Kenneth M. Baldwin

Professor Emeritus, Physiology & Biophysics
School of Medicine

PH.D., University of Iowa, 1970

Phone: (949) 824-7192, 4249
Fax: (949) 824-8540
Email: kmbaldwi@uci.edu

University of California, Irvine
D352 Medical Sciences 1
Mail Code: 4560
Irvine, CA 92697

picture of Kenneth M. Baldwin

Research
Interests
Skeletal isomyosin; thyroid control of cardiac isomyosin; Regulation of myosin gene expression
   
URL www.ucihs.uci.edu/pandb/faculty/kmbres.html
   
Academic
Distinctions
Academic Background:

1973-Present: Department of Physiology and Biophysics College of Medicine; University of California, Irvine 92717

1988-1996; Senior Associate Dean of Academic Affairs; School of Medicine; UCI

Positions:

1973 – 1979 Assistant Professor, University of California, Irvine
1979 – 1984 Associate Professor, University of California, Irvine
1984 – present Professor, Dept. of Physiology & Biophysics, College of Medicine, University of California Irvine
1988 – 1996 Senior Associate Dean, College of Medicine, University of 2000-California, Irvine
2000-2008 National Space Biomedical Research Institute(NSBRI): Team Leader for Muscle Atrophy and Alteratioins Research Group
2012 - present Emeritus Professor Recalled


Honors & Awards:

1988 Am. Physiology Society Adolf Award in Exercise Physiology
1989 NASA Public Service Award for Research
2003 Chair of NIH Study Section on Skeletal Muscle
2006 APS/EEP Honor Award for Research
2011 American College of Sports Medicine Honor Award
2015 National Academy Of Sciences Committee For Biological & Physiologica Sciences in Space
   
Appointments 1970-1973: Postdoctoral Trainee Fellow (NIH) Laboratory of Dr. John Holloszy Washington University School of Medicine
   
Research
Abstract
Since joining the Dept. of Physiology and Biophysics at UCI my research has focused on the general theme of plasticity of striated muscle. Over the years, our research group has developed several approaches to manipulate the structure and function of cardiac and Skeletal muscle in the in vivo setting using the primarily models of altered loading states such as functional overload, resistance training exercise, and limb unloading including spaceflight. Using these models, we have primarily focused on the myosin heavy chain (MHC) gene family of motor proteins as the marker genes of study. Consequently, our research has gradually evolved over many years into the molecular biology/physiology field by assembling a cadre of Co-Investigators (see below). Our research spanning ~ 40 years has been funded by three primary research entities: The National Heart, Lung, and Blood Institute; The National Institute of Arthritis and Musculoskeletal and Skin Diseases; and the NASA Life Sciences.

Our research on MHC plasticity expands our studies concerning the transcriptional regulation of the four adult MHC genes. In recent years we have made important findings suggesting that the fast MHC genes are transcriptionally regulated as a gene locus in which they communicate with one another through expression of non coding antisense RNA regulated by intergenic promoters. This area is one of the primary aims in the theme of genomic/epigenetic interaction and cooperative regulation of MHC genes that we have focused on in recent years. Also, we have explored these novel findings concerning muscle unloading targets that reduce expression of slow motor unit fibers by rapidly shutting down transcription of the slow MHC gene while expressing de novo the fastest MHC genes IIx and IIb as a functional mechanism to compensate for the weakness of the slow motor units.

A new area of focus for these studies is to ascertain the mechanisms whereby fast muscle fibers expressing chiefly the IIx/IIb isoforms have an impaired capability to express the slow antigravity type I MHC gene, there by limiting the ability of the muscle to increase its economy of function and fidelity of movement. Furthermore, we have observed epigenetic phenomena suggesting that histone modifications are also playing a key role in the regulation of MHC gene switching and in limiting slow MHC expression in fast type fibers. Hence we will delve further into this area as part of the layering of MHC transcriptional processes. In pursuing these future studies we also will take advantage of new technologies (ChIP, RNA interference, fluorescent labeling of muscle fibers) developed in our laboratory. Thus, the projects that we have identified will spearhead other research groups in pursuing new areas of study that have not been pursued before in the muscle plasticity field.
   
Publications Giger, J.M., F. Haddad, A.X. Qin, and K. M. Baldwin. Effects of cyclosporin A on the in vivo regulation of the type I MHC gene expression. J. Appl. Physiol.. 97: 475-483, 2004. http://jap.physiology.org/cgi/reprint/97/2/475
   
  Haddad, F., K. M. Baldwin, and P. A. Tesch. Pretranslational markers of contractile protein expression in human skeletal muscle: effects of limb unloading plus resistance exercise. J. Appl. Physiol. 98: 46-52. 2005.
   
  Giger, J.M., F. Haddad, A. X. Qin, M. Zeng, and K. M. Baldwin. Effect of unloading on type I myosin heavy chain gene regulation in rat soleus muscle. J. Appl. Physiol. 98: 1185-1194, 2005. http://jap.physiology.org/cgi/reprint/98/4/1185
   
  Haddad, F. G. R. Adams, P. W. Bodell, and K. M. Baldwin. Isometric resistance exercise fails to counteract skeletal atrophy processes during the early states of unloading. J. Appl. Physiol. 100(2):433-441, 2006. http://jap.physiology.org/cgi/reprint/100/2/433.
   
