Greener Golf: An Ecological, Behavioral, and Communal Study of the University of Michigan Golf Courses

As one of the leading public universities in the world, the University of Michigan, owns two 18-hole golf courses: Radrick Farms Golf Course (RFGC) and the University of Michigan Golf Course, also known as the Blue Course. The land on which RFGC is situated has a long and diverse history. Over 18,000 years ago, the area was covered by the Wisconsin glacier, the recession of which left a unique till mix and geological features, including Fleming Creek and deposits of sand and gravel. The presence of these resources led to the transformation of the landscape into a gravel mine, which functioned through the 1920s. In the early 1930s, University of Michigan alumnus Fredrick C. Matthaei, Sr., purchased the land from Cadillac Sand and Gravel, along with additional acreage surrounding the mine, and began the process of restoring the gravel pit by re-grading the area, planting alfalfa and red clover, and converting portions of the area to farmland. Following its donation to the University in 1957, the land was converted into a championship 18-hole golf course designed by world-renowned golf course architect Pete Dye. From its beginning, environmental considerations have been a priority at the RFGC. In 2001, the management of RFGC committed to the Michigan Turfgrass Environmental Stewardship Program (MTESP), initiating a series of strong sustainability objectives. Since 2001, RFGC has received special recognition from the Washtenaw County Pollution Prevention Program, in addition to becoming “one of only four courses in the state [of Michigan] with both MTESP and Audubon Cooperative Sanctuary certifications.”1 Radrick Farms Golf Course is also the only club in the state to become a Groundwater Guardian Green Site; in 2012, Washtenaw County presented RFGC with the 2012 Washtenaw County Environmental Excellence Award for Water Quality Protection, and in 2014, RFGC was recognized by the Department of Environmental Quality of the State of Michigan as a Clean Corporate Citizen (C3), the first golf course in the state to receive this recognition. The Blue Course, is located near the iconic Michigan football stadium, south of Central Campus. Prior to becoming a golf course, the area was used for farmland. In 1929, the Blue Course was designed by Dr. Alister Mackenzie, now revered as one of the greatest golf architects. The course officially opened in the spring of 1931 and immediately drew praise as one of the finest in America. At the time of its opening, the Blue Course was only the fourth course to be located on a college campus. In the mid-1990s, a multi-million dollar renovation was completed to restore the prestige of the Blue Course to the ranks of Mackenzie's other classics. A new practice range was added to assist Michigan's golf squads, as well as a number of practice greens and bunkers. The popularity of golf carts necessitated large stretches of cart paths that partition landscaped medians around the course. The unique combination of such a highly regarded and historic golf campus with a strong research university presented an opportunity to conduct a holistic exploration into the benefits that golf courses offer to the ecological, social, economic, and cultural health of the communities that contain them, as well as the opportunity to identify potential recommendations to enhance these benefits. The project team utilized an exploration of current trends in the golf industry, specifically the growing movement for integration of sustainability management techniques, in conjunction with a broader multi-disciplinary focus to inform a working definition of sustainable golf. This definition correlated with the three tenets of permaculture: care for the land, care for the people, and the concept of fair share. The project team assessed the current state of the Blue Course and RFGC in research designed around these three tenets. Specific research included an ecological inventory and site analysis, community perception survey and a study of pre- and post-test cognitive function in golfers, and a high-level, qualitative analysis of economic implications. Using the findings and results from this research, the project team provided recommendations informed by the tenets of sustainable golf. The recommendations presented by the Greener Golf Master’s Project Team highlight three approaches to pushing the boundaries of what it means to be a sustainable golf course. The Greener Golf Master’s Project Team has broadly labeled these three recommendations as engagement, accessibility, and innovation. In addition to the recommendations provided, the Greener Golf Master’s Project Team provided the design for a golf course and event space at RFGC that would provide multiple beneficial functions; one of them being the creation of a “living laboratory” where innovations in sustainable golf course management can be tested prior to implementation on the 18-hole golf courses. The team has preliminarily recommended the site be named the Gateway Course due its proximity to the entrance to RFGC as well as its mission to open a new door to how golf courses can play a role in society in the future. Appendix I is a project summary that includes further discussion of the team’s recommendations. This summary is intended for those who wish to learn more about the project, but cannot read the full report below. In addition, the project summary can be used in public distribution for press and other media opportunities.Master of Science Master of Landscape ArchitectureNatural Resources and EnvironmentUniversity of Michiganhttp://deepblue.lib.umich.edu/bitstream/2027.42/111007/1/GreenerGolfWhitePaper_FINAL.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/111007/2/GreenerGolf_GatewayDesignGuide_FINAL.pdfDescription of GreenerGolfWhitePaper_FINAL.pdf : Greener Golf DocumentDescription of GreenerGolf_GatewayDesignGuide_FINAL.pdf : Greener Golf Design Guid

