Can a Creation Model Explain the Origin of Mitochondria?

canacreationmodelexplaintheorigin

BY FAZALE RANA – NOVEMBER 23, 2016

Some called her a scientific heretic. Others were a bit more kind, describing her as a maverick.

Lynn Margulis (1938–2011) earned her reputation in the late 1960s when she proposed the endosymbiont hypothesis for the origin of eukaryotic cells. Because her ideas about evolution didn’t conform to Darwinian principles, evolutionary biologists summarily dismissed her idea out of hand and then went on to ignore her work for a couple of decades. She was ultimately vindicated, however, as the endosymbiont hypothesis gradually gained acceptance.

Today, Margulis’s proposal has become a cornerstone idea of the evolutionary paradigm and is taught in introductory high school and college biology courses. This classroom exposure explains why I am often asked about the endosymbiont hypothesis when I speak on university campuses. Many first-year biology students and professional life scientists alike find the evidence for this idea compelling, and consequently view it as providing broad support for an evolutionary explanation for the history and design of life.

Yet, new work by biochemists from Cambridge University make it possible to account for the origin of eukaryotic cells from a creation model perspective, providing a response to the endosymbiont hypothesis.1

The Endosymbiont Hypothesis

According to this hypothesis, complex cells originated when symbiotic relationships formed among single-celled microbes after free-living bacterial and/or archaeal cells were engulfed by a “host” microbe. (Ingested cells that take up permanent residence within other cells are referred to as endosymbionts.)

Accordingly, organelles, such as mitochondria, were once endosymbionts. Once taken inside the host cell, the endosymbionts presumably took up permanent residency within the host, with the endosymbionts growing and dividing inside the host. Over time, the endosymbionts and the host became mutually interdependent, with the endosymbionts providing a metabolic benefit for the host cell. The endosymbionts gradually evolved into organelles through a process referred to as genome reduction. This reduction resulted when genes from the endosymbionts’ genomes were transferred into the genome of the host organism. Eventually, the host cell evolved both the machinery to produce the proteins needed by the former endosymbiont and the processes needed to transport those proteins into the organelle’s interior.

Evidence for the Endosymbiont Hypothesis

The main line of evidence for the endosymbiont hypothesis is the similarity between organelles and bacteria. For example, mitochondria—which are believed to be descended from a group of α-proteobacteria—are about the same size and shape as a typical bacterium and have a double membrane structure like gram-negative cells. These organelles also divide in a way that is reminiscent of bacterial cells.

There is also biochemical evidence for the endosymbiont hypothesis. Evolutionary biologists view the existence of the diminutive mitochondrial genome as a vestige of this organelle’s evolutionary history. Additionally, the biochemical similarities between mitochondrial and bacterial genomes are taken as further evidence for the evolutionary origin of these organelles.

The presence of the unique lipid called cardiolipin in the mitochondrial inner membrane also serves as evidence for the endosymbiont hypothesis. Cardiolipin is an important lipid component of bacterial inner membranes, yet it is not found in the membranes of eukaryotic cells—except for the inner membranes of mitochondria. In fact, biochemists consider it a signature lipid for mitochondria and a vestige of this organelle’s evolutionary history.

A Creation Model Perspective on Mitochondria

So, as a creationist, how do I make sense of the evidence for the endosymbiont hypothesis?

Instead of focusing my efforts on refuting the endosymbiont hypothesis, here, I take a different approach. I maintain that it is reasonable to view eukaryotic cells as the work of a Creator, with the shared similarities between mitochondria and bacteria reflecting common design rather than common descent.

However, to legitimately interpret mitochondrial origins from a creation model perspective, there must be a reason for the biochemical similarities between mitochondria and bacteria. Previously, I wrote about discoveries that provide a rationale for why mitochondria have their own genomes. (See “Resources.”) Thanks to recent research advances, an explanation now exists for why the mitochondrial inner membranes harbor cardiolipin.

