William A. Hagins

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William Archer Hagins
William A. Hagins.png
DiedJune 6, 2012
Scientific career
FieldsThe transduction of electrical signal in photorecepters in retinal

William Archer Hagins (died June 6, 2012) [1] was an American medical researcher. He was chief of the Section of Membrane Biophysics in National Institute of Diabetes and Digestive and Kidney Diseases's Laboratory of Chemical Physics upon his retirement in 2007. [2] Hagins and colleagues made the seminal discovery of the dark current in photoreceptor cells. This finding became central to understanding how the visual cells worked and led to knowledge of the importance of reattaching a detached retina as soon as possible for continued use. As a fellow of Fulbright Program, he'd also served in the United States Navy as a Research Medical Officer. He joined NIDDK's Laboratory of Physical Biology in 1958, doing independent research in the Section of Photobiology, headed by Frederick Sumner Brackett. Hagins was a mentor to many, particularly through his work with the Brackett Foundation.

Contents

Education

William A. Hagins was a native Washingtonian, Chevy Chase resident. In Stanford University California, he got a bachelor's degree in biology, and continued to get a master's degree in anatomy in 1948. In 1951, he graduated from School of Medical in Stanford University. With a Fulbright fellowship, he studied at the physiology laboratory in University of Cambridge, England. In 1958, he received his doctorate.

Career

William A. Hagins joined NIDDK's Laboratory of Physical Biology in 1958. He was elected to the National Academy of Sciences and was a past president of the Biophysical Society. He was involved in various professional journals as an editor or editorial board member. He was a mentor to graduate students and postdoctoral physicians. [3] In the 1960s, Hagins and his group showed how the eye transforms images in the retina to produce the sensation of vision.

Research interests

Hagins as an graduate student in Stanford University worked on the project about the influence of diameter on the characteristics of the action potential of single nerve fibers. [4] At the physiology laboratory in University of Cambridge, Hagins focused on the phototransduction of rhodopsin, especially the photosensitivity, the photobleaching and flash photolysis. [5] [6] [7] [8]

After joining Laboratory of Physical Biology, Hagins went deep into this field and made more efforts on studying the photoelectric effects of functional photoreceptors in retina, especially squid retina. [9] [10] [11] [12] With enormous efforts on the photoelectric effects in retinal, Hagins and colleagues found the dark current in retinal rods. [13] Hagins with his group did a series of research to explore the cell biological mechanisms of rods and cones at molecular level. [14] [15] [16] [17] [18] [19] [20]

Hagins also did some works on optics and microscopy. [21]

Selected publications

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">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">Photoreceptor cell</span> Type of neuroepithelial cell

A photoreceptor cell is a specialized type of neuroepithelial cell found in the retina that is capable of visual phototransduction. The great biological importance of photoreceptors is that they convert light into signals that can stimulate biological processes. To be more specific, photoreceptor proteins in the cell absorb photons, triggering a change in the cell's membrane potential.

<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.

<span class="mw-page-title-main">Rod cell</span> Photoreceptor cells that can function in lower light better than cone cells

Rod cells are photoreceptor cells in the retina of the eye that can function in lower light better than the other type of visual photoreceptor, cone cells. Rods are usually found concentrated at the outer edges of the retina and are used in peripheral vision. On average, there are approximately 92 million rod cells in the human retina. Rod cells are more sensitive than cone cells and are almost entirely responsible for night vision. However, rods have little role in color vision, which is the main reason why colors are much less apparent in dim light.

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">Guanylate cyclase</span> Lyase enzyme that synthesizes cGMP from GTP

Guanylate cyclase is a lyase enzyme that converts guanosine triphosphate (GTP) to cyclic guanosine monophosphate (cGMP) and pyrophosphate:

<span class="mw-page-title-main">Retinal</span> Vitamin A aldehyde, a polyene chromophore

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">Retina bipolar cell</span> Type of neuron

As a part of the retina, bipolar cells exist between photoreceptors and ganglion cells. They act, directly or indirectly, to transmit signals from the photoreceptors to the ganglion cells.