  Pandorf, C.E., F. Haddad, R. R. Roy, A. X. Qin, V. R. Edgerton, K.M. Baldwin. Dynamics of myosin heavy chain gene regulation in slow skeletal muscle. J. Biol. Chem. 281:38330-38342, 2006. PMID: 17030512; http://www.jbc.org/content/281/50/38330.full.pdf+html
   
  Pandorf CE, Haddad F, Qin AX, and Baldwin KM. IIx myosin heavy chain promoter regulation cannot be characterized in vivo by direct gene transfer. Am J Physiol Cell Physiol: 293: C1338-C1346, 2007. PMID: 17670891; http://ajpcell.physiology.org/cgi/reprint/293/4/C1338
   
  Adams, GR, F. Haddad, P. W. Bodell, P. D. Tran, and K. M. Baldwin. Combined isometric, concentric, and eccentric resistance exercise prevents unloading induced muscle atrophy in rats. J. Appl. Physiol.1644-1654, 2007. PMID: 17872405; http://jap.physiology.org/cgi/reprint/103/5/1644
   
  Haddad, F., A. Qin, P. W. Bodell, W. Jiang, J. Giger, and K. M. Baldwin. Intergenic transcriptional regulation of cardiac myosin heavy chain genes. Am. J. Phyiol. Heart. Cir. Physiol., 294: H29-H40, 2008. PMID: 17982008; http://ajpheart.physiology.org/cgi/reprint/294/1/H29
   
  Rinaldi C, Haddad F, Bodell PW, Qin AX, Jiang W, and Baldwin KM. Intergenic bidirectional promoter and cooperative regulation of the IIx and IIb MHC genes in fast skeletal muscle. Am J Physiol Regul Integr Comp Physiol: 295: 208-218, 2008. PMID: 18434443; PMCID: PMC2494810; http://ajpregu.physiology.org/cgi/reprint/295/1/R208
   
  McCall GE, Haddad F, Roy R, Zhong H, Edgerton VR, and Baldwin KM. Transcriptional regulation of the myosin heavy chain IIb gene in inactive rat soleus. Muscle & Nerve 40: 411-419, 2009. PMID: 19623632; http://www3.interscience.wiley.com/cgi-bin/fulltext/122518709/PDFSTART
   
  Caiozzo VJ, Haddad F, Lee S, Baker M, Paloski W, and Baldwin KM. Artificial gravity as a countermeasure to microgravity: a pilot study examining the effects on knee extensor and plantar flexor muscle groups. J. Appl. Physiol. 107: 39-46, 2009. PMID: 19286573; PMCID: PMC2711791. http://jap.physiology.org/cgi/reprint/107/1/39
   
  Pandorf, C.E., F. Haddad, C. Wright, P. W. Bodell, and K. M. Baldwin. Differential epigenetic modifications of histones at the myosin heavy chain genes in fast and slow skeletal muscle fibers and in response to muscle unloading. Am. J. Physiol. Cell Physiol. 297: C6-C16, 2009. PMID: 19369448; PMCID: PMC2711647. http://ajpcell.physiology.org/cgi/reprint/297/1/C6
   
  Giger JM. Bodell PW , Zeng M, Baldwin KM, and Haddad F. Rapid muscle atrophy response to unloading: pretranslational processes involving MHC and actin. J. Appl. Physiol. 107:1204-1212, 2009. PMID: 19628726; PMC2763827. http://jap.physiology.org/cgi/reprint/107/4/1204
   
  Pandorf CE, Qin A, Jiang W, Bodell PW, Baldwin KM, and F Haddad. Calcineurin plays a modulatory role in loading-induced regulation of type I myosin heavy chain gene expression in slow skeletal muscle. Am J Physiol Regul Integr Comp Physiol 297:R1037-1048, 2009. PMID: 19657098; PMC2763824. http://ajpregu.physiology.org/cgi/reprint/297/4/R1037
   
  Haddad F, Jiang W, Bodell PW, Qin AX, and KM Baldwin. Cardiac myosin heavy chain gene regulation by thyroid hormone involves altered histone modifications. Am J Physiol Heart Circ Physiol 299(6):H1966-1980, 2010. PMID: 20833952. http://ajpheart.physiology.org/content/299/6/H1968.full.pdf+html
   
  Pandorf CE, Jiang W, Qin AX, Bodell PW, Baldwin KM, Haddad F. Regulation of an antisense RNA with the transition of neonatal to IIb myosin heavy chain during postnatal development and hypothyroidism in rat skeletal muscle Am J Physiol Regul Integr Comp Physiol. Nov;301(5):R1259-66, 2011 PMID:22262309
   
  Baldwin KM, Joanisse DR, Haddad F, Goldsmith RL, Gallagher D, Pavlovich KH, Shamoon EL, Leibel RL, Rosenbaum M. Effects of weight loss and leptin on skeletal muscle in human subjects. Am J Physiol Regul Integr Comp Physiol. 2011 Nov;301(5):R1259-66..2011. PMID 21917907
   
  Baldwin KM, Haddad F. History of Skeletal Muscle Plasticity in the Last Century. Human Kinetics; Charles M. Tipton edit. 2014
   
  Baldwin KM, Haddad F, Pandorf CE, Roy RR, Edgerton VR. Alterations in muscle mass and contractile phenotype in response to unloading models: role of transcriptional/pretranslational mechanisms.Front Physiol. 2013 Oct 11;4:284. doi: 10.3389/fphys.2013.00284. Review.PMID: 24130531
   
Professional
Societies
American Physiological Society;
American College of Sports Medicine
   
Graduate Programs Cell Biology

Biomedical Engineering

   
   
Link to this profile http://www.faculty.uci.edu/profile.cfm?faculty_id=2290
   
Last updated 05/03/2016