Cardiolipin’s Function

Previous studies identified close associations between cardiolipin and a number of proteins found in the mitochondrial inner membrane. These proteins play a role in harvesting energy for the cell to use. Compared to other lipid components found in the inner membrane, cardiolipin appears to preferentially associate with these proteins. Evidence indicates that cardiolipin helps to stabilize the structures of these proteins and serves to organize the proteins into larger functional complexes within the membrane.2 In fact, several studies have implicated defects in cardiolipin metabolism in the onset of a number of neuromuscular disorders.

The work of the Cambridge University investigators adds to this insight. These researchers were using computer simulations to model the interactions between cardiolipin and a protein complex called F1-F0 ATPase. Embedded within the inner membrane of mitochondria, this complex is a biomolecular rotary motor that produces the compound ATP—an energy storage material the cell’s machinery uses to power its operations.

Like other proteins found in the inner membrane, cardiolipin forms a close association with F1-F0 ATPase. However, instead of permanently binding to the surface of the protein complex, cardiolipin dynamically interacts with this membrane-embedded protein complex. The researchers think that this dynamic association and the unusual chemical structure of cardiolipin (which gives it the flexibility to interact with a protein surface) are critical for its role within the mitochondrial inner membrane. As it turns out, cardiolipin not only stabilizes the F1-F0 ATPase complex (as it does for other inner membrane proteins), but it also lubricates the protein’s rotor, allowing it to turn in the viscous cell membrane environment. Also, its unique structure helps move protons through the F1-F0 ATPase motor, providing the electrical power to operate this biochemical motor.

The bottom line: There is an exquisite biochemical rationale for why cardiolipin is found in mitochondrial inner membranes (and bacterial membranes). In light of this new insight, it is reasonable to view the shared similarities between these organelles and bacteria as reflecting common design—the product of the Creator’s handiwork. Like most biological systems, this organelle appears to be designed for a purpose.

Resources
Why Do Mitochondria Have DNA?” by Fazale Rana (article)
Mitochondrial Genomes: Evidence for Evolution or Creation?” by Fazale Rana (article)
Complex Protein Biogenesis Hints at Intelligent Design” by Fazale Rana (article)
Archetype or Ancestor? Sir Richard Owen and the Case for Design” by Fazale Rana (article)
Nanodevices Make Megascopic Statement” by Fazale Rana (article)

Endnotes

  1. Anna Duncan, Alan Robinson, and John Walker, “Cardiolipin Binds Selectively but Transiently to Conserved Lysine Residues in the Rotor of Metazoan ATP Synthases,” Proceedings of the National Academy of Sciences USA 113 (August 2016): 8687–92, doi:10.1073/pnas.1608396113.
  2. Giuseppe Paradies et al., “Functional Role of Cardiolipin in Mitochondrial Bioenergetics,” Biochimica et Biophysica Acta—Bioenergetics 1837 (April 2014): 408–17, doi:10.1016/j.bbabio.2013.10.006.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2016/11/23/can-a-creation-model-explain-the-origin-of-mitochondria

Science News Flash: Chimps Use Tools to Fish for Algae

chimpsfish

BY FAZALE RANA – NOVEMBER 16, 2016

Some of my fondest memories as a little kid are the summer afternoons I spent with my grandfather fishing in the Missouri River, near Mandan, North Dakota.

I don’t remember catching many fish, but that didn’t matter. I enjoyed spending time with my grandpa. I’m sure the experience was a bit trying for him though. If I detected even the slightest movement, I would reel in my line, hoping there would be a fish on the end. Inevitably, my excitement would give way to disappointment when I discovered that all I had caught was a clump of algae. And, of course, grandpa would have to clean up the mess I created and then recast my line.

But my response to reeling in an algae clump would have been different if I was a chimpanzee—if the field observations of primatologists from Germany are to be believed. Instead of disappointment, I would have been excited by my green, slimy, catch. As it turns out, chimpanzees will eat algae. It can be a valuable food source for them, rich in protein, carbohydrates, and minerals.