<span class="mw-page-title-main">Cyclic nucleotide–gated ion channel</span> Family of transport proteins

Cyclic nucleotide–gated ion channels or CNG channels are ion channels that function in response to the binding of cyclic nucleotides. CNG channels are nonselective cation channels that are found in the membranes of various tissue and cell types, and are significant in sensory transduction as well as cellular development. Their function can be the result of a combination of the binding of cyclic nucleotides and either a depolarization or a hyperpolarization event. Initially discovered in the cells that make up the retina of the eye, CNG channels have been found in many different cell types across both the animal and the plant kingdoms. CNG channels have a very complex structure with various subunits and domains that play a critical role in their function. CNG channels are significant in the function of various sensory pathways including vision and olfaction, as well as in other key cellular functions such as hormone release and chemotaxis. CNG channels have also been found to exist in prokaryotes, including many spirochaeta, though their precise role in bacterial physiology remains unknown.

Visual phototransduction is the sensory transduction process of the visual system by which light is detected by photoreceptor cells in the vertebrate retina. A photon is absorbed by a retinal chromophore, which initiates a signal cascade through several intermediate cells, then through the retinal ganglion cells (RGCs) comprising the optic nerve.

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

Retinylidene proteins, or rhodopsins in a broad sense, are proteins that use retinal as a chromophore for light reception. They are the molecular basis for a variety of light-sensing systems from phototaxis in flagellates to eyesight in animals. Retinylidene proteins include all forms of opsin and rhodopsin. While rhodopsin in the narrow sense refers to a dim-light visual pigment found in vertebrates, usually on rod cells, rhodopsin in the broad sense refers to any molecule consisting of an opsin and a retinal chromophore in the ground state. When activated by light, the chromophore is isomerized, at which point the molecule as a whole is no longer rhodopsin, but a related molecule such as metarhodopsin. However, it remains a retinylidene protein. The chromophore then separates from the opsin, at which point the bare opsin is a retinylidene protein. Thus, the molecule remains a retinylidene protein throughout the phototransduction cycle.

<span class="mw-page-title-main">Retinitis pigmentosa GTPase regulator</span> Protein found in humans

X-linked retinitis pigmentosa GTPase regulator is a GTPase-binding protein that in humans is encoded by the RPGR gene. The gene is located on the X-chromosome and is commonly associated with X-linked retinitis pigmentosa (XLRP). In photoreceptor cells, RPGR is localized in the connecting cilium which connects the protein-synthesizing inner segment to the photosensitive outer segment and is involved in the modulation of cargo trafficked between the two segments.

<span class="mw-page-title-main">ABCA4</span> Mammalian protein found in Homo sapiens

ATP-binding cassette, sub-family A (ABC1), member 4, also known as ABCA4 or ABCR, is a protein which in humans is encoded by the ABCA4 gene.

<span class="mw-page-title-main">PDE6B</span> Protein-coding gene in the species Homo sapiens

Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta is the beta subunit of the protein complex PDE6 that is encoded by the PDE6B gene. PDE6 is crucial in transmission and amplification of visual signal. The existence of this beta subunit is essential for normal PDE6 functioning. Mutations in this subunit are responsible for retinal degeneration such as retinitis pigmentosa or congenital stationary night blindness.

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

Disc shedding is the process by which photoreceptor cells in the retina are renewed. The disc formations in the outer segment of photoreceptors, which contain the photosensitive opsins, are completely renewed every ten days.

<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.

Denis Aristide Baylor was an American neurobiologist. He was professor emeritus of neurobiology at Stanford University. He is known for his research on nerve cells in the retina of the eye. He developed a widely-used method for observing the electrical activity of single rod and cone photoreceptor cells and described how they encode light stimuli. Baylor’s work has been recognized by his election to the American Academy of Arts and Sciences, the National Academy of Sciences, and the Royal Society of London.

