Paul Hargrave

Last updated
Paul A. Hargrave
Born1938
Palmyra, New York, United States[ citation needed ]
Alma mater Colgate University
University of Minnesota
Known forRhodopsin
Scientific career
Fields Biochemistry
Institutions California Institute of Technology
Southern Illinois University
University of Florida

Paul Hargrave (born 1938) is an American biochemist whose laboratory work established key features of the structure of rhodopsin. [1] [2]

Contents

Career

In 1970, Hargrave received a PhD from the University of Minnesota, where he studied with protein chemist Finn Wold. After post-doctoral work under William J. Dreyer at the California Institute of Technology, Hargrave joined the faculty at Southern Illinois University in 1973. [3]

In 1983, Hargrave and colleagues in his laboratory published the full amino acid sequence for rhodopsin, a photoreceptor protein, after having previously published partial sequences. [4] [5] [6] [7] The sequencing of rhodopsin was later described as a "monumental step" toward understanding the structure of rhodopsin. [8] [9] At the time, the purification of water-insoluble peptides was a challenge, and the Hargrave lab published several discoveries about how to manage them. [10]

Hargrave came to the University of Florida in 1984 as a Jules and Doris Stein Research to Prevent Blindness Professor [11] and in 1990 was named the Francis N. Bullard Professor and Eminent Scholar of Ophthalmology and Biochemistry at the University of Florida. [12] His work continued to explore the structure of rhodopsin, including developing a topographic model. [13] [14] He also pursued further research into the function of rhodopsin, including its role in visual disease such as retinitis pigmentosa and retinoblastoma. [15] [16]

In 1985, Hargrave chaired and secured funding for the first FASEB Science Research Conference on Biology and Chemistry of Vision, which has become a biennial conference. [17] [18]

Awards

In 2000, he received the Friedenwald Award of the Association for Research in Vision and Ophthalmology, which honors "outstanding research in the basic or clinical sciences as applied to ophthalmology." [19] [20]

Selected works

Personal life

Hargrave is a member of the 50 States Marathon Club, having completed a marathon in every state in the United States. [21]

He is the father of board game designer Elizabeth Hargrave. [22]

Related Research Articles

<span class="mw-page-title-main">Retina</span> Part of the eye

The retina is the innermost, light-sensitive layer of tissue of the eye of most vertebrates and some molluscs. The optics of the eye create a focused two-dimensional image of the visual world on the retina, which then processes that image within the retina and sends nerve impulses along the optic nerve to the visual cortex to create visual perception. The retina serves a function which is in many ways analogous to that of the film or image sensor in a camera.

<span class="mw-page-title-main">Rhodopsin</span> Light-sensitive receptor protein

Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene and a G-protein-coupled receptor (GPCR). It is the opsin of the rod cells in the retina and a light-sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, after which the rods are more sensitive. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness.

<span class="mw-page-title-main">Visual system</span> Body parts responsible for vision

The visual system is the physiological basis of visual perception. The system detects, transduces and interprets information concerning light within the visible range to construct an image and build a mental model of the surrounding environment. The visual system is associated with the eye and functionally divided into the optical system and the neural system.

<span class="mw-page-title-main">Retinitis pigmentosa</span> Gradual retinal degeneration leading to progressive sight loss

Retinitis pigmentosa (RP) is a genetic disorder of the eyes that causes loss of vision. Symptoms include trouble seeing at night and decreasing peripheral vision. As peripheral vision worsens, people may experience "tunnel vision". Complete blindness is uncommon. Onset of symptoms is generally gradual and often begins in childhood.

<span class="mw-page-title-main">Transducin</span>

Transducin (Gt) is a protein naturally expressed in vertebrate retina rods and cones and it is very important in vertebrate phototransduction. It is a type of heterotrimeric G-protein with different α subunits in rod and cone photoreceptors.

In visual physiology, adaptation is the ability of the retina of the eye to adjust to various levels of light. Natural night vision, or scotopic vision, is the ability to see under low-light conditions. In humans, rod cells are exclusively responsible for night vision as cone cells are only able to function at higher illumination levels. Night vision is of lower quality than day vision because it is limited in resolution and colors cannot be discerned; only shades of gray are seen. In order for humans to transition from day to night vision they must undergo a dark adaptation period of up to two hours in which each eye adjusts from a high to a low luminescence "setting", increasing sensitivity hugely, by many orders of magnitude. This adaptation period is different between rod and cone cells and results from the regeneration of photopigments to increase retinal sensitivity. Light adaptation, in contrast, works very quickly, within seconds.

<span class="mw-page-title-main">Fovea centralis</span> Small pit in the retina of the eye responsible for all central vision

The fovea centralis is a small, central pit composed of closely packed cones in the eye. It is located in the center of the macula lutea of the retina.

