean for development and alumni relations at Northwestern's Feinberg School of Medicine. He was previously senior investigator in the Laboratory of Cellular and Molecular Biology at the National Institutes of Health (NIH) and served as the first director of the Office of Portfolio Analysis and Strategic Initiatives (OPASI) and a deputy director of NIH. [1] He was Associate Dean for Children’s Health and the Shelagh Galligan Professor of Pediatrics at Stanford University.
Krensky was born in Chicago, Illinois in 1951 and attended New Trier High School (East). He received a B.A. in biology, Summa Cum Laude, and M.D. from the University of Pennsylvania. He was a Resident (medicine) and Fellow in Pediatrics at Children’s Hospital Boston and a research fellow at Dana Farber Cancer Institute, Boston. After one year on the faculty at Harvard and Boston Children’s Hospital, he moved to Stanford in 1984. He was on the faculty at Stanford for 23 years and developed the Children’s Health Initiative, a $500 million investment in research, education and clinical care, at Stanford and Lucile Packard Children's Hospital. [2] [3]
Krensky has published more than 280 papers and chapters in immunology and pediatrics, and holds 12 U.S. patents. He identified the human lymphocyte function-associated antigens 1-3, [4] [5] immunomodulatory HLA derived peptides (AllotrapTM), [6] chemokine RANTES (CCL5), proinflammatory and cytotoxic molecule granulysin (GNLY) and the transcription factor Kruppel-like factor 13 (KLF13).
At NIH, Krensky oversaw the Roadmap for Medical Research (Biomedical Research), introducing new programs in Epigenomics, Human Microbiome and Transformative RO1s. [7] Roadmap projects are designed to rapidly respond to emerging scientific opportunities and public health needs. He led the development of the [Research, Condition, and Disease Categorization (RCDC)] system, [8] a computerized tool to permit transparent accounting of NIH funding, and a Science of Science Management effort to develop metrics for accountability in scientific progress. He co-chaired the NIH [Council of Councils], [9] with responsibility for trans-NIH initiatives. [10] [11] [12]
Krensky holds numerous awards, including the American Academy of Pediatrics Award for Excellence in Pediatric Research, E. Mead Johnson Award for Research in Pediatrics, and Novartis Established Investigator Award of the American Society of Transplantation. He served as president of the Society for Pediatric Research and secretary treasurer of the American Society of Nephrology. He is a member of the American Society for Clinical Investigation and Association of American Physicians.
Chemokine ligand 5 is a protein which in humans is encoded by the CCL5 gene. The gene has been discovered in 1990 by in situ hybridisation and it is localised on 17q11.2-q12 chromosome. It is also known as RANTES. RANTES was first described by Dr. Tom Schall who named the protein, the original source of the name Rantes was from the Argentine movie Man Facing Southeast about an alien who shows up in a mental ward who was named Rantés, the rather clunky acronym was only made to fit the name.
HLA-DR is an MHC class II cell surface receptor encoded by the human leukocyte antigen complex on chromosome 6 region 6p21.31. The complex of HLA-DR and peptide, generally between 9 and 30 amino acids in length, constitutes a ligand for the T-cell receptor (TCR). HLA were originally defined as cell surface antigens that mediate graft-versus-host disease. Identification of these antigens has led to greater success and longevity in organ transplant.
HLA class II histocompatibility antigen, DR alpha chain is a protein that in humans is encoded by the HLA-DRA gene. HLA-DRA encodes the alpha subunit of HLA-DR. Unlike the alpha chains of other Human MHC class II molecules, the alpha subunit is practically invariable. However it can pair with, in any individual, the beta chain from 3 different DR beta loci, DRB1, and two of any DRB3, DRB4, or DRB5 alleles. Thus there is the potential that any given individual can form 4 different HLA-DR isoforms.
CD2 is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells. It has also been called T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, erythrocyte receptor and rosette receptor.