References

  1. "WILLIAM A. HAGINS Jr. Obituary (2012) the Washington Post". Legacy.com .
  2. "Commendations & Commencements, Fall 2012 | Director's Update | NIDDK". National Institute of Diabetes and Digestive and Kidney Diseases. U.S. Department of Health and Human Services. Retrieved April 27, 2020.
  3. Bernstein, Adam. "William A. Hagins, medical researcher". The Washington Post. Retrieved April 27, 2020.
  4. Hagins, William Archer (1948). The influence of fiber diameter on the characteristics of the action potential of single nerve fibers. Document:Thesis/dissertation, Stanford University 1948. OCLC   655068693.
  5. Hagins, W. A.; Rushton, W. A. (June 29, 1953). "The measurement of rhodopsin in the decerebrate albino rabbit". The Journal of Physiology. 120 (4): 61. ISSN   0022-3751. PMID   13070262.
  6. Hagins, W. A. (July 28, 1955). "The quantum efficiency of bleaching of rhodopsin in situ". The Journal of Physiology. 129 (1): 22–3P. ISSN   0022-3751. PMID   13252610.
  7. Hagins, W. A. (November 29, 1954). "The photosensitivity of mammalian rhodopsin in situ". The Journal of Physiology. 126 (2): 37. ISSN   0022-3751. PMID   13222326.
  8. Hagins, W. A. (May 26, 1956). "Flash photolysis of rhodopsin in the retina". Nature. 177 (4517): 989–90. Bibcode:1956Natur.177..989H. doi:10.1038/177989b0. ISSN   0028-0836. PMID   13322011. S2CID   4254310.
  9. Hagins, W. A.; Jennings, W. H. (July 7, 1959). "Radiationless migration of electronic excitation in retinal rods". Research Report. Naval School of Aviation Medicine. 1: 343–55. ISSN   0099-9237. PMID   24546338.
  10. Hagins, W. A.; Zonana, H. V.; Adams, R. G. (June 2, 1962). "Local membrane current in the outer segments of squid photoreceptors". Nature. 194 (4831): 844–7. Bibcode:1962Natur.194..844H. doi:10.1038/194844a0. ISSN   0028-0836. PMID   13903645. S2CID   30922080.
  11. Hagins, W. A. (1965). "Electrical signs of information flow in photoreceptors". Cold Spring Harbor Symposia on Quantitative Biology. 30: 403–18. doi:10.1101/sqb.1965.030.01.040. ISSN   0091-7451. PMID   5219490.
  12. Penn, R. D.; Hagins, W. A. (July 12, 1969). "Signal transmission along retinal rods and the origin of the electroretinographic a-wave". Nature. 223 (5202): 201–4. Bibcode:1969Natur.223..201P. doi:10.1038/223201a0. ISSN   0028-0836. PMID   4307228. S2CID   4281727.
  13. 1 2 Hagins, W. A.; Penn, R. D.; Yoshikami, S. (May 1970). "Dark current and photocurrent in retinal rods". Biophysical Journal. 10 (5): 380–412. Bibcode:1970BpJ....10..380H. doi:10.1016/S0006-3495(70)86308-1. ISSN   0006-3495. PMC   1367773 . PMID   5439318.
  14. Hagins, W. A.; Rüppel, H. (January 1971). "Fast photoelectric effects and the properties of vertebrate photoreceptors as electric cables". Federation Proceedings. 30 (1): 64–8. ISSN   0014-9446. PMID   5539875.
  15. Hagins, W. A. (1972). "The visual process: Excitatory mechanisms in the primary receptor cells". Annual Review of Biophysics and Bioengineering. 1: 131–58. doi:10.1146/annurev.bb.01.060172.001023. ISSN   0084-6589. PMID   4567751.
  16. Hagins, W. A.; Yoshikami, S. (March 1974). "Proceedings: A role for Ca2+ in excitation of retinal rods and cones". Experimental Eye Research. 18 (3): 299–305. doi:10.1016/0014-4835(74)90157-2. ISSN   0014-4835. PMID   4833765.
  17. Yoshikami, S.; Hagins, W. A. (April 28, 1978). "Calcium in excitation of vertebrate rods and cones: retinal efflux of calcium studied with dichlorophosphonazo III". Annals of the New York Academy of Sciences. 307 (1): 545–61. Bibcode:1978NYASA.307..545Y. doi:10.1111/j.1749-6632.1978.tb41981.x. ISSN   0077-8923. PMID   101121. S2CID   1150576.