The German primatologists recently generated headlines when they published a report in the American Journal of Primatology describing 15 months of field work in the Bakoun Classified Forest of Guinea.1 Using camera footage from 11 different sites, the research team observed both male and female chimpanzees of every age using sticks (ranging from 6 inches to 12 feet in length) to “fish” algae out of rivers, streams, and ponds during the dry season.

The chimpanzees’ fishing efforts could last for up to an hour, with the average duration being around nine minutes. The chimps typically collected around a tenth of a pound of algae for each fishing expedition.

Evolutionary anthropologists point to these types of observations as shedding important light on the evolution of human behavior. They maintain that the use of tools by chimpanzees is an antecedent to the advanced behaviors displayed by modern humans.

However, I take a different view, maintaining that these types of discoveries actually undermine the standard models of human evolution. How so? These insights place chimpanzee behavior closer to hominid behavior (inferred from the fossil record). The temptation is to see hominid tool use as transitional, a way station on the path to modern human behavior. Yet the newly recognized behavior of chimpanzees distances the hominids from modern humans. Just because hominids such as habilines and erectines made tools and engaged in other remarkable behaviors doesn’t mean that they were becoming human. Instead, their behavior appears to be increasingly animal-like, particularly in light of the newly discovered chimp activities.

Resources
Who Was Adam? by Fazale Rana with Hugh Ross (book)
Chimpanzee Behavior Supports RTB’s Model for Humanity’s Origin” by Fazale Rana (article)
Chimpanzees’ Sleeping Habits Closer to Hominid Behavior than to Humans‘” by Fazale Rana (article)
Chimpanzees Respond to Death like Humans: Evidence for Evolution or Creation? Part 1 (of 2)” by Fazale Rana (article)
Chimpanzees Respond to Death like Humans: Evidence for Evolution or Creation? Part 2 (of 2)” by Fazale Rana (article)

Endnotes

  1. Christophe Boesch et al,. “Chimpanzees Routinely Fish for Algae with Tools during the Dry Season in Bakoun, Guinea,” American Journal of Primatology, published electronically November 3, 2016, doi:10.1002/ajp.22613.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2016/11/16/science-news-flash-chimps-use-tools-to-fish-for-algae

The Logic of DNA Replication Makes a Case for Intelligent Design

thelogicofdnareplicationmakesacase

BY FAZALE RANA – NOVEMBER 9, 2016

Why do I think God exists?

In short: The elegance, sophistication, and ingenuity of biochemical systems—and their astonishing similarity to man-made systems—convinces me that God is responsible for life’s origin and design.

While many skeptics readily acknowledge the remarkable designs of biochemical systems, they would disagree with my conclusion about God’s existence. Why? Because for every biochemical system I point to that displays beauty and elegance, they can point to one that seems to be poorly designed. In their view, these substandard designs reflect life’s evolutionary origin. They argue that evolutionary mechanisms kludged together the cell’s chemical systems through a historically contingent process that co-opted preexisting systems, cobbling them together to form new biochemical systems.

According to skeptics, one doesn’t have to look hard to find biochemical systems that seem to have been put together in a haphazard manner, and DNA replication appears to be an example of this. In many respects, DNA replication lies at the heart of the cell’s chemical operations. If designed by a Creator, this biochemical system, above all others, should epitomize intelligent design. Yet the DNA replication process appears to be unwieldy, inefficient, and unduly complex—the type of system evolution would generate by force, not the type of system worthy to be designated the product of the Creator’s handiwork.

Yet new work by Japanese researchers helps explain why DNA replication is the way it is.1Instead of reflecting the cumbersome product of an unguided evolutionary history, the DNA replication process displays an exquisite molecular logic.

To appreciate the significance of the Japanese study and its implication for the creation/evolution controversy, a short biochemistry primer is in order. For readers who are familiar with DNA’s structure and the DNA replication process, you can skip the next two sections.

