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High-probability grants
According to our matching algorithm, George Preti is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
1982 — 2000 |
Preti, George Cutler, Winnifred |
N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information |
Olfactory Influences On Physiological Parameters @ Monell Chemical Senses Center |
1 |
1992 — 1994 |
Preti, George |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Olfactory Influences On Physiology Parameters @ Monell Chemical Senses Center
The axillary region is a body area with unique odor-producing characteristics. In the axillae; apocrine, sebaceous, eccrine and apoeccrine glands provide substrate for a large permanent population of microorganisms. Numerous studies have suggested that axillary secretions can convey information between individuals or groups of people. These odors allow individuals to identify their own odor as well as those of their spouse and close genetic kin. In addition, studies from our laboratory have shown that ethanol extracts made from male and female axillary secretions can change the length and timing of the human female menstrual cycle. Consequently, axillary secretions and their odors appear to be the best documented human odor source with chemical communicatory properties. Despite the fact that axillary secretions and their odors can convey information between individuals and/or groups of people, little information has been published concerning the structural nature of the axillary odors and the biochemical pathways that produce them. Previous studies of axillary odors have suggested that the volatile steroids and isovaleric acid are major contributors to the characteristic axillary odor. Our recently published studies have determined the nature of the axillary odors, in a combined male sample; they are C6 to C11 saturated, unsaturated and branched acids, with (E)-3-methyl-2-hexenoic acid being the largest component present. Our proposed studies will examine the odoriferous components in individual male and female subjects and document changes in these compounds across the menstrual cycle. The proposed study will also further characterize the proteinaceous precursors to the major axillary odorant: 3-methyl-2-hexenoic acid. We now have raised antibodies to both of the apocrine secretion odor binding proteins and will use these in an affinity column to obtain larger amounts of these compounds. The fact that a characteristic human odor is secreted onto the skin bound to proteins is a novel finding. It suggests that if the odors which characterize the axillae are responsible for the primer pheromone activity reported for axillary extracts (e.g., menstrual cycle alteration), the chemistry involved may be similar to other mammalian pheromone systems.
|
1 |
1999 — 2001 |
Preti, George |
P41Activity Code Description: Undocumented code - click on the grant title for more information. |
Glycoproteins in Axillary Glands @ Boston University Medical Campus
Annexins are a family of cakcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. Structural evidence has been obtained for a Ca~'-bridging mechanism, proposed for Ca2'-binding interfacial membrane proteins such as annexins, protein kinase C, and certain coagulation proteins. Crystal structures of Ca~'-annexin V complexes with phospholipid polar heads provide molecular details of Ca~'-bridges as key features in the membrane attachment exhibited by these proteins. Distinct binding sites for phospholipid head groups are observed, including a novel, double-Ca~' recognition site for phosphoserine that may serve as a phosphatidylserine receptor site in vivo. We have solved the crystal structure of rat annexin V to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes. Mass spectrometry experiments are being used to obtain profiles of the phospholipids associated with annexin V.
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0.909 |