  18. Robinson, W. E.; Hagins, W. A. (April 1979). "A light-activated GTPase in retinal rod outer segments". Photochemistry and Photobiology. 29 (4): 693. doi:10.1111/j.1751-1097.1979.tb07750.x. ISSN   0031-8655. PMID   221947. S2CID   29053911.
  19. Robinson, W. E.; Hagins, W. A. (August 2, 1979). "GTP hydrolysis in intact rod outer segments and the transmitter cycle in visual excitation". Nature. 280 (5721): 398–400. Bibcode:1979Natur.280..398R. doi:10.1038/280398a0. ISSN   0028-0836. PMID   223060. S2CID   4372290.
  20. Yoshikami, S.; George, J. S.; Hagins, W. A. (July 24, 1980). "Light-induced calcium fluxes from outer segment layer of vertebrate retinas". Nature. 286 (5771): 395–8. Bibcode:1980Natur.286..395Y. doi:10.1038/286395a0. ISSN   0028-0836. PMID   7402322. S2CID   4351135.
  21. Hagins, W. A. (January 25, 1980). "Near-infrared microscopy". Science. 207 (4429): 359. Bibcode:1980Sci...207..359H. doi:10.1126/science.7350669. ISSN   0036-8075. PMID   7350669.
  22. Hagins, W. A.; McGaughy, R. E. (January 12, 1968). "Membrane origin of the fast photovoltage of squid retina". Science. 159 (3811): 213–5. Bibcode:1968Sci...159..213H. doi:10.1126/science.159.3811.213. ISSN   0036-8075. PMID   5634917. S2CID   9572987.
  23. Hagins, W. A.; McGaughy, R. E. (August 18, 1967). "Molecular and thermal origins of fast photoelectric effects in the squid retina". Science. 157 (3790): 813–6. Bibcode:1967Sci...157..813H. doi:10.1126/science.157.3790.813. ISSN   0036-8075. PMID   17842786. S2CID   40374674.
  24. Penn, R.D.; Hagins, W.A. (August 1972). "Kinetics of the Photocurrent of Retinal Rods". Biophysical Journal. 12 (8): 1073–94. Bibcode:1972BpJ....12.1073P. doi:10.1016/S0006-3495(72)86145-9. ISSN   0006-3495. PMC   1484246 . PMID   5044581.
  25. Yoshikami, S.; Robinson, W. E.; Hagins, W. A. (September 27, 1974). "Topology of the outer segment membranes of retinal rods and cones revealed by a fluorescent probe". Science. 185 (4157): 1176–9. Bibcode:1974Sci...185.1176Y. doi:10.1126/science.185.4157.1176. ISSN   0036-8075. PMID   4138020. S2CID   19340959.
  26. Hagins, W. A.; Yoshikami, S. (December 30, 1975). "Ionic mechanisms in excitation of photoreceptors". Annals of the New York Academy of Sciences. 264 (1): 314–25. Bibcode:1975NYASA.264..314H. doi:10.1111/j.1749-6632.1975.tb31492.x. ISSN   0077-8923. PMID   769641. S2CID   7951969.
  27. Hagins, W. A.; Robinson, W. E.; Yoshikami, S. (1975). "Ionic Aspects of Excitation in Rod Outer Segments". Ciba Foundation Symposium 31 - Energy Transformation in Biological Systems. Novartis Foundation Symposia. Vol. 31. pp. 169–89. doi:10.1002/9780470720134.ch10. ISBN   9780470720134. ISSN   0300-5208. PMID   1080099.{{cite book}}: |journal= ignored (help)
  28. George, J. S.; Hagins, W. A. (May 26, 1983). "Control of Ca2+ in rod outer segment disks by light and cyclic GMP". Nature. 303 (5915): 344–8. Bibcode:1983Natur.303..344G. doi:10.1038/303344a0. ISSN   0028-0836. PMID   6304517. S2CID   4347636.
  29. Hagins, W. A.; Ross, P. D.; Tate, R. L.; Yoshikami, S. (February 1989). "Transduction heats in retinal rods: tests of the role of cGMP by pyroelectric calorimetry". Proceedings of the National Academy of Sciences of the United States of America. 86 (4): 1224–8. Bibcode:1989PNAS...86.1224H. doi: 10.1073/pnas.86.4.1224 . ISSN   0027-8424. PMC   286660 . PMID   2537492.