DNA

DNA consists of chain-like molecules known as polynucleotides. Two polynucleotide chains align in an antiparallel fashion to form a DNA molecule. (The two strands are arranged parallel to one another with the starting point of one strand in the polynucleotide duplex located next to the ending point of the other strand and vice versa.) The paired polynucleotide chains twist around each other to form the well-known DNA double helix. The cell’s machinery forms polynucleotide chains by linking together four different subunit molecules called nucleotides. The nucleotides used to build DNA chains are adenosine, guanosine, cytidine, and thymidine, famously abbreviated A, G, C, and T, respectively.

The nucleotide molecules that make up the strands of DNA are, in turn, complex molecules consisting of both a phosphate moiety, and a nucleobase (either adenine, guanine, cytosine, or thymine) joined to a 5-carbon sugar (deoxyribose).

replication-makes-case-for-intelligent-design-1

Image 1: Adenosine Monophosphate, a Nucleotide

Repeatedly linking the phosphate group of one nucleotide to the deoxyribose unit of another nucleotide forms the backbone of the DNA strand. The nucleobases extend as side chains from the backbone of the DNA molecule and serve as interaction points when the two DNA strands align and twist to form the double helix.
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Image 2: The DNA Backbone

When the two DNA strands align, the adenosine (A) side chains of one strand always pair with thymidine (T) side chains from the other strand. Likewise, the guanosine (G) side chains from one DNA strand always pair with cytidine (C) side chains from the other strand.

DNA Replication

Biochemists refer to DNA replication as a template-directed, semi-conservative process. By template-directed, biochemists mean that the nucleotide sequences of the “parent” DNA molecule function as a template, directing the assembly of the DNA strands of the two “daughter” molecules. By semi-conservative, biochemists mean that after replication, each daughter DNA molecule contains one newly formed DNA strand and one strand from the parent molecule.

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Image 3: Semi-Conservative DNA Replication

Conceptually, template-directed, semi-conservative DNA replication entails the separation of the parent DNA double-helix into two single strands. By using the base-pairing rules, each strand serves as a template for the cell’s machinery to use when it forms a new DNA strand with a nucleotide sequence complementary to the parent strand. Because each strand of the parent DNA molecule directs the production of a new DNA strand, two daughter molecules result. Each one possesses an original strand from the parent molecule and a newly formed DNA strand produced by a template-directed synthetic process.

DNA replication begins at specific sites along the DNA double helix, called replication origins. The DNA double helix unwinds locally at the origin of replication to produce what biochemists call a replication bubble. The bubble expands in both directions from the origin during the course of DNA replication. Once the individual strands of the DNA double helix unwind and are exposed within the replication bubble, they are available to direct the production of the daughter strand. The site where the DNA double helix continuously unwinds is called the replication fork. Because DNA replication proceeds in both directions away from the origin, there are two replication forks within each bubble.

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Image 4: DNA Replication

DNA replication can only proceed in a single direction, from the top of the DNA strand to the bottom. Because the strands that form the DNA double helix align in an antiparallel fashion with the top of one strand juxtaposed to the bottom of the other strand, only one strand at each replication fork has the proper orientation (bottom-to-top) to direct the assembly of a new strand, in the top-to-bottom direction. For this strand—referred to as the “leading strand”—DNA replication proceeds rapidly and continuously in the direction of the advancing replication fork.

DNA replication can’t proceed along the strand with the top-to-bottom orientation until the replication bubble has expanded enough to expose a sizable stretch of DNA. When this happens, DNA replication moves away from the advancing replication fork. DNA replication can only proceed a short distance for the top-to-bottom oriented strand before the replication process has to stop and wait for more of the parent DNA strand to be exposed. When a sufficient length of the parent DNA template is exposed for a second time, DNA replication can proceed again, but only briefly before it has to stop again and wait for more DNA to be exposed. The process of discontinuous DNA replication takes place repeatedly until the entire strand is replicated. Each time DNA replication starts and stops, a small fragment of DNA is produced. Biochemists refer to these pieces of DNA (that will eventually comprise the daughter strand) as “Okazaki fragments,” named after the biochemist who discovered them. Biochemists call the strand produced discontinuously the “lagging strand,”because DNA replication for this strand lags behind the more rapidly produced leading strand.