Recognition chemistry of anionic amino acids for hepatocyte transport and for neurotransmittory action compared

Comparison of neuronal and non-neuronal membrane transport of, and neuroexcitation by, the dicarboxylic amino acids bring out provocative similarities in structural selectivity, and hence in the strategies for studying them. Parallel anomalies in stereoselectivity show for both phenomena that the recognition sites are indeed chiral, as expected for biological functions, even though both fail in special instances to discriminate between pairs. High and low affinity, or Na+-dependence or Na+-independence, are not fully reliable bases for discriminating receptor sites serving one of these functions. Tolerance of N-methylation of the amino acid serves in discriminating families of recognition sites for both phenomena, as does substitution of the sulfonate or sulfinate for the distal carboxylate group, or other structural changes. Analogs in which the functional groups of aspartate or glutamate are presented in restrained arrays serve for both, although they have so far suggested identity neither of recognition sites for transport and excitation, nor of the events consequent to binding for these two phenomena.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/25042/1/0000469.pd

What are the requisites for a model transport analog?

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/27404/1/0000437.pd

Characterization of a transport system for anionic amino acids in human fibroblast lysosomes

-Aspartate and -glutamate are transported into human fibroblast lysosomes by a single, low Km, Na+-independent transport system, which has been provisionally named lysosomal system d. This system resembles the Na+-dependent plasma membrane system xAG-, although these differences have been observed: (1) lysosomal system d recognizes the - as well as the -isomers of both aspartate and glutamate, whereas only for aspartate is the -isomer recognized by system xAG-; (2) the anion -homocysteate is not accepted by system xAG-, but is an effective inhibitor of lysosomal system d; (3) N-methyl, [alpha]-methyl, and [omega]-hydroxamate derivatives of both aspartate and glutamate inhibit lysosomal system d, but only the aspartate derivatives are accepted by system xAG-; (4) lysosomal system d shows a preference for the substrate amino group in the [alpha]-position, a preference not seen for system xAG-. These points imply differences at the two recognition sites with respect to substrate length, size and rotation, with the lysosomal site generally being the less restrictive.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/27627/1/0000002.pd

Functional Induction of the Cystine-Glutamate Exchanger System Xc- Activity in SH-SY5Y Cells by Unconjugated Bilirubin

We have previously reported that exposure of SH-SY5Y neuroblastoma cells to unconjugated bilirubin (UCB) resulted in a marked up-regulation of the mRNA encoding for the Na+ -independent cystine∶glutamate exchanger System Xc− (SLC7A11 and SLC3A2 genes). In this study we demonstrate that SH-SY5Y cells treated with UCB showed a higher cystine uptake due to a significant and specific increase in the activity of System Xc−, without the contribution of the others two cystine transporters (XAG− and GGT) reported in neurons. The total intracellular glutathione content was 2 folds higher in the cells exposed to bilirubin as compared to controls, suggesting that the internalized cystine is used for gluthathione synthesis. Interestingly, these cells were significantly less sensitive to an oxidative insult induced by hydrogen peroxide. If System Xc− is silenced the protection is lost. In conclusion, these results suggest that bilirubin can modulate the gluthathione levels in neuroblastoma cells through the induction of the System Xc−, and this renders the cell less prone to oxidative damage

Amino acid transport systems of lysosomes: Possible substitute utility of a surviving transport system for one congenitally defective or absent

Ways in which other transport systems may compensate for one that is genetically defective are considered. Comparisons of the transport systems of organelles (here the lysosome) with the transport system at the plasma membrane has significant implications for chemotherapy.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/44194/1/10540_2005_Article_BF01116456.pd

Anionic Amino Acid Transport Across the Plasma Membrane of Cultured Rat Hepatocytes and Hepatoma Cell Lines.