<span class="mw-page-title-main">Retinal</span> Chemical compound

Retinal is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision).

<span class="mw-page-title-main">Melanopsin</span> Mammalian protein found in Homo sapiens

Melanopsin is a type of photopigment belonging to a larger family of light-sensitive retinal proteins called opsins and encoded by the gene Opn4. In the mammalian retina, there are two additional categories of opsins, both involved in the formation of visual images: rhodopsin and photopsin in the rod and cone photoreceptor cells, respectively.

<span class="mw-page-title-main">Opsin</span> Class of light-sensitive proteins

Animal opsins are G-protein-coupled receptors and a group of proteins made light-sensitive via a chromophore, typically retinal. When bound to retinal, opsins become retinylidene proteins, but are usually still called opsins regardless. Most prominently, they are found in photoreceptor cells of the retina. Five classical groups of opsins are involved in vision, mediating the conversion of a photon of light into an electrochemical signal, the first step in the visual transduction cascade. Another opsin found in the mammalian retina, melanopsin, is involved in circadian rhythms and pupillary reflex but not in vision. Humans have in total nine opsins. Beside vision and light perception, opsins may also sense temperature, sound, or chemicals.

The Stiles–Crawford effect is a property of the human eye that refers to the directional sensitivity of the cone photoreceptors.

Rhodopsin kinase is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the following chemical reaction:

<span class="mw-page-title-main">OPN1SW</span> Protein-coding gene in the species Homo sapiens

Blue-sensitive opsin is a protein that in humans is encoded by the OPN1SW gene.

<span class="mw-page-title-main">OPN1MW</span> Protein-coding gene in the species Homo sapiens

Green-sensitive opsin is a protein that in humans is encoded by the OPN1MW gene. OPN1MW2 is a similar opsin.

<span class="mw-page-title-main">GUCA1B</span> Protein-coding gene in the species Homo sapiens

Guanylyl cyclase-activating protein 2 is an enzyme that in humans is encoded by the GUCA1B gene. Alternative names:

Krzysztof Palczewski is a Polish-American biochemist working at the University of California, Irvine.

<span class="mw-page-title-main">Retinal degeneration (rhodopsin mutation)</span> Retinopathy

Retinal degeneration is a retinopathy which consists in the deterioration of the retina caused by the progressive death of its cells. There are several reasons for retinal degeneration, including artery or vein occlusion, diabetic retinopathy, R.L.F./R.O.P., or disease. These may present in many different ways such as impaired vision, night blindness, retinal detachment, light sensitivity, tunnel vision, and loss of peripheral vision to total loss of vision. Of the retinal degenerative diseases retinitis pigmentosa (RP) is a very important example.

Aristostomias is a genus of barbeled dragonfishes native to the ocean depths in the Pacific, Atlantic and Indian oceans.

<span class="mw-page-title-main">King-Wai Yau</span> Chinese-American neuroscientist

King-Wai Yau is a Chinese-born American neuroscientist and Professor of Neuroscience at Johns Hopkins University School of Medicine in Baltimore, Maryland.

<span class="mw-page-title-main">Davida Teller</span> American psychologist

Davida Young Teller was a professor in the Departments of Psychology and Physiology/Biophysics at the University of Washington, Seattle, Washington. She was a leader in the scientific study of infant visual development.