One additional point: The leading strand at one replication fork is the lagging strand at the other replication fork, since the replication forks at the two ends of the replication bubble advance in opposite directions.

Before the newly formed daughter strands can be produced, a small RNA primer must be produced. The protein that synthesizes new DNA by reading the parent DNA template strand—DNA polymerase—can’t start production from scratch. It has to be primed. A massive protein complex, called the primosome, which consists of more than 15 different proteins, produces the RNA primer needed by DNA polymerase.

Once primed, DNA polymerase will continuously produce DNA along the leading strand. However, for the lagging strand, DNA polymerase can only generate DNA in spurts to produce Okazaki fragments. Each time DNA polymerase generates an Okazaki fragment, the primosome complex must produce a new RNA primer.

Once DNA replication is completed, the RNA primers are removed from the continuous DNA of the leading strand and the Okazaki fragments that make up the lagging strand. A protein called a 3’–5’ exonuclease removes the RNA primers. A different DNA polymerase fills in the gaps created by the removal of the RNA primers. Finally, a protein called a ligase connects all the Okazaki fragments together to form a continuous piece of DNA out of the lagging strand.

DNA Replication and the Case for Evolution

This cursory description of DNA replication clearly illustrates the complexity of this biochemical operation. (Many details of the process were left out of the discussion.) This description also reveals why biochemists view this process as cumbersome and unwieldy. There is no obvious reason why DNA replication proceeds as a semi-conservative, RNA primer-dependent, unidirectional process involving leading and lagging strands to produce DNA daughter molecules. Because of this uncertainty, skeptics view DNA replication as a chance outcome of a historically contingent process, kludged together from the biochemical leftovers of the RNA world.

If there is one feature of DNA replication that is responsible for the complexity of the process, it is the directionality of DNA replication—from top to bottom. At first glance, it would seem as if the process would be simpler and more elegant if replication could proceed in both directions. Skeptics argue that the fact that it doesn’t reflects the evolutionary origin of the replication process.

Yet work by the team from Sapporo, Japan indicates that there is an exquisite molecular rationale for the directionality of DNA replication.

Why DNA Replication Proceeds in a Single Direction

These researchers recognized an important opportunity to ask why DNA replication proceeds only in a single direction with the discovery of a class of enzymes that add nucleotides to the ends of transfer RNA (tRNA) molecules. (tRNA molecules ferry amino acids to the ribsosome during protein synthesis.) If damaged, tRNA molecules cannot properly carry out their role in protein production. Fortunately, there are repair enzymes that can fix damaged tRNA molecules. One of them is called Thg-1-like protein (TLP).

TLP adds nucleotides to damaged ends of tRNA molecules. But instead of adding the nucleotides top to bottom, the enzyme adds these subunit molecules to the tRNA bottom to top, the opposite direction of DNA replication.

By determining the mechanism employed by TLP during bottom-to-top nucleotide addition, the researchers gained important insight into the constraints of DNA replication. As it turns out, bottom-to-top addition is a much more complex process than the normal top-to-bottom nucleotide addition. Bottom-to-top addition is a cumbersome two-step process that requires an enzyme with two active sites that have to be linked together in a precise way. In contrast, top-to-bottom addition is a simple, one-step reaction that proceeds with a single active site. In other words, DNA replication proceeds in a single direction (top-to-bottom) because it is mechanistically simpler and more efficient.