The charge on the amino acid molecule has emerged as the primary criterion determining which mediation will serve for its transport across the membrane of mammalian cells. Three systems serving for the uptake of anionic amino acids into rat hepatocytes, fetal rat hepatocytes and the hepatoma cell lines HTC, H4-II-E-C(,3) and McA-RH7777 have been characterized, two of which systems (x(,c)('-), x(,AG)('-)) are kinetically distinguishable from others serving for neutral (A, ASC, L and N) or for basic (y('+)) amino acids. The third system, first defined as x(,A)('-), and later apparently shown identical with System ASC, serves for neutral amino acids at pH 7.4 and for anionic ones at reduced pH. Interconvertible service for amino acids of unlike charge appears in this case consistent with protonation of the mediator rather than the substrate molecules. The chain length of an anionic amino acid determines which of the three systems will serve for its transport. The Na('+)-independent System x(,c)('-) observed in fetal hepatocytes and HTC cells, but barely perceptible in the other cells of hepatic origin tested (hepatocytes, H4-II-E-C(,3), McA-RH7777), serves for uptake of anionic amino acids as long or longer than glutamate but not longer than cystine. The formally neutral cystine becomes a substrate for x(,c)('-) at those pH values which allow it to be at least partially anionic, shown by the increase in glutamate-inhibitable cystine uptake on raising the pH from 5 to 7.5. Uptake of anionic amino acids by x(,c)('-) is both pH-independent and stereoselective. The two Na('+)-dependent systems x(,AG)('-) and x(,A)('-)/ASC were detected in all the cells of hepatic origin tested. System x(,AG)('-) serves with high affinity for aspartate, glutamate and for the short-chain analogs cysteate and cysteinesulfinate. Uptake by x(,AG)('-) is pH-independent and displays a stereoselective anomaly, readily distinguishing the D- and L-isomers of glutamate but not of aspartate. System x(,A)('-)/ASC serves for both short-chain neutral amino acids and the short-chain anionics transported by x(,AG)('-), but excludes L-glutamate. Systems x(,AG)('-) and x(,c)('-), when present, are the primary routes of anionic amino acid uptake under physiological conditions; uptake by x(,A)('-)/ASC is largely inhibited at physiological pH by the preferred neutral amino acid substrates.Ph.D.BiologyUniversity of Michiganhttp://deepblue.lib.umich.edu/bitstream/2027.42/159426/1/8314327.pd

A stereoselective anomaly in dicarboxylic amino acid transport

Using L-cysteate and tcysteinesulfinate as model substrates, we characterize here a transport system, both in culturerda t hepatocytes and human skin fibroblasts, serving for thea nions glutamate and aspartate, but not for the dipolar species glutamic and aspartic acids. This system appears to be accompanied by a second, lower affinity system for the anionic forms, which is also Na’-dependent; this lower affinity system applies at least to glutamate. These systems show the usual degree of preference for L- over D-glutamate and, in the fibroblast, for L- over DL-a-aminoadipate. D-ASpartate proved nearly as inhibitory to the uptake of Lcysteate or t-aspartate, however, as did L-aspartate itself, a comparison recalling a similar stereoselective anomaly discovered by Pall in Neurospora (Pall, M. (1976) Biochim Biophys. Acta 211, 513-520). We conclude that this anomaly arises from the ability of the two substrate carboxylate groups tob ond in the spatial order eithera # for the L-isomer or &a for the D-isomer and also to bond in the order a,y for L-glutamate, but scarcely in the order y,a for D-glutamate. A major lack of inhibition by D-cysteate, whichm ight be expected to bind like aspartate in the inverted order, shows, however, that thetw o anionic groups are not recognized in identical manners by the two corresponding subsites, Precedent for a chemical difference in these two subsites is available from transport systems for neutral aand p-amino acids. A strong transporti nhibition of the hepatocyte system by 3-aminoglutarate shows that an a,a relation between the amino group and eitheor f the carboxylate groups of the anionic amino acid is not required. The above anomaly in stereoselectivity is compared with a corresponding one, applying to the reactions of aspartic acid and asparagine, versus glutamic acid and glutamine, with System L for neutral amino acid transport in the Ehrlich cell. A weak pHdependent inhibition of the uptake of anionic amino acids by cysteine can be associated with its unique mode of conversion to an anionic species