References

  1. ↑ American Men and Women of Science: Chemistry. Bowker. 1977. p. 479. ISBN   9780835210119 . Retrieved 26 November 2018.
  2. ↑ American men & women of science: Physical and Biological Sciences. Bowker. 1989. p. 501. ISBN   9780835214179 . Retrieved 26 November 2018.
  3. ↑ Papermaster, David S. (2001-01-01). "Introducing Paul Hargrave, the 2000 Recipient of the Friedenwald Award". Investigative Ophthalmology & Visual Science. 42 (1): 1–2. ISSN   1552-5783. PMID   11133840.
  4. ↑ Hargrave, P. A. (1977-05-27). "The amino-terminal tryptic peptide of bovine rhodopsin. A glycopeptide containing two sites of oligosaccharide attachment". Biochimica et Biophysica Acta (BBA) - Protein Structure. 492 (1): 83–94. doi:10.1016/0005-2795(77)90216-1. ISSN   0006-3002. PMID   861254.
  5. ↑ Hargrave, Paul A (1982-01-01). "The carboxyl-terminal one-third of bovine rhodopsin: Its structure and function". Vision Research. 22 (12). et al: 1429–1438. doi:10.1016/0042-6989(82)90205-X. ISSN   0042-6989. PMID   7182998. S2CID   1556264.
  6. ↑ Hargrave, P. A.; McDowell, J. H.; Curtis, Donna R.; Wang, Janet K.; Juszczak, Elizabeth; Fong, Shao-Ling; Mohana Rao, J. K.; Argos, P. (1983). "The structure of bovine rhodopsin". Biophysics of Structure and Mechanism. 9 (4): 235–244. doi:10.1007/bf00535659. ISSN   0340-1057. PMID   6342691. S2CID   20407577.
  7. ↑ Hargrave, P. A.; McDowell, J. H.; Feldmann, R. J.; Atkinson, P. H.; Rao, J. K.; Argos, P. (1984). "Rhodopsin's protein and carbohydrate structure: selected aspects". Vision Research. 24 (11): 1487–1499. doi:10.1016/0042-6989(84)90311-0. ISSN   0042-6989. PMID   6533983. S2CID   31984423.
  8. ↑ Dratz, Edward; Hargrave, Paul A (1983-04-01). "The structure of rhodopsin and the rod outer segment disk membrane". Trends in Biochemical Sciences. 8 (4): 128–131. doi:10.1016/0968-0004(83)90235-9. ISSN   0968-0004.
  9. ↑ Palczewski, Krzysztof (February 2011). "Focus on vision: 3 decades of remarkable contributions to biology and medicine". The FASEB Journal. 25 (2): 439–443. doi: 10.1096/fj.11-0202ufm . ISSN   0892-6638. PMC   3228347 . PMID   21282210.
  10. ↑ Papermaster, David S. (2001-01-01). "Introducing Paul Hargrave, the 2000 Recipient of the Friedenwald Award". Investigative Ophthalmology & Visual Science. 42 (1): 1–2. ISSN   1552-5783. PMID   11133840.
  11. ↑ "News and Comment". Archives of Ophthalmology. 103 (4): 492. 1985-04-01. doi:10.1001/archopht.1985.01050040034012. ISSN   0003-9950.
  12. ↑ "Paul Hargrave, Ph.D. | UFRF Professors". ufrfprofessors.feed.research.ufl.edu. Retrieved 2018-11-16.
  13. ↑ Unger, Vinzenz M.; Hargrave, Paul A.; Baldwin, Joyce M.; Schertler, Gebhard F. X. (September 1997). "Arrangement of rhodopsin transmembrane α-helices". Nature. 389 (6647): 203–206. Bibcode:1997Natur.389..203U. doi:10.1038/38316. ISSN   0028-0836. PMID   9296501. S2CID   205026444.
  14. ↑ Hargrave, Paul A; McDowell, J Hugh (1993-01-01). "Rhodopsin and Phototransduction". International Review of Cytology. 137: 49–97. doi:10.1016/S0074-7696(08)62600-5. ISBN   9780123645388. ISSN   0074-7696. PMID   1478822.
  15. ↑ Deretic, Dusanka; Williams, Andrew H.; Ransom, Nancy; Morel, Valerie; Hargrave, Paul A.; Arendt, Anatol (2005-03-01). "Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4)". Proceedings of the National Academy of Sciences. 102 (9): 3301–3306. Bibcode:2005PNAS..102.3301D. doi: 10.1073/pnas.0500095102 . ISSN   0027-8424. PMC   552909 . PMID   15728366.
  16. ↑ Vrabec, Tamara; Arbizo, Violeta; Adamus, Grazyna; McDowell, J Hugh; Hargrave, PA; Donoso, Larry (1989-07-01). "Rod Cell-Specific Antigens in Retinoblastoma". Archives of Ophthalmology. 107 (7): 1061–3. doi:10.1001/archopht.1989.01070020123044. ISSN   0003-9950. PMID   2473730.
  17. ↑ Kefalov, Vladimir J.; Arshavsky, Vadim Y. (June 2014). "FASEB Science Research Conference on Biology and Chemistry of Vision". The FASEB Journal. 28 (6): 2395–2397. doi: 10.1096/fj.14-0602ufm . ISSN   0892-6638. PMC   6137602 . PMID   24891609.
  18. ↑ Paul, Hargrave. "FASEB Conference: Biology and Chemistry of Vision August 11-16, 1985; Saxton's River, Vermont". Grantome.
  19. ↑ Papermaster, David S. (2001-01-01). "Introducing Paul Hargrave, the 2000 Recipient of the Friedenwald Award". Investigative Ophthalmology & Visual Science. 42 (1): 1–2. ISSN   1552-5783. PMID   11133840.
  20. ↑ "International society honors UF vision scientist". UF Health, University of Florida Health. 2000-06-07. Retrieved 2018-11-17.
  21. ↑ "USA Male Finishers by Date". 50 States Club. Retrieved 2018-11-16.
  22. ↑ @elizhargrave (October 13, 2020). "(Elizabeth Hargrave links to this Wikipedia profile as belonging to her father)" (Tweet) – via Twitter.
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