One could argue that the complexity that arises by the top-to-bottom DNA replication process is a trade-off for a mechanistically simpler nucleotide addition reaction. Still, if DNA replication proceeded in both directions the process would be complex and unwieldy. For example, if replication proceeded in two directions, the cell would require two distinct types of primosomes and DNA polymerases, one set for each direction of DNA replication. Employing two sets of primosomes and DNA polymerases is clearly less efficient than employing a single set of enzymes.

Ironically, if DNA replication could proceed in two directions, there still would be a leading and a lagging strand. Why? Because bottom-to-top replication is a two-step process and would proceed more slowly than the single step of top-to-bottom replication. In other words, the assembly of the DNA strand in a bottom-to-top direction would lag behind the assembly of the DNA strand that traveled in a top-to-bottom direction.

Bidirectional DNA replication would also cause another complication due to a crowding effect. Once the replication bubble opens, both sets of replication enzymes would have to fit into the replication bubble’s constrained space. This molecular overcrowding would further compromise the efficiency of the replication process. Overcrowding is not an issue for unidirectional DNA replication that proceeds in a top-to-bottom direction.

The bottom line: In light of this new insight, it is hard to argue that DNA replication has been cobbled together via a historically contingent pathway. Instead, it is looking more and more like a process ingenuously designed by a Divine Mind.

Resources
The Cell’s Design: How Chemistry Reveals the Creator’s Artistry by Fazale Rana (book)
DNA Soaks Up Sun’s Rays” by Fazale Rana (article)
DNA: Designed for Flexibility” by Fazale Rana (article)
How the Central Dogma of Molecular Biology Points to Design” by Fazale Rana (article)
Why I Believe God Exists: Evidences from a Biochemist” by Fazale Rana (video)

Endnotes
  1. Shoko Kimura et al., “Template-Dependent Nucleotide Addition in the Reverse (3’–5’) Direction by Thg1-like Protein,” Science Advances 2 (March 2016): e1501397, doi:10.1126/sciadv.1501397.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2016/11/09/the-logic-of-dna-replication-makes-a-case-for-intelligent-design

Can New Medical Technology Boldly Go Where No Man Has Gone Before?

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BY FAZALE RANA – NOVEMBER 2, 2016

When I was in junior high, I would rush home every day after school to tune in to the afternoon reruns of Star Trek.

Fascinated by the technology possessed by the crew of the Enterprise, I often imagined what it would be like if I had their high-tech devices.

I was particularly intrigued by the tricorder Spock used to collect readings when the team beamed down to a planet’s surface. As a professional biochemist, I really came to appreciate the powerful technology Spock had at his fingertips. Gaining even cursory insight into a biochemical sample can take weeks of hard work in the lab. But for Spock, pointing the tricorder in the direction of the alien life-form was all he had to do. Of course, Spock didn’t get to have all the fun.

Dr. McCoy had a tricorder too. His instrument could be used to diagnose sick and injured crew members by simply passing a wand over the patients. Wouldn’t it be great if physicians could diagnosis our ailments so quickly and easily? No more trips to the doctor’s office. No more late-night excursions to the emergency room.

Well, science fiction is about to become science fact, thanks to work by engineers from Washington University. These researchers developed a smart phone app that can measure hemoglobin concentration in a patient’s blood after the patient presses his/her finger against the phone’s camera.1

This new technology represents an important advance in medical screening, allowing physicians to quickly test for anemia. This blood disorder is rampant in the developing world, caused by malnutrition and parasite infections.

Measuring the blood’s oxygen-carrying capacity is key for diagnosing anemia. Detecting and monitoring anemia can be difficult in a third-world context, because the most reliable method for determining the oxygen-carrying capacity of blood involves drawing blood and counting red blood cells. This procedure: (1) exposes medical workers to the patient’s blood; (2) runs the risk of being unsanitary, introducing the risk of infection; and (3) requires access to a laboratory to count the red blood cells.

Noninvasive methods exist, but they require expensive medical instruments.

These limitations motivated the University of Washington team to develop the smart phone app to measure hemoglobin content in blood. This technology is relatively inexpensive, mobile, and can yield rapid results—ideal for screening for anemia in the field.