Lymphocyte function-associated antigen 1 (LFA-1) is an integrin found on lymphocytes and other leukocytes. LFA-1 plays a key role in emigration, which is the process by which leukocytes leave the bloodstream to enter the tissues. LFA-1 also mediates firm arrest of leukocytes. Additionally, LFA-1 is involved in the process of cytotoxic T cell mediated killing as well as antibody mediated killing by granulocytes and monocytes. As of 2007, LFA-1 has 6 known ligands: ICAM-1, ICAM-2, ICAM-3, ICAM-4, ICAM-5, and JAM-A. LFA-1/ICAM-1 interactions have recently been shown to stimulate signaling pathways that influence T cell differentiation. LFA-1 belongs to the integrin superfamily of adhesion molecules.
Major histocompatibility complex, class II, DQ alpha 1, also known as HLA-DQA1, is a human gene present on short arm of chromosome 6 (6p21.3) and also denotes the genetic locus which contains this gene. The protein encoded by this gene is one of two proteins that are required to form the DQ heterodimer, a cell surface receptor essential to the function of the immune system.
HLA class II histocompatibility antigen, DP(W2) beta chain is a protein that in humans is encoded by the HLA-DPB1 gene.
HLA class II histocompatibility antigen, DRB3-1 beta chain is a protein that in humans is encoded by the HLA-DRB3 gene.
HLA class II histocompatibility antigen, DM beta chain is a protein that in humans is encoded by the HLA-DMB gene.
HLA class II histocompatibility antigen, DM alpha chain is a protein that in humans is encoded by the HLA-DMA gene.
Granulysin (GNLY) is a protein expressed in most mammals which functions as an antimicrobial peptide released by killer lymphocytes in cytotoxic granules. It is a pore-forming peptide, as it can puncture a microbial cell wall, allowing for other death-inducing enzymes to enter the microbe and cause microptosis. GNLY is inhibited by cholesterol, and is most effective in helping to kill cholesterol-deficient microbes.
HLA class II histocompatibility antigen, DO alpha chain is a protein that in humans is encoded by the HLA-DOA gene.
HLA class II histocompatibility antigen, DO beta chain is a protein that in humans is encoded by the HLA-DOB gene.
Protein melan-A also known as melanoma antigen recognized by T cells 1 or MART-1 is a protein that in humans is encoded by the MLANA or "MALENA" gene. A fragment of the protein, usually consisting of the nine amino acids 27 to 35, is bound by MHC class I complexes which present it to T cells of the immune system. These complexes can be found on the surface of melanoma cells. Decameric peptides (26-35) are being investigated as cancer vaccines.
CD160 antigen is a protein that in humans is encoded by the CD160 gene.
HLA class II histocompatibility antigen, DX beta chain is a protein that in humans is encoded by the HLA-DQB2 gene.
Eugene C. "Gene" Butcher is an American immunologist and a professor of pathology at Stanford University.
Timothy "Tim" A. Springer, Ph.D. is an immunologist and Latham Family Professor at Harvard Medical School. Springer is best known for his pioneering work in discovering the first integrins and intercellular adhesion molecules (ICAMs) and elucidating how these cell adhesion molecules function in the immune system. His innovative use of monoclonal antibodies in his research paved the way for the development of therapeutic antibodies, known as selective adhesion molecule inhibitors, to treat autoimmune diseases. In recent years, Springer's research interest has expanded to include malaria, transforming growth factor beta (TGF-β) signaling molecules, and von Willebrand factor.
Gene Martin Shearer is an American immunologist who works at the National Institutes of Health (NIH). He first achieved fame for his discovery in 1974 that T lymphocytes recognized chemically modified surface antigens only in the context of self major histocompatibility complex (MHC) encoded molecules, identifying the central feature of antigen recognition by T lymphocytes known as MHC restriction. His discovery of MHC restriction using chemically modified surface antigens was simultaneous with the discovery of MHC restricted T lymphocyte recognition of virus infected cells by Rolf Zinkernagel and Peter Doherty, who received the 1996 Nobel Prize in Physiology or Medicine.
Carol Shoshkes Reiss, an American viral immunologist, has been professor in New York University's department of biology since 1991. Her research focused on the dynamic contest between the mouse immune system and virus replication during infection of the central nervous system. Reiss was editor-in-chief of the journal Viral Immunology (2000–2006) and is currently editor-in-chief of the journal DNA and Cell Biology (2012–present).