HemaApp

The University of Washington team dubbed their app: HemaApp. The app makes use of an algorithm that converts video images of the patient’s finger into a series of oscillating curves corresponding to different wavelengths of light. The form of these curves is influenced by the absorption of light by hemoglobin in the blood (which causes blood’s red color). The more hemoglobin, the greater the blood’s light absorption at certain wavelengths of light.

In a pilot study (involving men and women, patients of all ages, and several ethnicities), the researchers showed that HemaApp performed as well as the leading noninvasive blood monitoring technologies, paving the way to use this technology in the field.

These researchers think that their accomplishments are the first step toward broader usage of smart phones for medical screening. It is conceivable that the technology can be adapted to screen for sickle-cell anemia, which is caused by mutations to the gene encoding hemoglobin. These mutations lead to hemoglobin with a distorted structure, which alters its light absorption spectrum.

This technology will also be a benefit to people living in the first world. Patients with anemia can monitor the hemoglobin level of their blood at home, providing them with a tool to more effectively manage their health issues. Because the hemoglobin measurements are made with a smart phone, the data can be easily sent to the patient’s physician.

HemaApp isn’t quite as impressive as a medical tricorder, but it sure is a big step in that direction.

Yet, as promising as the biomedical implications are for this advance, the bioethical implications are even more exciting.

Biomedical Technology, Bioethics, and Social Justice

Many Christians are vigilant about the ethical implications associated with biomedical advances, raising concerns when technologies undermine the sanctity of human life.

Yet, a neglected area of bioethics relates to the accessibility of medical care and emerging biomedical technologies. Many diagnostic tools and medical procedures require highly specialized equipment and highly trained personnel. These requirements sometimes render even the most basic medical care so costly that only a relatively small percentage of the world’s population has access to life-saving biomedical technologies.

In my view, the inequitable distribution of medical care should be considered as much a pro-life issue as the destruction of human embryos associated with many emerging biotechnologies or euthanasia. Like all Christians, I hold the view that all human life has immeasurable value—inherent worth and dignity—because all human beings are made in God’s image. If so, then it is reasonable to think that all human beings have fundamental human rights. And, in my view, that includes equal access to basic medical care. And ideally, beyond that, all human beings should be able to equally benefit from biomedical advances.

The use of smartphones as a medical screening tool moves us one step closer to realizing this ideal. HemaApp stands as a powerful new biomedical technology, but it is affordable and portable. These features make it possible for the wealthiest and poorest people on the planet to benefit from this advance. In fact, this technology could be transformative for some of the poorest parts of the world by helping medical workers quickly identify and treat those people suffering from anemia.

The University of Washington researchers bring us one step closer to the dream of a young teenager who loved to watch Star Trek. They are also making it possible to envision how, as human beings, we can boldly go where no one has gone before—to a world where biotechnology provides treatments and therapies for many horrible diseases and injuries andalso makes basic medical care accessible to the world’s poor.

Resources

Embryonic Stem Cell Research: An Interview with Dr. Fazale ‘Fuz’ Rana” (article)
Q&A: Is a New in vitro Fertilization Method Ethical?” by Fazale Rana (article)
GNINOLC: We Have It All Backwards” by Fazale Rana (article)
Advance Holds Potential to Resolve Cloning’s Ethical Challenges” by Fazale Rana (article)

Endnotes

  1. Edward Jay Wang et al., “HemaApp: Noninvasive Blood Screening of Hemoglobin Using Smartphone Cameras,” Proceedings of the 2016 ACM International Joint Conference on Pervasive and Ubiquitous Computing (September 2016): 593–604, doi:10.1145/2971648.2971653.
Reprinted with permission by the author
Original article at:
https://www.reasons.org/explore/blogs/the-cells-design/read/the-cells-design/2016/11/02/can-new-medical-technology-boldly-go-where-no-man-has-gone-before